|
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: 635.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 44 ITEAQRFSHLPKRSAVDIEfVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGM 123
Cdd:TIGR00955 1 LTYSWRNSDVFGRVAQDGS-WKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 124 KGQ--ILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTA 199
Cdd:TIGR00955 80 KGSgsVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVREHLMFQAHLRMPRRvtKKEKRERVDEVLQALGLRKCANTRIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 200 L------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYI 273
Cdd:TIGR00955 160 VpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIIL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 274 LSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGEYGDLNPMlfRAVQNGLCAmAEKKSSPEKNEVPAPCPP 353
Cdd:TIGR00955 240 MAEGRVAYLGSPDQAVPFFSDLGHPCPENYNPADFYVQVLAVIPGSENES--RERIEKICD-SFAVSDIGRDMLVNTNLW 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 354 CPPEVDPI------ESHTFATSTLTQFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCL 427
Cdd:TIGR00955 317 SGKAGGLVkdsenmEGIGYNASWWTQFYALLKRSWLSVLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGAL 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 428 FFSMLFLMFAALMPTVLTFPLEMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFS 507
Cdd:TIGR00955 397 FLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRVSAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFL 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 508 ALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG-ME 586
Cdd:TIGR00955 477 FLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIPFLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSdVD 556
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 587 RGDLTC--LEERCPFrEPQSILRALDVEDAKLYMDFLVLGIFFLALRLLAYLVLRYRVKSER 646
Cdd:TIGR00955 557 NIECTSanTTGPCPS-SGEVILETLSFRNADLYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
58-283 |
9.10e-93 |
|
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: 284.83 E-value: 9.10e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 58 AVDIEFVELSYSVREgpcWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES-GMKGQILVNGRPREL 136
Cdd:cd03213 1 GVTLSFRNLTVTVKS---SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlGVSGEVLINGRPLDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 137 RTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELV 216
Cdd:cd03213 78 RSFRKIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------GL-----------SGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 217 NNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
82-644 |
6.82e-82 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 271.75 E-value: 6.82e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFRKMScYIMQDDMLLPHLTVLE 160
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGrIQGNNFTGTILANNRKPTKQILKRTG-FVTQDDILYPHLTVRE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKL--SEKQEVKKELVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PLN03211 160 TLVFCSLLRLpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 234 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVA 313
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNPADFLLDLA 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 314 SGeYGDLNPMLFRA---VQNGLCAMAEKKSSPEKNEVPAPCPPCPPEVDPIESHTFA----------TSTLTQFCILFKR 380
Cdd:PLN03211 320 NG-VCQTDGVSEREkpnVKQSLVASYNTLLAPKVKAAIEMSHFPQANARFVGSASTKehrssdrisiSTWFNQFSILLQR 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 381 TfLSILRDTVLTHLRFMSHVVIGVLIGLLYLHigDDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLNY 460
Cdd:PLN03211 399 S-LKERKHESFNTLRVFQVIAAALLAGLMWWH--SDFRDVQDRLGLLFFISIFWGVFPSFNSVFVFPQERAIFVKERASG 475
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 461 WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPV 540
Cdd:PLN03211 476 MYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLVLLGYVLVSQGLGLALGAAIMDAKKASTIVTV 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 541 TAIPVLLFSGFFVSfkTIPTYLQWSSYLSYVRYGFEGVILTIYGMERGDLTCLEERCPFREPQSILRALDVE---DAKLY 617
Cdd:PLN03211 556 TMLAFVLTGGFYVH--KLPSCMAWIKYISTTFYSYRLLINVQYGEGKRISSLLGCSLPHGSDRASCKFVEEDvagQISPA 633
|
570 580
....*....|....*....|....*..
gi 215820660 618 MDFLVLGIFFLALRLLAYLVLRyRVKS 644
Cdd:PLN03211 634 TSVSVLIFMFVGYRLLAYLALR-RIKH 659
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
78-584 |
2.87e-65 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 233.46 E-value: 2.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGM--KGQILVNGRPRElRTFRKMSCYIMQDDMLLPH 155
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVitGGDRLVNGRPLD-SSFQRSIGYVQQQDLHLPT 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMMVSANLKLSEK--QEVKKELVTEILTALGLMSCSHTRTAL----LSGGQRKRLAIALELVNNPP-VMFFDEPT 228
Cdd:TIGR00956 851 STVRESLRFSAYLRQPKSvsKSEKMEYVEEVIKLLEMESYADAVVGVpgegLNVEQRKRLTIGVELVAKPKlLLFLDEPT 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 229 SGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQG-QCIFKGVV----TNLIPYLKGLGLH-CPTY 302
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDRLLLLQKGgQTVYFGDLgensHTIINYFEKHGAPkCPED 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 303 HNPADFIIEVASGEYGD----------LNPMLFRAVQNGLCAM------AEKKSSPEKNevpapcppcppevdpiesHTF 366
Cdd:TIGR00956 1011 ANPAEWMLEVIGAAPGAhanqdyhevwRNSSEYQAVKNELDRLeaelskAEDDNDPDAL------------------SKY 1072
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 367 ATSTLTQFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFfsMLFLMFAALMPTVL-T 445
Cdd:TIGR00956 1073 AASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKVGTSLQGLQNQMFAVF--MATVLFNPLIQQYLpP 1150
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 446 F-PLEMAVFMREHLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTG-------QPAETSRFLLFSALATATALVA 517
Cdd:TIGR00956 1151 FvAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPVGfywnaskTGQVHERGVLFWLLSTMFFLYF 1230
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 518 QSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 584
Cdd:TIGR00956 1231 STLGQMVISFNPNADNAAVLASLLFTMCLSFCGVLAPPSRMPGFWIFMYRCSPFTYLVQALLSTGLA 1297
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
77-283 |
1.80e-60 |
|
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: 201.35 E-value: 1.80e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRPRELRTFRKMSCYIMQDDMLLP 154
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgtTSGQILFNGQPRKPDQFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 HLTVLEAMMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSsdaIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215820660 232 DSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
61-283 |
4.00e-54 |
|
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: 183.21 E-value: 4.00e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREgpcwrKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRElRTF 139
Cdd:cd03232 4 LTWKNLNYTVPV-----KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGvITGEILINGRPLD-KNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 140 RKMSCYIMQDDMLLPHLTVLEAMMVSANLKlsekqevkkelvteiltalGLmscshtrtallSGGQRKRLAIALELVNNP 219
Cdd:cd03232 78 QRSTGYVEQQDVHSPNLTVREALRFSALLR-------------------GL-----------SVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 220 PVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKG 283
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKRgGKTVYFG 192
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
84-584 |
6.80e-54 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 199.69 E-value: 6.80e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 84 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 162
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSekQEVKKE----LVTEILTALGLMSCSHTRTAL-----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PLN03140 975 IYSAFLRLP--KEVSKEekmmFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 234 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQ-GQCIFKGVV----TNLIPYLKGL-GL-HCPTYHNPA 306
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLgrnsHKIIEYFEAIpGVpKIKEKYNPA 1132
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 307 DFIIEVASgeygdlnpmLFRAVQNGLCAMAEKKSSP----EKNEVPAPCPPCPPEVDPIESHTFATSTLTQFCILFKRTF 382
Cdd:PLN03140 1133 TWMLEVSS---------LAAEVKLGIDFAEHYKSSSlyqrNKALVKELSTPPPGASDLYFATQYSQSTWGQFKSCLWKQW 1203
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 383 LSILRDTVLTHLRFMSHVVIGVLIGLLYLHIG---DDASKVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMREHLN 459
Cdd:PLN03140 1204 WTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGtkrSNANDLTMVIGAMYAAVLFVGINNCSTVQPMVAVERTVFYRERAA 1283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 460 YWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVAT-FVG 538
Cdd:PLN03140 1284 GMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFSFLYFTYYGMMTVSLTPNQQVAAiFAA 1363
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 215820660 539 PVTAIpVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVILTIYG 584
Cdd:PLN03140 1364 AFYGL-FNLFSGFFIPRPKIPKWWVWYYWICPVAWTVYGLIVSQYG 1408
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
77-579 |
2.58e-51 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 192.25 E-value: 2.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES---GMKGQILVNGRPRE--LRTFRKMSCYIMQDDM 151
Cdd:TIGR00956 69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfhiGVEGVITYDGITPEeiKKHYRGDVVYNAETDV 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 LLPHLTVLEAMMVSANLK-------LSEKQEVKKELVTEILTALGLmscSHTRTAL--------LSGGQRKRLAIALELV 216
Cdd:TIGR00956 149 HFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATYGL---SHTRNTKvgndfvrgVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 217 NNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGL 295
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANiLDTTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 296 GLHCPTYHNPADFIIEVAS-------GEYGDLNPM-------LFRAVQNGLCAMAEKKSSPEKNEVPAPCPPCPPEVDPI 361
Cdd:TIGR00956 306 GFKCPDRQTTADFLTSLTSpaerqikPGYEKKVPRtpqefetYWRNSPEYAQLMKEIDEYLDRCSESDTKEAYRESHVAK 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 362 ES-HTFATSTLT-----QFCILFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASKVFNNTGCLFFSMLFLM 435
Cdd:TIGR00956 386 QSkRTRPSSPYTvsfsmQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGALFFAILFNA 465
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 436 FAALMPTVLTFplEMAVFMREHLNY-WYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATA 514
Cdd:TIGR00956 466 FSSLLEIASMY--EARPIVEKHRKYaLYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGRFFFYLLILFICT 543
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 515 LVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 579
Cdd:TIGR00956 544 LAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLM 608
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
377-579 |
1.67e-48 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 168.61 E-value: 1.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 377 LFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLHIGDDASkVFNNTGCLFFSMLFLMFAALMPTVLTFPLEMAVFMRE 456
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQG-GLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 457 HLNYWYSLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATF 536
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 215820660 537 VGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGVI 579
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALR 202
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
62-278 |
3.76e-42 |
|
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: 151.47 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 62 EFVELSYSvregpcwRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRT 138
Cdd:cd03225 1 ELKNLSFS-------YPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGP-TSGEVLVDGKDltkLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 139 FRKMSCYIMQ--DDMLLpHLTVLEAMMVSA-NLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALEL 215
Cdd:cd03225 73 LRRKVGLVFQnpDDQFF-GPTVEEEVAFGLeNLGLPEEEIEER--VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215820660 216 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 278
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLD-LLLELADRVIVLEDGK 211
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
96-289 |
9.57e-42 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 151.37 E-value: 9.57e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK-LSE 172
Cdd:COG1131 27 EIFGLLGPNGAGKTTTIRMLLGLLRPT-SGEVRVLGEDvaRDPAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYgLPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 173 KQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 252
Cdd:COG1131 106 KE--ARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKT 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 215820660 253 IICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 289
Cdd:COG1131 184 VLLSTHYLEE-AERLCDRVAIIDKGRIVADGTPDELK 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
61-283 |
3.70e-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: 146.71 E-value: 3.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---REL 136
Cdd:COG1122 1 IELENLSFSYPGG--------TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGlLKPT--SGEVLVDGKDitkKNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 137 RTFRKMSCYIMQ--DDMLLpHLTVLEAMMVS-ANLKLSEKqEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIAL 213
Cdd:COG1122 71 RELRRKVGLVFQnpDDQLF-APTVEEDVAFGpENLGLPRE-EIR-ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDL-VAELADRVIVLDDGRIVADG 216
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
94-278 |
6.12e-40 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 6.12e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAgyresGM----KGQILVNGRP------RELRTFRKMSC-YIMQDDMLLPHLTVLEAM 162
Cdd:COG1136 33 AGEFVAIVGPSGSGKSTLLNILG-----GLdrptSGEVLIDGQDisslseRELARLRRRHIgFVFQFFNLLPELTALENV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:COG1136 108 ALPLLLA-GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLEL 186
|
170 180 190
....*....|....*....|....*....|....*..
gi 215820660 243 MKSLA-QGGRTIICTIHqpSAKLFEMFDKLYILSQGQ 278
Cdd:COG1136 187 LRELNrELGTTIVMVTH--DPELAARADRVIRLRDGR 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
96-278 |
6.51e-38 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 139.93 E-value: 6.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAMMVSAN 167
Cdd:cd03255 31 EFVAIVGPSGSGKSTLLNILGG-LDRPTSGEVRVDGTDisklseKELAAFRrrHIG-FVFQSFNLLPDLTALENVELPLL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:cd03255 109 LAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELN 187
|
170 180 190
....*....|....*....|....*....|..
gi 215820660 248 -QGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03255 188 kEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
78-280 |
4.83e-36 |
|
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: 134.94 E-value: 4.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPH 155
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTG-ELRPTSGTAYINGYSirTDRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMMVSANLK-LSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:cd03263 90 LTVREHLRFYARLKgLPKSEI--KEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 235 SCFQVVSLMKSLaQGGRTIICTIHqpSAKLFEMF-DKLYILSQGQ--CI 280
Cdd:cd03263 168 SRRAIWDLILEV-RKGRSIILTTH--SMDEAEALcDRIAIMSDGKlrCI 213
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
96-285 |
5.20e-36 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 135.37 E-value: 5.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 173
Cdd:COG4555 28 EITGLLGPNGAGKTTLLRMLAGLLKPD-SGSILIDGEDvrKEPREARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 QEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 253
Cdd:COG4555 107 EELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTV 185
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 254 ICTIHQPS--AKLfemFDKLYILSQGQCIFKGVV 285
Cdd:COG4555 186 LFSSHIMQevEAL---CDRVVILHKGKVVAQGSL 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
61-283 |
1.51e-35 |
|
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: 133.78 E-value: 1.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSvregpcwrkRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR----- 134
Cdd:cd03261 1 IELRGLTKS---------FGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGlLRPD--SGEVLIDGEDIsglse 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 135 -ELRTFRKMSCYIMQDDMLLPHLTVLE--AMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAI 211
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTVFEnvAFPLREHTRLSE--EEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 212 ALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL--AQGGRTIICTiHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLkkELGLTSIMVT-HDLDT-AFAIADRIAVLYDGKIVAEG 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
80-283 |
3.42e-34 |
|
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: 130.38 E-value: 3.42e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYREsGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLL 153
Cdd:cd03256 12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVE-PTSGSVLIDGtdinklKGKALRQLRRQIGMIFQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 PHLTVLEAMMV---------SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 224
Cdd:cd03256 91 ERLSVLENVLSgrlgrrstwRSLFGLFPKEE--KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 225 DEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDlAREY--ADRIVGLKDGRIVFDG 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
85-229 |
1.82e-33 |
|
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: 125.07 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVLEA 161
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAG-LLSPTEGTILLDGQDltdDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 162 MMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:pfam00005 80 LRLGLLLKGLSKREKDAR-AEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
78-578 |
3.70e-33 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 136.90 E-value: 3.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK--GQILVNGRprELRTF--RKMSCYIMQDDMLL 153
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKvsGEITYNGY--RLNEFvpRKTSAYISQNDVHV 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 PHLTVLEAMMVSAN--------------------------------LKLSEKQEVKKELVTE-ILTALGLMSCSHTRTAL 200
Cdd:PLN03140 252 GVMTVKETLDFSARcqgvgtrydllselarrekdagifpeaevdlfMKATAMEGVKSSLITDyTLKILGLDICKDTIVGD 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 -----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAKLFEMFDKLYIL 274
Cdd:PLN03140 332 emirgISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHlTEATVLMSLLQPAPETFDLFDDIILL 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 275 SQGQCIFKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASGE-----YGDLN-PMLFRAV----------------QNGL 332
Cdd:PLN03140 412 SEGQIVYQGPRDHILEFFESCGFKCPERKGTADFLQEVTSKKdqeqyWADRNkPYRYISVsefaerfksfhvgmqlENEL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 333 CAMAEKKSSPEknevpapcppcppEVDPIESHTFATSTLTQFCilFKRTFLSILRDTVLTHLRFMSHVVIGVLIGLLYLH 412
Cdd:PLN03140 492 SVPFDKSQSHK-------------AALVFSKYSVPKMELLKAC--WDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLR 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 413 I-------GDDASKVfnntGCLFFSMLFLMFAALMPTVLTFPlEMAVFMRE-----HLNYWYSLKAYYLAktmadVPFQV 480
Cdd:PLN03140 557 TemhtrneEDGALYI----GALLFSMIINMFNGFAELALMIQ-RLPVFYKQrdllfHPPWTFTLPTFLLG-----IPISI 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 481 VCPVVYCSIVYWMTGQPAETSRFLLFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPT 560
Cdd:PLN03140 627 IESVVWVVITYYSIGFAPEASRFFKQLLLVFLIQQMAAGIFRLIASVCRTMIIANTGGALVLLLVFLLGGFILPKGEIPN 706
|
570
....*....|....*...
gi 215820660 561 YLQWSSYLSYVRYGFEGV 578
Cdd:PLN03140 707 WWEWAYWVSPLSYGFNAL 724
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
82-278 |
5.70e-33 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 124.43 E-value: 5.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVL 159
Cdd:cd03230 13 KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD-SGEIKVLGKDikKEPEEVKRRIGYLPEEPSLYENLTVR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 EammvsaNLKLSekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:cd03230 92 E------NLKLS-------------------------------GGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190
....*....|....*....|....*....|....*....
gi 215820660 240 VSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQ 278
Cdd:cd03230 135 WELLRELKKEGKTILLSSHILEE-AERLCDRVAILNNGR 172
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
76-278 |
2.48e-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: 123.07 E-value: 2.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 76 WRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDD 150
Cdd:cd03229 7 SKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGL-EEPDSGSILIDGEDltdleDELPPLRRRIGMVFQDF 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 151 MLLPHLTVLEammvsaNLklsekqevkkelvteiltALGLmscshtrtallSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:cd03229 86 ALFPHLTVLE------NI------------------ALGL-----------SGGQQQRVALARALAMDPDVLLLDEPTSA 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 231 LDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 278
Cdd:cd03229 131 LDPITRREVRALLKSLqAQLGITVVLVTHDL-DEAARLADRVVVLRDGK 178
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
77-278 |
3.77e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.39 E-value: 3.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRKMSCYIMQDdmll 153
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADL-DPPTSGEIYLDGKPLSampPPEWRRQVAYVPQE---- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 phlTVLEAMMVSANLKLS---EKQEVKKELVTEILTALGL-MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG4619 83 ---PALWGGTVRDNLPFPfqlRERKFDRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 215820660 230 GLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQ 278
Cdd:COG4619 160 ALDPENTRRVEELLREYlAEEGRAVLWVSHDP-EQIERVADRVLTLEAGR 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
97-283 |
7.24e-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: 7.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 97 LIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 174
Cdd:cd03264 27 MYGLLGPNGAGKTTLMRILATLTPPS-SGTIRIDGQDvlKQPQKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 175 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 254
Cdd:cd03264 106 EVKAR-VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVI 183
|
170 180
....*....|....*....|....*....
gi 215820660 255 CTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03264 184 LSTHIVE-DVESLCNQVAVLNKGKLVFEG 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
79-260 |
1.75e-31 |
|
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: 121.43 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELR--TFRKMSCYIMQDDMLLPHL 156
Cdd:COG4133 12 RGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPP-SAGEVLWNGEPIRDAreDYRRRLAYLGHADGLKPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLKlseKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 236
Cdd:COG4133 91 TVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGV 167
|
170 180
....*....|....*....|....
gi 215820660 237 FQVVSLMKSLAQGGRTIICTIHQP 260
Cdd:COG4133 168 ALLAELIAAHLARGGAVLLTTHQP 191
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
82-284 |
4.33e-31 |
|
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: 121.64 E-value: 4.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPH 155
Cdd:TIGR02315 15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS-SGSILLEGtditklRGKKLRKLRRRIGMIFQHYNLIER 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMMVSA-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 228
Cdd:TIGR02315 94 LTVLENVLHGRlgykptwRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILADEPI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 229 SGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFEmfDKLYILSQGQCIFKGV 284
Cdd:TIGR02315 174 ASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDlAKKYA--DRIVGLKAGEIVFDGA 229
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
79-258 |
4.88e-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: 120.44 E-value: 4.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPRELRTFRKMSCYIMQD-DMLLPHL 156
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGlIKES--SGSILLNGKPIKAKERRKSIGYVMQDvDYQLFTD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLkLSEKQEVkkelVTEILTALGL--MSCSHTRTalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:cd03226 88 SVREELLLGLKE-LDAGNEQ----AETVLKDLDLyaLKERHPLS--LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180
....*....|....*....|....
gi 215820660 235 SCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:cd03226 161 NMERVGELIRELAAQGKAVIVITH 184
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
77-283 |
6.19e-31 |
|
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: 120.06 E-value: 6.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRES--GMKGQILVNGRP--RELRTFRKMSCYIMQDDML 152
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvSVEGDIHYNGIPykEFAEKYPGEIIYVSEEDVH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 153 LPHLTVLEAMMVSANLKLSEKqeVKKelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03233 95 FPTLTVRETLDFALRCKGNEF--VRG----------------------ISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215820660 233 SASCFQVVSLMKSLAQG-GRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03233 151 SSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
94-258 |
6.85e-31 |
|
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: 120.21 E-value: 6.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP------RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 167
Cdd:cd03292 26 AGEFVFLVGPSGAGKSTLLKLIYK-EELPTSGTIRVNGQDvsdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYENVAFALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:cd03292 105 VTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKIN 183
|
170
....*....|.
gi 215820660 248 QGGRTIICTIH 258
Cdd:cd03292 184 KAGTTVVVATH 194
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
96-288 |
2.42e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 119.78 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMV----- 164
Cdd:COG3638 30 EFVALIGPSGAGKSTLLRCLNG-LVEPTSGEILVDGqdvtalRGRALRRLRRRIGMIFQQFNLVPRLSVLTNVLAgrlgr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 ----SANLKLSEKQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:COG3638 109 tstwRSLLGLFPPED--RERALEALERVGLADKAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVM 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 215820660 241 SLMKSLAQ-GGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKGVVTNL 288
Cdd:COG3638 187 DLLRRIAReDGITVVVNLHQVDlARRY--ADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
94-283 |
2.61e-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: 119.08 E-value: 2.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------PREL------RTFRKMScyimqddmLLPHLTVLE 160
Cdd:cd03219 25 PGEIHGLIGPNGAGKTTLFNLISGfLRPT--SGSVLFDGEditglpPHEIarlgigRTFQIPR--------LFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKLSE---------KQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:cd03219 95 NVMVAAQARTGSglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215820660 232 DSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEG 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
75-278 |
2.82e-30 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 116.58 E-value: 2.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 75 CWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRKMSCYIMQddm 151
Cdd:cd00267 5 LSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT-SGEILIDGKDiakLPLEELRRRIGYVPQ--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 llphltvleammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 232 DSASCFQVVSLMKSLAQGGRTIICTIHQPS-AKLFemFDKLYILSQGQ 278
Cdd:cd00267 112 DPASRERLLELLRELAEEGRTVIIVTHDPElAELA--ADRVIVLKDGK 157
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
96-259 |
1.48e-29 |
|
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: 116.48 E-value: 1.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNG-----RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSAN 167
Cdd:cd03262 27 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTIIIDGlkltdDKKNINELRQKVGMVFQQFNLFPHLTVLENITLAPI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 --LKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 245
Cdd:cd03262 103 kvKGMSKAEAEERAL--ELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGEVLDVMKD 180
|
170
....*....|....
gi 215820660 246 LAQGGRTIICTIHQ 259
Cdd:cd03262 181 LAEEGMTMVVVTHE 194
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
82-286 |
1.62e-29 |
|
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: 117.45 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP------RELRtfRKMScYIMQDDMLLPH 155
Cdd:COG1120 14 RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS-SGEVLLDGRDlaslsrRELA--RRIA-YVPQEPPAPFG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMM------VSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG1120 90 LTVRELVAlgryphLGLFGRPSAEDR---EAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215820660 230 GLDSASCFQVVSLMKSLAQG-GRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG----VVT 286
Cdd:COG1120 167 HLDLAHQLEVLELLRRLARErGRTVVMVLHDLNlAARY--ADRLVLLKDGRIVAQGppeeVLT 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
80-279 |
4.30e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 115.96 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRtfRKMSCYIMQD---DMLLPhL 156
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPP-TSGTVRLFGKPPRRA--RRRIGYVPQRaevDWDFP-I 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:COG1121 93 TVRDVVLmgrygrRGLFRRPSRAD---REAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 231 LDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQC 279
Cdd:COG1121 170 VDAATEEALYELLRELRREGKTILVVTHDLGA-VREYFDRVLLLNRGLV 217
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
92-283 |
2.72e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 112.59 E-value: 2.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 92 FCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMM 163
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGF-ETPQSGRVLINGVdvtaapPAD----RPVS-MLFQENNLFAHLTVEQnvGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 243
Cdd:cd03298 95 LSPGLKLTAED---RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 244 KSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
94-287 |
2.79e-28 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 112.95 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPreLRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSE 172
Cdd:cd03293 29 EGEFVALVGPSGCGKSTLLRIIAGlERPTS--GEVLVDGEP--VTGPGPDRGYVFQQDALLPWLTVLDNVALGLELQGVP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 173 KQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV-VSLMKSLAQGGR 251
Cdd:cd03293 105 KAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALTREQLqEELLDIWRETGK 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 215820660 252 TIICTIHQPSAKLFeMFDKLYILSQGQCIFKGVVTN 287
Cdd:cd03293 184 TVLLVTHDIDEAVF-LADRVVVLSARPGRIVAEVEV 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
82-283 |
4.87e-28 |
|
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: 112.77 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFR-KMScYIMQDDMLLP 154
Cdd:COG1127 18 RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRP-DSGEILVDGQditglsEKELYELRrRIG-MLFQGGALFD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 HLTVLE--AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG1127 96 SLTVFEnvAFPLREHTDLSEAE--IRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEPTAGLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 215820660 233 SASCFQVVSLMKSL--AQGGRTIICTiHQ-PSAklFEMFDKLYILSQGQCIFKG 283
Cdd:COG1127 174 PITSAVIDELIRELrdELGLTSVVVT-HDlDSA--FAIADRVAVLADGKIIAEG 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
78-283 |
7.63e-28 |
|
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: 110.22 E-value: 7.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMqddmLLPhlT 157
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS-SGEILLDGKDLASLSPKELARKIA----YVP--Q 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 VLEAMMVSAnlkLSEKQevkkelVTEiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:cd03214 81 ALELLGLAH---LADRP------FNE-----------------LSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 238 QVVSLMKSLA-QGGRTIICTIHQPS-AKLFemFDKLYILSQGQCIFKG 283
Cdd:cd03214 135 ELLELLRRLArERGKTVVMVLHDLNlAARY--ADRVILLKDGRIVAQG 180
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
61-278 |
1.40e-27 |
|
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: 109.39 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-REL--R 137
Cdd:cd03228 1 IEFKNVSFSYPGRP-------KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT-SGEILIDGVDlRDLdlE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 138 TFRKMSCYIMQDDMLLpHLTVLEammvsaNLklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVN 217
Cdd:cd03228 73 SLRKNIAYVPQDPFLF-SGTIRE------NI--------------------------------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 218 NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAK-GKTVIVIAHRLS--TIRDADRIIVLDDGR 171
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
53-289 |
1.90e-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: 117.17 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 53 LPKRSAVDIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR 132
Cdd:COG4988 329 LPAAGPPSIELEDVSFSYPGG--------RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP-YSGSILINGV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 133 P-REL--RTFRKMSCYIMQDDMLlPHLTVLEammvsaNLKLSE----KQEVKKEL----VTEILTAL--GLmscsHTRT- 198
Cdd:COG4988 400 DlSDLdpASWRRQIAWVPQNPYL-FAGTIRE------NLRLGRpdasDEELEAALeaagLDEFVAALpdGL----DTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 199 ---ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTiHQPSakLFEMFDKLYILS 275
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRLA--LLAQADRILVLD 545
|
250
....*....|....
gi 215820660 276 QGQCIFKGVVTNLI 289
Cdd:COG4988 546 DGRIVEQGTHEELL 559
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
46-278 |
3.94e-27 |
|
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: 116.86 E-value: 3.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 46 EAQRFSHLPKRSAvDIEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmK 124
Cdd:COG2274 460 EGRSKLSLPRLKG-DIELENVSFRYPGDS-------PPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGlYEPT--S 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 125 GQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSeKQEVKKELVTEILTALGLMS--CSH---- 195
Cdd:COG2274 530 GRILIDGIDLrqiDPASLRRQIGVVLQDVFLF-SGTIRE------NITLG-DPDATDEEIIEAARLAGLHDfiEALpmgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 196 -----TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSakLFEMFDK 270
Cdd:COG2274 602 dtvvgEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLS--TIRLADR 678
|
....*...
gi 215820660 271 LYILSQGQ 278
Cdd:COG2274 679 IIVLDKGR 686
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
85-258 |
6.52e-27 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 107.89 E-value: 6.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTV 158
Cdd:TIGR01166 8 LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRP-QSGAVLIDGEPldysrKGLLERRQRVGLVFQDpDDQLFAADV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 159 LEAMMVSA-NLKLSEkQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:TIGR01166 87 DQDVAFGPlNLGLSE-AEVE-RRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|.
gi 215820660 238 QVVSLMKSLAQGGRTIICTIH 258
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTH 185
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
94-280 |
1.06e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 108.75 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTFRKMSCYIMQDDM--LLPHLTV----LEA 161
Cdd:cd03257 30 KGETLGLVGESGSGKSTLARAILGL-LKPTSGSIIFDGKDllklsrRLRKIRRKEIQMVFQDPMssLNPRMTIgeqiAEP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MMVsanLKLSEKQEVKKELVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03257 109 LRI---HGKLSKKEARKEAVLLLLVGVGL-----PEEVLnrypheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSV 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 236 CFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCI 280
Cdd:cd03257 181 QAQILDLLKKLQEElGLTLLFITHDLGV-VAKIADRVAVMYAGKIV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
96-278 |
1.16e-26 |
|
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: 107.99 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTFrkmsCYIMQDDMLLPHLTVLEAMMVSANLKL 170
Cdd:cd03259 27 EFLALLGPSGCGKTTLLRLIAGL-ERPDSGEILIDGRdvtgvPPERRNI----GMVFQDYALFPHLTVAENIAFGLKLRG 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQG 249
Cdd:cd03259 102 VPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELREELKELqREL 180
|
170 180 190
....*....|....*....|....*....|
gi 215820660 250 GRTIICTIHQPS-AklFEMFDKLYILSQGQ 278
Cdd:cd03259 181 GITTIYVTHDQEeA--LALADRIAVMNEGR 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
94-254 |
1.24e-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: 114.23 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP------RELRTFRKMSCYIMQD--DMLLPHLTVLEAMMV 164
Cdd:COG1123 290 RGETLGLVGESGSGKSTLARLLLGlLRPTS--GSILFDGKDltklsrRSLRELRRRVQMVFQDpySSLNPRMTVGDIIAE 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 SA-NLKLSEKQEVKkELVTEILTALGLM-SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:COG1123 368 PLrLHGLLSRAERR-ERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNL 446
|
170
....*....|...
gi 215820660 243 MKSL-AQGGRTII 254
Cdd:COG1123 447 LRDLqRELGLTYL 459
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
100-258 |
1.32e-26 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 108.22 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRE---LRtfRKMScYIMQDDMLLPHLTVLEammvsaNLK 169
Cdd:COG2884 33 LTGPSGAGKSTLLKLLYGeERPT--SGQVLVNGqdlsrlKRREipyLR--RRIG-VVFQDFRLLPDRTVYE------NVA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LS------EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 243
Cdd:COG2884 102 LPlrvtgkSRKEIRRR-VREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIMELL 180
|
170
....*....|....*
gi 215820660 244 KSLAQGGRTIICTIH 258
Cdd:COG2884 181 EEINRRGTTVLIATH 195
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
80-259 |
1.56e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 108.64 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFM---NILagyrESGMKGQILV-----NGRPRELRTFRKMSCYIMQDDM 151
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLrciNKL----EEITSGDLIVdglkvNDPKVDERLIRQEAGMVFQQFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 LLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:PRK09493 88 LFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSAL 167
|
170 180
....*....|....*....|....*...
gi 215820660 232 DSASCFQVVSLMKSLAQGGRTIICTIHQ 259
Cdd:PRK09493 168 DPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
94-283 |
1.66e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 108.97 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PREL------RTFrkmscyimQDDMLLPHLTVLE 160
Cdd:COG0411 29 RGEIVGLIGPNGAGKTTLFNLITGfYRPTS--GRILFDGRditglpPHRIarlgiaRTF--------QNPRLFPELTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSA-------------NLKLSEKQEVK-KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:COG0411 99 NVLVAAharlgrgllaallRLPRARREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 227 PTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG0411 179 PAAGLNPEETEELAELIRRLRDErGITILLIEHDMDL-VMGLADRIVVLDFGRVIAEG 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
96-260 |
2.43e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLE--AMMVSAN 167
Cdd:COG3840 26 ERVAILGPSGAGKSTLLNLIAGFLPP-DSGRILWNGQdltalpPAE----RPVS-MLFQENNLFPHLTVAQniGLGLRPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:COG3840 100 LKLTAEQ---RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELC 176
|
170
....*....|....
gi 215820660 248 QG-GRTIICTIHQP 260
Cdd:COG3840 177 RErGLTVLMVTHDP 190
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
54-232 |
6.19e-26 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.48 E-value: 6.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 54 PKRSAVDIEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP 133
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-------VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGL-EKPTSGEVLVDGKP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 RElRTFRKMScYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEvKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLA 210
Cdd:COG1116 75 VT-GPGPDRG-VVFQEPALLPWLTVLDNVALGLELRGVPKAE-RRERARELLELVGL---AGFEDAYphqLSGGMRQRVA 148
|
170 180
....*....|....*....|..
gi 215820660 211 IALELVNNPPVMFFDEPTSGLD 232
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALD 170
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
82-277 |
9.46e-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: 105.31 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG----YResgmkGQILVNGRPreLRTFRKMSCYIMQD---DMLLP 154
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGllkpTS-----GSIRVFGKP--LEKERKRIGYVPQRrsiDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 hLTVLEAMM------VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 228
Cdd:cd03235 85 -ISVRDVVLmglyghKGLFRRLSKAD---KAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 229 SGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQG 277
Cdd:cd03235 161 AGVDPKTQEDIYELLRELRREGMTILVVTHDLGL-VLEYFDRVLLLNRT 208
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
96-289 |
1.11e-25 |
|
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: 105.74 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 169
Cdd:cd03258 32 EIFGIIGRSGAGKSTLIRCINGL-ERPTSGSVLVDGTdltllsGKELRKARRRIGMIFQHFNLLSSRTVFENVALPLEIA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:cd03258 111 GVPKAEIEER-VLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRE 189
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 250 -GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVVTNLI 289
Cdd:cd03258 190 lGLTIVLITHEMEV-VKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
80-283 |
1.41e-25 |
|
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: 104.61 E-value: 1.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR--PRELRTFRKMSCyIMQDDMLLPHL 156
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGlIKPDS--GEITFDGKsyQKNIEALRRIGA-LIEAPGFYPNL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 236
Cdd:cd03268 88 TARENLRLLARLLGIRKKRID-----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDGI 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 215820660 237 FQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03268 163 KELRELILSLRDQGITVLISSHLLS-EIQKVADRIGIINKGKLIEEG 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
69-278 |
1.48e-25 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 106.04 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 69 SVREGPCWRKRgykTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMSCY 145
Cdd:COG1124 8 SVSYGQGGRRV---PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGL-ERPWSGEVTFDGRPvtrRRRKAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 146 IMQDDM--LLPHLTVLEAmmVSANLKLSEKQEVKKElVTEILTALGLmscshTRTAL------LSGGQRKRLAIALELVN 217
Cdd:COG1124 84 VFQDPYasLHPRHTVDRI--LAEPLRIHGLPDREER-IAELLEQVGL-----PPSFLdryphqLSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 218 NPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPSAKLFeMFDKLYILSQGQ 278
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAH-LCDRVAVMQNGR 216
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
96-283 |
1.84e-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: 104.68 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------------PRElrtfRKMScYIMQDDMLLPHLTVLEAMM 163
Cdd:cd03297 24 EVTGIFGASGAGKSTLLRCIAGL-EKPDGGTIVLNGTvlfdsrkkinlpPQQ----RKIG-LVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSANLKlseKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 243
Cdd:cd03297 98 FGLKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 215820660 244 KSLAQ--GGRTIICTiHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03297 175 KQIKKnlNIPVIFVT-HDLS-EAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
61-283 |
8.11e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----R 134
Cdd:PRK13639 2 LETRDLKYSYPDG--------TEALKGINFKAEKGEMVALLGPNGAGKSTlFLHFNGILKPT--SGEVLIKGEPikydkK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 135 ELRTFRKMSCYIMQ--DDMLL-PhlTVLEAMMVSA-NLKLSeKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLA 210
Cdd:PRK13639 72 SLLEVRKTVGIVFQnpDDQLFaP--TVEEDVAFGPlNLGLS-KEEVEKR-VKEALKAVGMEGFENKPPHHLSGGQKKRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 211 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQpsAKLFEMF-DKLYILSQGQCIFKG 283
Cdd:PRK13639 148 IAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHD--VDLVPVYaDKVYVMSDGKIIKEG 219
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
81-278 |
1.25e-24 |
|
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: 102.25 E-value: 1.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 81 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPR-ELRTFRKMSCYIMQDDMLLPHLTVL 159
Cdd:TIGR01277 10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEP-ASGSIKVNDQSHtGLAPYQRPVSMLFQENNLFAHLTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 E--AMMVSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:TIGR01277 89 QniGLGLHPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 215820660 238 QVVSLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQ 278
Cdd:TIGR01277 166 EMLALVKQLCsERQRTLLMVTHHLS-DARAIASQIAVVSQGK 206
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
94-288 |
2.07e-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: 101.68 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKl 170
Cdd:cd03265 25 RGEIFGLLGPNGAGKTTTIKMLTTLlKPTS--GRATVAGHDvvREPREVRRRIGIVFQDLSVDDELTGWENLYIHARLY- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQG 249
Cdd:cd03265 102 GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLkEEF 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 215820660 250 GRTIICTIH-QPSAKlfEMFDKLYILSQGQCIFKGVVTNL 288
Cdd:cd03265 182 GMTILLTTHyMEEAE--QLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
96-267 |
3.03e-24 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 101.99 E-value: 3.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGRP-----RELRTFRKMSCYIMQDDMLLPHLTVLE----AMM 163
Cdd:COG1126 28 EVVVIIGPSGSGKSTLlrcINLL----EEPDSGTITVDGEDltdskKDINKLRRKVGMVFQQFNLFPHLTVLEnvtlAPI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 243
Cdd:COG1126 104 KV--KKMS-KAEAE-ERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVM 179
|
170 180
....*....|....*....|....
gi 215820660 244 KSLAQGGRTIICTIHqpsaklfEM 267
Cdd:COG1126 180 RDLAKEGMTMVVVTH-------EM 196
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
96-232 |
5.25e-24 |
|
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: 101.16 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQ 174
Cdd:cd03300 27 EFFTLLGPSGCGKTTLLRLIAGF-ETPTSGEILLDGKDiTNLPPHKRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKA 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 175 EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03300 106 EIKER-VAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
96-283 |
6.03e-24 |
|
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: 100.36 E-value: 6.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG------RPRELRtfRKMScYIMQDdmllPHL---TVLEammvsa 166
Cdd:cd03245 31 EKVAIIGRVGSGKSTLLKLLAGLYKP-TSGSVLLDGtdirqlDPADLR--RNIG-YVPQD----VTLfygTLRD------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSeKQEVKKELVTEILTALGLMSCSHT-----------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03245 97 NITLG-APLADDERILRAAELAGVTDFVNKhpngldlqigeRGRGLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 236 CFQVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03245 176 EERLKERLRQLL-GDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
57-283 |
6.50e-24 |
|
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: 106.39 E-value: 6.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 57 SAVDIEFVELSYSVREGPCWrkrgyktLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RE 135
Cdd:COG4987 330 GGPSLELEDVSFRYPGAGRP-------VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDP-QSGSITLGGVDlRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 136 LR--TFRKMSCYIMQDdmllPHL---TVLEammvsaNLKLSeKQEVKKELVTEILTALGL--MSCS-----HTRT----A 199
Cdd:COG4987 402 LDedDLRRRIAVVPQR----PHLfdtTLRE------NLRLA-RPDATDEELWAALERVGLgdWLAAlpdglDTWLgeggR 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 200 LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQC 279
Cdd:COG4987 471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAG--LERMDRILVLEDGRI 547
|
....
gi 215820660 280 IFKG 283
Cdd:COG4987 548 VEQG 551
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
61-283 |
7.42e-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: 7.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGY--RESGMKGQILVNGR-----P 133
Cdd:COG1123 5 LEVRDLSVRYPGGD-------VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlpHGGRISGEVLLDGRdllelS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 RELRtfRKMSCYIMQDDM--LLPhLTVLEAMM-VSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLA 210
Cdd:COG1123 78 EALR--GRRIGMVFQDPMtqLNP-VTVGDQIAeALENLGLSRAE--ARARVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 211 IALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1123 153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDG 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
96-260 |
1.64e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 105.58 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNIL-------AG-YRESGMKGQILVNGRPRELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSAN 167
Cdd:PRK10535 35 EMVAIVGASGSGKSTLMNILgcldkptSGtYRVAGQDVATLDADALAQLR--REHFGFIFQRYHLLSHLTAAQNVEVPAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:PRK10535 113 YAGLERKQ-RLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLR 191
|
170
....*....|...
gi 215820660 248 QGGRTIICTIHQP 260
Cdd:PRK10535 192 DRGHTVIIVTHDP 204
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
77-283 |
1.75e-23 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 98.89 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKR-GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMScYIMQDDMLLPH 155
Cdd:cd03269 7 TKRfGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD-SGEVLFDGKPLDIAARNRIG-YLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03269 85 MKVIDQLVYLAQLKGLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 236 CFQVVSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03269 164 VELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
96-277 |
5.82e-23 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 98.28 E-value: 5.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILV-----------NGRPRELRTFRKMSCYIMQDDMLLPHLTVLEA 161
Cdd:PRK11264 30 EVVAIIGPSGSGKTTLlrcINLL----EQPEAGTIRVgditidtarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 241
Cdd:PRK11264 106 IIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 242 LMKSLAQGGRTIICTIHQPS-----AKLFEMFDKLYILSQG 277
Cdd:PRK11264 186 TIRQLAQEKRTMVIVTHEMSfardvADRAIFMDQGRIVEQG 226
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
94-283 |
6.52e-23 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 97.50 E-value: 6.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLK 169
Cdd:cd03224 25 EGEIVALLGRNGAGKTTLLKTIMGLLPP-RSGSIRFDGRDiTGLPPHERARagiGYVPEGRRIFPELTVEENLLLGAYAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:cd03224 104 RRAKRKARLERVYELFPRLKERR--KQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE 181
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 250 GRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03224 182 GVTIL-LVEQNARFALEIADRAYVLERGRVVLEG 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
85-259 |
6.71e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 98.16 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGkfcrrELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDML 152
Cdd:COG4161 23 LECPSG-----ETLVLLGPSGAGKSSLlrvLNLL----ETPDSGQLNIAGHqfdfsqkpsEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 153 LPHLTVLEAMmVSAN---LKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG4161 94 WPHLTVMENL-IEAPckvLGLSKEQAREK--AMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTA 170
|
170 180 190
....*....|....*....|....*....|
gi 215820660 230 GLDSASCFQVVSLMKSLAQGGRTIICTIHQ 259
Cdd:COG4161 171 ALDPEITAQVVEIIRELSQTGITQVIVTHE 200
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
85-244 |
1.71e-22 |
|
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: 96.64 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR-----PRELRTFrkmsCYIMQDDMLLPHLTVL 159
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD-SGKILLNGKditnlPPEKRDI----SYVPQNYALFPHMTVY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 EAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:cd03299 90 KNIAYGLKKRKVDKKEIERK-VLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
....*
gi 215820660 240 VSLMK 244
Cdd:cd03299 169 REELK 173
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
54-261 |
1.83e-22 |
|
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: 96.35 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 54 PKRSAVDIEFVELSYSVREGPCwrkrgykTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP 133
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGEL-------TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGL-DRPTSGTVRLAGQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 ------RELRTFRKMSC-YIMQDDMLLPHLTVLEAMMVSANLKlSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQR 206
Cdd:COG4181 76 lfaldeDARARLRARHVgFVFQSFQLLPTLTALENVMLPLELA-GRRD--ARARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 215820660 207 KRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIHQPS 261
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
76-278 |
3.86e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 95.01 E-value: 3.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 76 WRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQD 149
Cdd:cd03301 7 TKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGL-EEPTSGRIYIGGRdvtdlpPKD----RDIA-MVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 150 DMLLPHLTVLEAMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:cd03301 81 YALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215820660 230 GLDSASCFQVVSLMKSLAQG-GRTIICTIH-QPSAklFEMFDKLYILSQGQ 278
Cdd:cd03301 160 NLDAKLRVQMRAELKRLQQRlGTTTIYVTHdQVEA--MTMADRIAVMNDGQ 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
60-283 |
9.77e-22 |
|
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: 94.21 E-value: 9.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 60 DIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---REL 136
Cdd:cd03254 2 EIEFENVNFSYDEK--------KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDP-QKGQILIDGIDirdISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 137 RTFRKMSCYIMQDDMLLPHlTVLEammvsaNLKLSeKQEVKKELVTEILTALGL----MSCSH-------TRTALLSGGQ 205
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSG-TIME------NIRLG-RPNATDEEVIEAAKEAGAhdfiMKLPNgydtvlgENGGNLSQGE 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 206 RKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPSAKLFEmfDKLYILSQGQCIFKG 283
Cdd:cd03254 145 RQLLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEG 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
96-283 |
1.13e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 95.08 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGY----RESGMKGQILVN-----GR-PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVS 165
Cdd:PRK09984 31 EMVALLGPSGSGKSTLLRHLSGLitgdKSAGSHIELLGRtvqreGRlARDIRKSRANTGYIFQQFNLVNRLSVLENVLIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 166 A-------NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 238
Cdd:PRK09984 111 AlgstpfwRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 239 VVSLMKSLAQG-GRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK09984 191 VMDTLRDINQNdGITVVVTLHQVDYAL-RYCERIVALRQGHVFYDG 235
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
96-278 |
1.27e-21 |
|
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: 92.28 E-value: 1.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAmmvsanlklse 172
Cdd:cd03246 29 ESLAIIGPSGSGKSTLARLILGLLRPT-SGRVRLDGADISqwdPNELGDHVGYLPQDDELFSG-SIAEN----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 173 kqevkkelvteiltalglmscshtrtaLLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 252
Cdd:cd03246 96 ---------------------------ILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGAT 148
|
170 180
....*....|....*....|....*.
gi 215820660 253 IICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03246 149 RIVIAHRPE--TLASADRILVLEDGR 172
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
14-261 |
1.54e-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: 98.51 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 14 GPGAVAMAVTLEDGAEPPVLtthlkkvenhiteaqrfSHLPKRSAVD--IEFVELSYsvregpcwRKRGYKTLLKCLSGK 91
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPRPLA-----------------GKAPVTAAPAssLEFSGVSV--------AYPGRRPALRPVSFT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 92 FCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQddmlLPHLTvleAMMVSANL 168
Cdd:TIGR02857 345 VPPGERVALVGPSGAGKSTLLNLLLGFVDPT-EGSIAVNGVPLadaDADSWRDQIAWVPQ----HPFLF---AGTIAENI 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKqEVKKELVTEILTALGLMSCS-------HT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:TIGR02857 417 RLARP-DASDAEIREALERAGLDEFVaalpqglDTpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEA 495
|
250 260
....*....|....*....|....
gi 215820660 238 QVVSLMKSLAQgGRTIICTIHQPS 261
Cdd:TIGR02857 496 EVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
96-232 |
1.68e-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: 96.32 E-value: 1.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN-- 167
Cdd:COG3842 32 EFVALLGPSGCGKTTLLRMIAGF-ETPDSGRILLDGRdvtglpPEK----RNVG-MVFQDYALFPHLTVAE------Nva 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 168 --LKLS--EKQEVkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG3842 100 fgLRMRgvPKAEI-RARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDEPLSALD 167
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
96-234 |
1.84e-21 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 93.49 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG----------RPRELrtfrkmscyIMQDDMLLPHLTVLE--AMM 163
Cdd:PRK10771 26 ERVAILGPSGAGKSTLLNLIAGFLTPA-SGSLTLNGqdhtttppsrRPVSM---------LFQENNLFSHLTVAQniGLG 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 164 VSANLKLSEKQevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSA 234
Cdd:PRK10771 96 LNPGLKLNAAQ---REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
79-260 |
2.08e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 2.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTV 158
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPP-AAGTIKLDGGDIDDPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 159 LEAMMVSANLKLSEKQEVkkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 238
Cdd:PRK13539 91 AENLEFWAAFLGGEELDI-----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|...
gi 215820660 239 VVSLMKS-LAQGGRTIICTiHQP 260
Cdd:PRK13539 166 FAELIRAhLAQGGIVIAAT-HIP 187
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
85-259 |
2.36e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 93.54 E-value: 2.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGkfcrrELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR---------PRELRTFRKMSCYIMQDDMLLPH 155
Cdd:PRK11124 23 LDCPQG-----ETLVLLGPSGAGKSSLLRVL-NLLEMPRSGTLNIAGNhfdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLE-----AMMVsanLKLSEKQEVKKELvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:PRK11124 97 LTVQQnlieaPCRV---LGLSKDQALARAE--KLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171
|
170 180
....*....|....*....|....*....
gi 215820660 231 LDSASCFQVVSLMKSLAQGGRTIICTIHQ 259
Cdd:PRK11124 172 LDPEITAQIVSIIRELAETGITQVIVTHE 200
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
19-289 |
2.58e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 95.67 E-value: 2.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 19 AMAVTLEDGAEPPVLTTHLKKVENHITEAQRfshlpKRSAVDIEFVELSYSVregpcwrkrGYKTLLKCLSGKFCRRELI 98
Cdd:PRK13536 5 AVAEEAPRRLELSPIERKHQGISEAKASIPG-----SMSTVAIDLAGVSKSY---------GDKAVVNGLSFTVASGECF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEV 176
Cdd:PRK13536 71 GLLGPNGAGKSTIARMILGMTSPD-AGKITVLGVpvPARARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 177 KkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICT 256
Cdd:PRK13536 150 E-AVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLT 228
|
250 260 270
....*....|....*....|....*....|....*
gi 215820660 257 IH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 289
Cdd:PRK13536 229 THfmEEAERL---CDRLCVLEAGRKIAEGRPHALI 260
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
96-233 |
2.65e-21 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 95.60 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-------PRElrtfRKMScYIMQDDMLLPHLTVLEammvsaN- 167
Cdd:COG1118 29 ELVALLGPSGSGKTTLLRIIAGL-ETPDSGRIVLNGRdlftnlpPRE----RRVG-FVFQHYALFPHMTVAE------Ni 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 168 ------LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG1118 97 afglrvRPPSKAE--IRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDA 166
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
94-288 |
3.14e-21 |
|
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: 94.76 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGY-RESGmkGQILVNG-----RPRELR-----TFRKMSCYimqDDmllphLTVLEAM 162
Cdd:TIGR01188 18 EGEVFGFLGPNGAGKTTTIRMLTTLlRPTS--GTARVAGydvvrEPRKVRrsigiVPQYASVD---ED-----LTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLK-LSEKqeVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 241
Cdd:TIGR01188 88 EMMGRLYgLPKD--EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 215820660 242 LMKSLAQGGRTIICTIHQpsakLFE---MFDKLYILSQGQCIFKGVVTNL 288
Cdd:TIGR01188 166 YIRALKEEGVTILLTTHY----MEEadkLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
78-283 |
4.55e-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: 92.84 E-value: 4.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPR------ELRTfrkmscYI----- 146
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLFGERRggedvwELRK------RIglvsp 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 147 -MQDDmLLPHLTVLEaMMVSA-------NLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNN 218
Cdd:COG1119 86 aLQLR-FPRDETVLD-VVLSGffdsiglYREPTDEQR---ERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215820660 219 PPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1119 161 PELLILDEPTAGLDLGARELLLALLDKLAAeGAPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAG 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
79-258 |
5.76e-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: 91.86 E-value: 5.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGMK----GQILVNGR--------PRELRTFRKMscyI 146
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGapdeGEVLLDGKdiydldvdVLELRRRVGM---V 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 147 MQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFF 224
Cdd:cd03260 87 FQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRLHAlgLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 225 DEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH 258
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAELKK-EYTIVIVTH 198
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
79-234 |
5.91e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESG--MKGQILVNGRP-RELRTFRKMSCYIMQDDMLLPH 155
Cdd:COG4136 11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsASGEVLLNGRRlTALPAEQRRIGILFQDDLLFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLE--AMMVSANLKLSEKqevkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG4136 91 LSVGEnlAFALPPTIGRAQR----RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
.
gi 215820660 234 A 234
Cdd:COG4136 167 A 167
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
76-283 |
6.43e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.15 E-value: 6.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 76 WRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKST-FMNILAGYRESgmKGQILVNGRP-----RELRTFRKMSCYIMQD 149
Cdd:PRK13638 8 WFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTlFMNLSGLLRPQ--KGAVLWQGKPldyskRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 150 -DMLLPHLTVLEAMMVS-ANLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK13638 86 pEQQIFYTDIDSDIAFSlRNLGVPEAEITRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 215820660 228 TSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDL-IYEISDAVYVLRQGQILTHG 218
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
96-289 |
6.84e-21 |
|
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: 91.84 E-value: 6.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTfRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 170
Cdd:cd03218 27 EIVGLLGPNGAGKTTTFYMIVGL-VKPDSGKILLDGQditklPMHKRA-RLGIGYLPQEASIFRKLTVEENILAVLEIRG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKELVtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 250
Cdd:cd03218 105 LSKKEREEKLE-ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQKIIKILKDRG 183
|
170 180 190
....*....|....*....|....*....|....*....
gi 215820660 251 RTIICTIHQPSAKLfEMFDKLYILSQGQCIFKGVVTNLI 289
Cdd:cd03218 184 IGVLITDHNVRETL-SITDRAYIIYEGKVLAEGTPEEIA 221
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
77-259 |
8.44e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 92.34 E-value: 8.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKR-GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGR----------------PRELRTF 139
Cdd:PRK10619 12 HKRyGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSEGSIVVNGQtinlvrdkdgqlkvadKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 140 RKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNN 218
Cdd:PRK10619 91 RTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAME 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 219 PPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQ 259
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
84-256 |
1.09e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.42 E-value: 1.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 84 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfRKMScYIMQDDMLLP 154
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGL-DTPTSGDVIFNGQPmsklssaakAELRN-QKLG-FIYQFHHLLP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 HLTVLE--AM-MVSANLKLSEKQEVKKELvteiLTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:PRK11629 101 DFTALEnvAMpLLIGKKKPAEINSRALEM----LAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180
....*....|....*....|....*..
gi 215820660 232 DSASCFQVVSLMKSL--AQGGRTIICT 256
Cdd:PRK11629 177 DARNADSIFQLLGELnrLQGTAFLVVT 203
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
96-289 |
1.33e-20 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 93.60 E-value: 1.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRK---MscyIMQDDMLLPHLTVLEamm 163
Cdd:COG1135 32 EIFGIIGYSGAGKSTLircINLL----ERPTSGSVLVDGVdltalsERELRAARRkigM---IFQHFNLLSSRTVAE--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 vsaN----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:COG1135 102 ---NvalpLEIAgvPKAEIRKR-VAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTR 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 238 QVVSLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTNLI 289
Cdd:COG1135 178 SILDLLKDInRELGLTIVLITH-------EMdvvrriCDRVAVLENGRIVEQGPVLDVF 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
96-258 |
1.43e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 91.79 E-value: 1.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR----------------PRELRTFRKMSCYIMQDDMLLPHL 156
Cdd:COG4598 35 DVISIIGSSGSGKSTFlrcINLL----ETPDSGEIRVGGEeirlkpdrdgelvpadRRQLQRIRTRLGMVFQSFNLWSHM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMM-----VsanLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:COG4598 111 TVLENVIeapvhV---LGRP-KAEAI-ERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSAL 185
|
170 180
....*....|....*....|....*..
gi 215820660 232 DSASCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:COG4598 186 DPELVGEVLKVMRDLAEEGRTMLVVTH 212
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
79-260 |
2.38e-20 |
|
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: 89.47 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMSC-YIMQDDMLLPHL 156
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPP-LAGRVLLNGGPlDFQRDSIARGLlYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLKLSEKqevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 236
Cdd:cd03231 89 SVLENLRFWHADHSDEQ-------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|....
gi 215820660 237 FQVVSLMKSLAQGGRTIICTIHQP 260
Cdd:cd03231 162 ARFAEAMAGHCARGGMVVLTTHQD 185
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
79-260 |
6.07e-20 |
|
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: 88.18 E-value: 6.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPR-ELRTFRKMSC-YIMQDDMLLPHL 156
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRP-DSGEVRWNGTPLaEQRDEPHENIlYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 236
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIE-----DALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|....*
gi 215820660 237 FQVVSLMKS-LAQGGRTIICTiHQP 260
Cdd:TIGR01189 164 ALLAGLLRAhLARGGIVLLTT-HQD 187
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
60-248 |
7.75e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 93.23 E-value: 7.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 60 DIEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTfmNILAGYRESGMKGQILVNGRPRELRTF 139
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST--TGLALLRLINSQGEIWFDGQPLHNLNR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 140 RKMSCY------IMQD--DMLLPHLTVLEamMVSANLKLSEKQ---EVKKELVTEILTALGLMSCSHTR-TALLSGGQRK 207
Cdd:PRK15134 355 RQLLPVrhriqvVFQDpnSSLNPRLNVLQ--IIEEGLRVHQPTlsaAQREQQVIAVMEEVGLDPETRHRyPAEFSGGQRQ 432
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 208 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 248
Cdd:PRK15134 433 RIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
96-232 |
9.25e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 91.29 E-value: 9.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR------PRElrtfRKMScyiM--QDDMLLPHLTVLEammvsa 166
Cdd:COG3839 30 EFLVLLGPSGCGKSTLLRMIAGlEDPTS--GEILIGGRdvtdlpPKD----RNIA---MvfQSYALYPHMTVYE------ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 167 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG3839 95 NiafpLKLRkvPKAEIDRR-VREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSNLD 165
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
94-283 |
3.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-----RELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA- 166
Cdd:PRK13636 31 KGEVTAILGGNGAGKSTLFQNLNGILKP-SSGRILFDGKPidysrKGLMKLRESVGMVFQDpDNQLFSASVYQDVSFGAv 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSEKqEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 246
Cdd:PRK13636 110 NLKLPED-EVRKR-VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEM 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 215820660 247 AQG-GRTIICTIHQ-PSAKLFemFDKLYILSQGQCIFKG 283
Cdd:PRK13636 188 QKElGLTIIIATHDiDIVPLY--CDNVFVMKEGRVILQG 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
77-289 |
3.56e-19 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 88.71 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKR-GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR--PRELRTFRKMSCYIMQDDMLL 153
Cdd:PRK13537 14 EKRyGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP-DAGSISLCGEpvPSRARHARQRVGVVPQFDNLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 PHLTVLEAMMVSAN-LKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13537 93 PDFTVRENLLVFGRyFGLSAAA--ARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 233 SASCFQVVSLMKSLAQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGVVTNLI 289
Cdd:PRK13537 171 PQARHLMWERLRSLLARGKTILLTTHfmEEAERL---CDRLCVIEEGRKIAEGAPHALI 226
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
96-283 |
3.82e-19 |
|
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: 91.85 E-value: 3.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG------RPRELRtfRKMScYIMQDDMLLpHLTVLEammvsaNL 168
Cdd:TIGR03375 492 EKVAIIGRIGSGKSTLLKLLLGlYQPT--EGSVLLDGvdirqiDPADLR--RNIG-YVPQDPRLF-YGTLRD------NI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSeKQEVKKELVTEILTALGLMSC--SHT---------RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:TIGR03375 560 ALG-APYADDEEILRAAELAGVTEFvrRHPdgldmqigeRGRSLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEE 638
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 238 QVVSLMKSLAqGGRTIICTIHQPSakLFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR03375 639 RFKDRLKRWL-AGKTLVLVTHRTS--LLDLVDRIIVMDNGRIVADG 681
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
61-283 |
4.05e-19 |
|
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: 87.89 E-value: 4.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPCWRKRGyktlLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR------P 133
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKA----LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGlLKPT--SGTVTIDGRditakkK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 RELRTFRKMSCYIMQddmlLPH-----LTVLEAMM-VSANLKLSEKqEVKkELVTEILTALGL------MSCSHtrtalL 201
Cdd:TIGR04521 75 KKLKDLRKKVGLVFQ----FPEhqlfeETVYKDIAfGPKNLGLSEE-EAE-ERVKEALELVGLdeeyleRSPFE-----L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 202 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRTIICTIHQPSaKLFEMFDKLYILSQGQCI 280
Cdd:TIGR04521 144 SGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKeKGLTVILVTHSME-DVAEYADRVIVMHKGKIV 222
|
...
gi 215820660 281 FKG 283
Cdd:TIGR04521 223 LDG 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
77-278 |
8.62e-19 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 86.20 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRtfRKMScYIMQDD 150
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEP-TSGEIFIDGEdireqdPVELR--RKIG-YVIQQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 151 MLLPHLTVLEAmmVSANLKLSE-KQEVKKELVTEILTALGLMSCSHTR--TALLSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:cd03295 85 GLFPHMTVEEN--IALVPKLLKwPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALAADPPLLLMDEP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 228 TSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQpsakLFEMF---DKLYILSQGQ 278
Cdd:cd03295 163 FGALDPITRDQLQEEFKRLQQElGKTIVFVTHD----IDEAFrlaDRIAIMKNGE 213
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
85-283 |
9.16e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.05 E-value: 9.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRP------RELRTFRkmsCYIMQDDMLLPHLTV 158
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG--QGEILLNGRPlsdwsaAELARHR---AYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 159 LEAMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNPP--VMFFDEPTSGL 231
Cdd:COG4138 87 FQYLALHQPAGASS--EAVEQLLAQLAEALGLEDKLSRPLTQLSGGewQRVRLAAVLLQVwptINPEgqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 215820660 232 DSAScfQVV--SLMKSLAQGGRTIICTIHQPSAKLFEMfDKLYILSQGQCIFKG 283
Cdd:COG4138 165 DVAQ--QAAldRLLRELCQQGITVVMSSHDLNHTLRHA-DRVWLLKQGKLVASG 215
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
94-260 |
2.13e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---------RELRTfrKMSCYIMQDDMLLPHLTVLEAMMV 164
Cdd:PRK10584 35 RGETIALIGESGSGKSTLLAILAGL-DDGSSGEVSLVGQPlhqmdeearAKLRA--KHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 SANLKlSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 244
Cdd:PRK10584 112 PALLR-GESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170
....*....|....*..
gi 215820660 245 SLAQG-GRTIICTIHQP 260
Cdd:PRK10584 191 SLNREhGTTLILVTHDL 207
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
96-278 |
2.98e-18 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 88.68 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP-RE--LRTFRKMSCYIMQDDMLLpHLTVLEammvsaNLKLSE 172
Cdd:COG1132 367 ETVALVGPSGSGKSTLVNLLLRFYDPT-SGRILIDGVDiRDltLESLRRQIGVVPQDTFLF-SGTIRE------NIRYGR 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 173 K----QEV----KKELVTEILTAL--GLmscsHT----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 238
Cdd:COG1132 439 PdatdEEVeeaaKAAQAHEFIEALpdGY----DTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEAL 514
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 239 VVSLMKSLAQgGRTIIcTI-HQPSAklFEMFDKLYILSQGQ 278
Cdd:COG1132 515 IQEALERLMK-GRTTI-VIaHRLST--IRNADRILVLDDGR 551
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
99-254 |
3.90e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRK-------MscyIMQDDMLLPHLTVLEammvsaNLKL 170
Cdd:COG1129 34 ALLGENGAGKSTLMKILSGvYQPDS--GEILLDGEPVRFRSPRDaqaagiaI---IHQELNLVPNLSVAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SekQEVKK----------ELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:COG1129 103 G--REPRRgglidwramrRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERLF 180
|
170
....*....|....
gi 215820660 241 SLMKSLAQGGRTII 254
Cdd:COG1129 181 RIIRRLKAQGVAII 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
93-232 |
5.02e-18 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 84.62 E-value: 5.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 93 CRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP------RELRTFR--KMScYIMQDDMLLPHLTVLEAmmV 164
Cdd:cd03294 48 REGEIFVIMGLSGSGKSTLLRCINRLIEP-TSGKVLIDGQDiaamsrKELRELRrkKIS-MVFQSFALLPHRTVLEN--V 123
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 165 SANLKLS-EKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03294 124 AFGLEVQgVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
96-277 |
5.18e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.24 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRE--SG--MKGQILVNGRPRELRTFrKMscyIMQDDMLLPHLTVLEAMmvSANLKLS 171
Cdd:PRK11000 30 EFVVFVGPSGCGKSTLLRMIAGLEDitSGdlFIGEKRMNDVPPAERGV-GM---VFQSYALYPHLSVAENM--SFGLKLA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 172 --EKQEVKK--ELVTEILTALGLMScshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ----VVSLM 243
Cdd:PRK11000 104 gaKKEEINQrvNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQmrieISRLH 180
|
170 180 190
....*....|....*....|....*....|....*
gi 215820660 244 KSLaqgGRTIICTIH-QPSAklFEMFDKLYILSQG 277
Cdd:PRK11000 181 KRL---GRTMIYVTHdQVEA--MTLADKIVVLDAG 210
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
75-285 |
7.30e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 84.08 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 75 CWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQ--D 149
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKP-TSGSVLIRGEPitkENIREVRKFVGLVFQnpD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 150 DMLLPHLTVLEAMMVSANLKLSEkqEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK13652 89 DQIFSPTVEQDIAFGPINLGLDE--ETVAHRVSSALHMLGL---EELRDRVphhLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 227 PTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKGVV 285
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDL-VPEMADYIYVMDKGRIVAYGTV 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
100-278 |
8.98e-18 |
|
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: 84.85 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYrESGMKGQILVNG-----RPRELRTFRKMscyiMQDDMLLPHLTVLEAmmVSANLKL-SEK 173
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGF-EQPDSGSIMLDGedvtnVPPHLRHINMV----FQSYALFPHMTVEEN--VAFGLKMrKVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 QEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRT 252
Cdd:TIGR01187 74 RAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQeQLGIT 153
|
170 180
....*....|....*....|....*.
gi 215820660 253 IICTIHQPSAKLfEMFDKLYILSQGQ 278
Cdd:TIGR01187 154 FVFVTHDQEEAM-TMSDRIAIMRKGK 178
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
94-248 |
9.47e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 84.72 E-value: 9.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESGM-KGQILVNGR------PRELRTFR--KMScYIMQDDM--LLPHLTVLEA 161
Cdd:COG0444 30 RGETLGLVGESGSGKSTLARAILGlLPPPGItSGEILFDGEdllklsEKELRKIRgrEIQ-MIFQDPMtsLNPVMTVGDQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MM--VSANLKLSEKQevKKELVTEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD- 232
Cdd:COG0444 109 IAepLRIHGGLSKAE--ARERAIELLERVGL---PDPERRLdrypheLSGGMRQRVMIARALALEPKLLIADEPTTALDv 183
|
170
....*....|....*...
gi 215820660 233 --SAscfQVVSLMKSLAQ 248
Cdd:COG0444 184 tiQA---QILNLLKDLQR 198
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
96-233 |
9.79e-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: 82.77 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMSC-YIMQDDMLLPHLTVLEAmmVSANLKLSEKQ 174
Cdd:cd03296 29 ELVALLGPSGSGKTTLLRLIAGL-ERPDSGTILFGGEDATDVPVQERNVgFVFQHYALFRHMTVFDN--VAFGLRVKPRS 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 175 EV-----KKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:cd03296 106 ERppeaeIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDA 169
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
96-283 |
1.24e-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: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-----RPRELRtfRKMScyIMQDDM-LLPHLTVLEAMMVSANLK 169
Cdd:cd03266 32 EVTGLLGPNGAGKTTTLRMLAGLLEPD-AGFATVDGfdvvkEPAEAR--RRLG--FVSDSTgLYDRLTARENLEYFAGLY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:cd03266 107 GLKGDELTAR-LEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 215820660 250 GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 283
Cdd:cd03266 186 GKCILFSTHimQEVERL---CDRVVVLHRGRVVYEG 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
96-283 |
1.50e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.63 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGR-----PRELRTFRKMScYIMQDDMLLPHLTVLEAMMVSANL 168
Cdd:PRK10895 30 EIVGLLGPNGAGKTTTFYMVVGIvpRDAG---NIIIDDEdisllPLHARARRGIG-YLPQEASIFRRLSVYDNLMAVLQI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKQEVKKELVTEILTALGLmscSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 245
Cdd:PRK10895 106 RDDLSAEQREDRANELMEEFHI---EHLRDSMgqsLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH 182
|
170 180 190
....*....|....*....|....*....|....*...
gi 215820660 246 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK10895 183 LRDSGLGVLITDHNVRETL-AVCERAYIVSQGHLIAHG 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
79-232 |
1.81e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILvngRPRELRtfrkMScYIMQDDMLLPHLTV 158
Cdd:COG0488 8 FGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAG-ELEPDSGEVS---IPKGLR----IG-YLPQEPPLDDDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 159 LEAMMVS-------------ANLKLSEKQEVKKEL------------------VTEILTALGLMSCSHTR-TALLSGGQR 206
Cdd:COG0488 79 LDTVLDGdaelraleaeleeLEAKLAEPDEDLERLaelqeefealggweaearAEEILSGLGFPEEDLDRpVSELSGGWR 158
|
170 180
....*....|....*....|....*.
gi 215820660 207 KRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG0488 159 RRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
96-283 |
2.11e-17 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 81.89 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG---RPRELRTFRKMSCYIMQDDMLLpHLTVLEAMM--------- 163
Cdd:cd03251 29 ETVALVGPSGSGKSTLVNLIPRFYDVD-SGRILIDGhdvRDYTLASLRRQIGLVSQDVFLF-NDTVAENIAygrpgatre 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 -VSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:cd03251 107 eVEEAARAANAHEFIMELPEGYDTVIG------ERGVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESERLVQAA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 243 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03251 181 LERLMK-NRTTFVIAHRLST--IENADRIVVLEDGKIVERG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
92-283 |
2.72e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 86.61 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 92 FCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRE--LRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 169
Cdd:TIGR01257 953 FYENQITAFLGHNGAGKTTTLSILTGLLPP-TSGTVLVGGKDIEtnLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:TIGR01257 1032 GRSWEEAQLEM-EAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSG 1110
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 250 GRTIICTIHQPSAKLfeMFDKLYILSQGQCIFKG 283
Cdd:TIGR01257 1111 RTIIMSTHHMDEADL--LGDRIAIISQGRLYCSG 1142
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
96-343 |
3.67e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 3.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG----RPRELRTFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLK 169
Cdd:PRK13644 29 EYIGIIGKNGSGKSTLALHLNGLLRP-QKGKVLVSGidtgDFSKLQGIRKLVGIVFQNpETQFVGRTVEEDLAFGPeNLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSeKQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:PRK13644 108 LP-PIEIRK-RVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEK 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 250 GRTIICTIHqpSAKLFEMFDKLYILSQGQCIFKGVVTNLI--PYLKGLGLHCPTyhnpadfIIEVASgeygdlnpmlfRA 327
Cdd:PRK13644 186 GKTIVYITH--NLEELHDADRIIVMDRGKIVLEGEPENVLsdVSLQTLGLTPPS-------LIELAE-----------NL 245
|
250
....*....|....*.
gi 215820660 328 VQNGLCAMAEKKSSPE 343
Cdd:PRK13644 246 KMHGVVIPWENTSSPS 261
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
96-260 |
3.70e-17 |
|
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: 85.10 E-value: 3.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP---RELRTFRKMSCYIMQDdmllPHL---TVLEammvsaNLK 169
Cdd:TIGR02868 362 ERVAILGPSGSGKSTLLATLAGLLDP-LQGEVTLDGVPvssLDQDEVRRRVSVCAQD----AHLfdtTVRE------NLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSeKQEVKKELVTEILTALGL----------MSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 238
Cdd:TIGR02868 431 LA-RPDATDEELWAALERVGLadwlralpdgLDTVlGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADE 509
|
170 180
....*....|....*....|..
gi 215820660 239 VVSLMKSlAQGGRTIICTIHQP 260
Cdd:TIGR02868 510 LLEDLLA-ALSGRTVVLITHHL 530
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
96-232 |
4.07e-17 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 83.46 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELR---TfrkmscyIMQDDMLLPHLTVLEAmmVSAN 167
Cdd:PRK09452 41 EFLTLLGPSGCGKTTVLRLIAGF-ETPDSGRIMLDGQdithvPAENRhvnT-------VFQSYALFPHMTVFEN--VAFG 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 168 LKLSE--KQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK09452 111 LRMQKtpAAEIT-PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALD 176
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
96-283 |
6.09e-17 |
|
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: 84.79 E-value: 6.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR------PRELRtfRKMSCyIMQDDMLL------------PHLT 157
Cdd:TIGR01846 484 EFIGIVGPSGSGKSTLTKLLQRLY-TPQHGQVLVDGVdlaiadPAWLR--RQMGV-VLQENVLFsrsirdnialcnPGAP 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 VLEammVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:TIGR01846 560 FEH---VIHAAKLAGAHDFISELPQGYNTEVG------EKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEA 630
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 238 QVVSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:TIGR01846 631 LIMRNMREICR-GRTVIIIAHRLST--VRACDRIIVLEKGQIAESG 673
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
80-283 |
7.56e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 80.83 E-value: 7.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTFRKMSCYIMqddmLLP-HLTV 158
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTP-QSGTVFLGDKPISMLSSRQLARRLA----LLPqHHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 159 LEAMMV--------SANL----KLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK11231 88 PEGITVrelvaygrSPWLslwgRLSAEDN---ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 227 PTSGLDSASCFQVVSLMKSLAQGGRTIICTIH---QPSaklfEMFDKLYILSQGQCIFKG 283
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQGKTVVTVLHdlnQAS----RYCDHLVVLANGHVMAQG 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
96-278 |
8.36e-17 |
|
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: 82.47 E-value: 8.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----------PRELRTFRkmscYIMQDDMLLPHLTVLEAMMV 164
Cdd:TIGR02142 24 GVTAIFGRSGSGKTTLIRLIAGL-TRPDEGEIVLNGRtlfdsrkgiflPPEKRRIG----YVFQEARLFPHLSVRGNLRY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 SANLKLSEKQEVKKELVTEILtalGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 244
Cdd:TIGR02142 99 GMKRARPSERRISFERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 245 SLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGR 209
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
95-287 |
8.62e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 80.34 E-value: 8.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 95 RELIGIMGPSGAGKSTFMNILAG----YRESGMKGQILVNGR---PRELRTFRKMSCYIMQDDMLLPHLTVLEAmmVSAN 167
Cdd:PRK14247 29 NTITALMGPSGSGKSTLLRVFNRlielYPEARVSGEVYLDGQdifKMDVIELRRRVQMVFQIPNPIPNLSIFEN--VALG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQEVKKEL---VTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK14247 107 LKLNRLVKSKKELqerVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKIE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215820660 241 SLMKSLAQgGRTIICTIHQPsAKLFEMFDKLYILSQGQCIFKG----VVTN 287
Cdd:PRK14247 187 SLFLELKK-DMTIVLVTHFP-QQAARISDYVAFLYKGQIVEWGptreVFTN 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
96-283 |
8.77e-17 |
|
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: 80.22 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---ELRTFRKMSCYIMQDDMLLpHLTVLE-------AM--- 162
Cdd:cd03252 29 EVVGIVGRSGSGKSTLTKLIQRFYVPE-NGRVLVDGHDLalaDPAWLRRQVGVVLQENVLF-NRSIRDnialadpGMsme 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:cd03252 107 RVIEAAKLAGAHDFISELPEGYDTIVG------EQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESEHAIMRN 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 243 MKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03252 181 MHDICA-GRTVIIIAHRLST--VKNADRIIVMEKGRIVEQG 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
96-287 |
9.05e-17 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 82.16 E-value: 9.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNILagyrESGMKGQILVNGR------PRELRTFRKmscyimQDDMLLPHLTVLEAMMVSA 166
Cdd:PRK11153 32 EIFGVIGASGAGKSTLircINLL----ERPTSGRVLVDGQdltalsEKELRKARR------QIGMIFQHFNLLSSRTVFD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 N----LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK11153 102 NvalpLELAgtPKAEIKAR-VTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 215820660 241 SLMKSL-AQGGRTIICTIHqpsaklfEM------FDKLYILSQGQCIFKGVVTN 287
Cdd:PRK11153 181 ELLKDInRELGLTIVLITH-------EMdvvkriCDRVAVIDAGRLVEQGTVSE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
94-233 |
1.00e-16 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 80.68 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP-------RELrtfrkmscyIMQDDMLLPHLTVLEAmmVSA 166
Cdd:COG4525 32 SGEFVVALGASGCGKTTLLNLIAGF-LAPSSGEITLDGVPvtgpgadRGV---------VFQKDALLPWLNVLDN--VAF 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 167 NLKLS--EKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG4525 100 GLRLRgvPKAE-RRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDA 167
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
78-283 |
1.02e-16 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 80.54 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCY--IM-QDDMLLP 154
Cdd:COG4559 10 RLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPS-SGEVRLNGRPLAAWSPWELARRraVLpQHSSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 HLTVLE--AMMVSANlklSEKQEVKKELVTEILTALGLMSCSHTRTALLSGG--QRKRLAIAL----ELVNNPP-VMFFD 225
Cdd:COG4559 89 PFTVEEvvALGRAPH---GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGeqQRVQLARVLaqlwEPVDGGPrWLFLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 226 EPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSakLFEMF-DKLYILSQGQCIFKG 283
Cdd:COG4559 166 EPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLN--LAAQYaDRILLLHQGRLVAQG 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-260 |
1.20e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.09 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE---SGMK--GQILVNGRPR---ELRTFRKMSCYIMQDDMLL 153
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKvdGKVLYFGKDIfqiDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 PHLTVLEAmmVSANLK---LSEKQEVKKeLVTEILTALGLMSCSHTR----TALLSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK14246 103 PHLSIYDN--IAYPLKshgIKEKREIKK-IVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190
....*....|....*....|....*....|....
gi 215820660 227 PTSGLDSASCFQVVSLMKSLaQGGRTIICTIHQP 260
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITEL-KNEIAIVIVSHNP 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
83-260 |
1.28e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.43 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 83 TLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYResgmkgqilvngRPRELRTFRKMSC---YIMQ---DDMLLPhL 156
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVL------------RPTSGTVRRAGGArvaYVPQrseVPDSLP-L 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TVLEAMMVSANLKLSEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:NF040873 73 TVRDLVAMGRWARRGLWRRLTRDdraAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*..
gi 215820660 234 ASCFQVVSLMKSLAQGGRTIICTIHQP 260
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDL 179
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
78-280 |
1.32e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 80.20 E-value: 1.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGR------PRELRTFRKMscyimqddm 151
Cdd:PRK13548 11 RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD-SGEVRLNGRpladwsPAELARRRAV--------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 lLPH-------LTVLE--AMMVSAnlkLSEKQEVKKELVTEILTALGlmsCSHTRTAL---LSGG--QRKRLAIAL---- 213
Cdd:PRK13548 81 -LPQhsslsfpFTVEEvvAMGRAP---HGLSRAEDDALVAAALAQVD---LAHLAGRDypqLSGGeqQRVQLARVLaqlw 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHqpSAKLFEMF-DKLYILSQGQCI 280
Cdd:PRK13548 154 EPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLH--DLNLAARYaDRIVLLHQGRLV 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
82-283 |
1.35e-16 |
|
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: 78.12 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPREL--RTFRKMSCYIMQDdmllPHLtvl 159
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKP-QQGEITLDGVPVSDleKALSSLISVLNQR----PYL--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 eammvsanlklsekqevkkeLVTEILTALGLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:cd03247 87 --------------------FDTTLRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 215820660 240 VSLMKSLAQgGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03247 138 LSLIFEVLK-DKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
96-277 |
1.62e-16 |
|
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: 79.05 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRTFRKMscYIMQDDMLLPHLTVLE--AMMVSANLKLSEK 173
Cdd:TIGR01184 12 EFISLIGHSGCGKSTLLNLISGL-AQPTSGGVILEGKQITEPGPDRM--VVFQNYSLLPWLTVREniALAVDRVLPDLSK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 QEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS-LMKSLAQGGRT 252
Cdd:TIGR01184 89 SE-RRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEeLMQIWEEHRVT 167
|
170 180
....*....|....*....|....*
gi 215820660 253 IICTIHQPSAKLFeMFDKLYILSQG 277
Cdd:TIGR01184 168 VLMVTHDVDEALL-LSDRVVMLTNG 191
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
42-283 |
3.30e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 82.18 E-value: 3.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 42 NHITEAQ---RFS--HLPKRSAVDIEF--VELSYSVREGPcwrkrgyktLLKCLSGKFCRRELIGIMGPSGAGKSTFMNI 114
Cdd:PRK11160 315 NEITEQKpevTFPttSTAAADQVSLTLnnVSFTYPDQPQP---------VLKGLSLQIKAGEKVALLGRTGCGKSTLLQL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 115 LAGYRESGmKGQILVNGRP----RElRTFRKMSCYIMQDdmllPHL---TVLEammvsaNLKLSEKQEVKKELvTEILTA 187
Cdd:PRK11160 386 LTRAWDPQ-QGEILLNGQPiadySE-AALRQAISVVSQR----VHLfsaTLRD------NLLLAAPNASDEAL-IEVLQQ 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 188 LGLMSCSHTRTAL----------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTI 257
Cdd:PRK11160 453 VGLEKLLEDDKGLnawlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMIT 531
|
250 260
....*....|....*....|....*.
gi 215820660 258 HQpsAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK11160 532 HR--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
67-283 |
4.40e-16 |
|
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: 78.14 E-value: 4.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 67 SYSVREGPCW----------RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNG-RP- 133
Cdd:cd03267 9 SYRVYSKEPGligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGlLQPTS--GEVRVAGlVPw 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 -RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIA 212
Cdd:cd03267 87 kRRKKFLRRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRL-DELSELLDLEELLDTPVRQLSLGQRMRAEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 213 LELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL-AQGGRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKG 283
Cdd:cd03267 166 AALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHymKDIEAL---ARRVLVIDKGRLLYDG 236
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
98-283 |
5.39e-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: 77.66 E-value: 5.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 98 IGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RE--LRTFRKMSCYIMQDdMLLPHLTVLEAMMVsANLKLSEKQ 174
Cdd:cd03253 30 VAIVGPSGSGKSTILRLLFRFYDV-SSGSILIDGQDiREvtLDSLRRAIGVVPQD-TVLFNDTIGYNIRY-GRPDATDEE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 175 EV---KKELVTEILTAL-----------GLMscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:cd03253 107 VIeaaKAAQIHDKIMRFpdgydtivgerGLK---------LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQ 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 215820660 241 SLMKSLAQgGRTIICTIHQPS----AklfemfDKLYILSQGQCIFKG 283
Cdd:cd03253 178 AALRDVSK-GRTTIVIAHRLStivnA------DKIIVLKDGRIVERG 217
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-288 |
6.29e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 78.60 E-value: 6.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNIL-------AGYRESGmkgQILVNGRP----RELRTFRKMSCYIMQDD 150
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSG---DVLLGGRSifnyRDVLEFRRRVGMLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 151 MLLPhLTVLEAMMVSANL-KLSEKQEVKKeLVTEILTALGLMSCSHTRTA----LLSGGQRKRLAIALELVNNPPVMFFD 225
Cdd:PRK14271 111 NPFP-MSIMDNVLAGVRAhKLVPRKEFRG-VAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 215820660 226 EPTSGLDSASCFQVVSLMKSLAQggRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 288
Cdd:PRK14271 189 EPTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
61-283 |
9.91e-16 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 77.19 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEF--VELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRE 135
Cdd:cd03249 1 IEFknVSFRYPSRPD--------VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDP-TSGEILLDGvdiRDLN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 136 LRTFRKMSCYIMQDdmllPHL---TVLEAMMVSAN-LKLSEKQEV-KKELVTEILTAL--GLMSCSHTRTALLSGGQRKR 208
Cdd:cd03249 72 LRWLRSQIGLVSQE----PVLfdgTIAENIRYGKPdATDEEVEEAaKKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 209 LAIALELVNNPPVMFFDEPTSGLDSASCFQVvslMKSL--AQGGRTIICTIHQPSAklFEMFDKLYILSQGQCIFKG 283
Cdd:cd03249 148 IAIARALLRNPKILLLDEATSALDAESEKLV---QEALdrAMKGRTTIVIAHRLST--IRNADLIAVLQNGQVVEQG 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
94-280 |
1.03e-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: 75.16 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRkmscyimqddmllphltvlEAMmvsanlklsek 173
Cdd:cd03216 25 RGEVHALLGENGAGKSTLMKILSGLYKPD-SGEILVDGKEVSFASPR-------------------DAR----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 qevkkelvteiltALGlMSCSHTrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 253
Cdd:cd03216 74 -------------RAG-IAMVYQ----LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAV 135
|
170 180 190
....*....|....*....|....*....|
gi 215820660 254 ICTIHqpsaKLFEMF---DKLYILSQGQCI 280
Cdd:cd03216 136 IFISH----RLDEVFeiaDRVTVLRDGRVV 161
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
52-283 |
1.09e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 80.66 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 52 HLPKRSAVDIEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG---YResgmkGQIL 128
Cdd:PRK11174 341 ELASNDPVTIEAEDLEILSPDG--------KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGflpYQ-----GSLK 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 129 VNG---RPRELRTFRKMSCYIMQDDmLLPHLTVLEAMMVsANLKLSE---KQEVKKELVTEILTAL--GLMSCSHTRTAL 200
Cdd:PRK11174 408 INGielRELDPESWRKHLSWVGQNP-QLPHGTLRDNVLL-GNPDASDeqlQQALENAWVSEFLPLLpqGLDTPIGDQAAG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTiHQPSAkLFEMfDKLYILSQGQCI 280
Cdd:PRK11174 486 LSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQLED-LAQW-DQIWVMQDGQIV 562
|
...
gi 215820660 281 FKG 283
Cdd:PRK11174 563 QQG 565
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
95-235 |
1.13e-15 |
|
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: 78.99 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 95 RELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTF-----RKMScYIMQDDMLLPHLTVLEammvsa 166
Cdd:COG4148 25 RGVTALFGPSGSGKTTLLRAIAGL-ERPDSGRIRLGGEVlqdSARGIFlpphrRRIG-YVFQEARLFPHLSVRG------ 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 167 NLKLSEKQEVK---KELVTEILTALGLmscSH---TRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:COG4148 97 NLLYGRKRAPRaerRISFDEVVELLGI---GHlldRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
82-258 |
1.21e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 77.52 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILaGYRESGMKGQILVNGRPREL---RTFRKMSCYIMQDdmlLPH--- 155
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKML-GRHQPPSEGEILLDAQPLESwssKAFARKVAYLPQQ---LPAaeg 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMMVSA---NLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK10575 100 MTVRELVAIGRypwHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
170 180
....*....|....*....|....*..
gi 215820660 233 SASCFQVVSLMKSLAQG-GRTIICTIH 258
Cdd:PRK10575 180 IAHQVDVLALVHRLSQErGLTVIAVLH 206
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
58-283 |
1.76e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 77.46 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 58 AVDiefvELSYSVREGpcwrkrgyktllkclsgkfcrrELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRE 135
Cdd:COG4152 16 AVD----DVSFTVPKG----------------------EIFGLLGPNGAGKTTTIRIILGilAPDSG---EVLWDGEPLD 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 136 LRTFRKMScYimqddM-----LLPHLTVLEAMMVSANLKLSEKQEVKKELvTEILTALGLMSCSHTRTALLSGGQRKRLA 210
Cdd:COG4152 67 PEDRRRIG-Y-----LpeergLYPKMKVGEQLVYLARLKGLSKAEAKRRA-DEWLERLGLGDRANKKVEELSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 211 IALELVNNPPVMFFDEPTSGLDSAScfqvVSLMKS----LAQGGRTIICTIHQ-PSAKlfEMFDKLYILSQGQCIFKG 283
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVN----VELLKDvireLAAKGTTVIFSSHQmELVE--ELCDRIVIINKGRKVLSG 211
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
96-232 |
2.80e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 77.95 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR-----PRELRTFRKMscyiMQDDMLLPHLTVleammvSANLKL 170
Cdd:PRK11607 46 EIFALLGASGCGKSTLLRMLAGF-EQPTAGQIMLDGVdlshvPPYQRPINMM----FQSYALFPHMTV------EQNIAF 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 171 SEKQE--VKKEL---VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11607 115 GLKQDklPKAEIasrVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
96-231 |
3.74e-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: 75.40 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRP-RELRTFRKMS---CYIMQDDMLLPHLTVLEammvsaNLKL- 170
Cdd:COG0410 30 EIVALLGRNGAGKTTLLKAISGLLPP-RSGSIRFDGEDiTGLPPHRIARlgiGYVPEGRRIFPSLTVEE------NLLLg 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 171 ----SEKQEVKK--ELVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:COG0410 103 ayarRDRAEVRAdlERVYELFPRLKERR--RQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
67-248 |
3.95e-15 |
|
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: 78.57 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 67 SYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmkGQILVNGRP------RELRTFR 140
Cdd:COG4172 284 WFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE--GEIRFDGQDldglsrRALRPLR 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 141 KMSCYIMQDDM--LLPHLTVL----EAMMVSAnLKLSEKQevKKELVTEILTALGLmscshTRTAL------LSGGQRKR 208
Cdd:COG4172 362 RRMQVVFQDPFgsLSPRMTVGqiiaEGLRVHG-PGLSAAE--RRARVAEALEEVGL-----DPAARhrypheFSGGQRQR 433
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 215820660 209 LAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 248
Cdd:COG4172 434 IAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQR 473
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
60-291 |
5.20e-15 |
|
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: 78.63 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 60 DIEFVELSYSVregpcwrkrGY-KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR---E 135
Cdd:TIGR01193 473 DIVINDVSYSY---------GYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR-SGEILLNGFSLkdiD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 136 LRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSEkQEVKKEL-VTEILTALGLMSCS-HTRTAL----LSGGQRKRL 209
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSG-SILENLLLGAKENVSQ-DEIWAACeIAEIKDDIENMPLGyQTELSEegssISGGQKQRI 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 210 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQggRTIICTIHQPSakLFEMFDKLYILSQGQCIFKGVVTNLI 289
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS--VAKQSDKIIVLDHGKIIEQGSHDELL 696
|
..
gi 215820660 290 PY 291
Cdd:TIGR01193 697 DR 698
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
99-254 |
5.24e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAG-YR-ESgmkGQILVNGRPRELRTFRK-MSCYI-M--QDDMLLPHLTVLE----AMMVSANL 168
Cdd:COG3845 35 ALLGENGAGKSTLMKILYGlYQpDS---GEILIDGKPVRIRSPRDaIALGIgMvhQHFMLVPNLTVAEnivlGLEPTKGG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASCFQVvslMKS 245
Cdd:COG3845 112 RLDRKAARAR--IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpqEADELFEI---LRR 186
|
....*....
gi 215820660 246 LAQGGRTII 254
Cdd:COG3845 187 LAAEGKSII 195
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
61-283 |
5.90e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 75.54 E-value: 5.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGpcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGR---PRELR 137
Cdd:PRK13647 5 IEVEDLHFRYKDG--------TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIY-LPQRGRVKVMGRevnAENEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 138 TFRKMSCYIMQD-DMLLPHLTVLEAMMVSA-NLKLSeKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALEL 215
Cdd:PRK13647 76 WVRSKVGLVFQDpDDQVFSSTVWDDVAFGPvNMGLD-KDEVE-RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 216 VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAA-EWADQVIVLKEGRVLAEG 220
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
79-260 |
6.02e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.07 E-value: 6.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRP-RELRT-FRKMSCYIMQDDMLLP 154
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGlaRPDAG---EVLWQGEPiRRQRDeYHQDLLYLGHQPGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 155 HLTVLEammvsaNLKLSEK--QEVKKELVTEILTALGL-----MSCSHtrtalLSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK13538 88 ELTALE------NLRFYQRlhGPGDDEALWEALAQVGLagfedVPVRQ-----LSAGQQRRVALARLWLTRAPLWILDEP 156
|
170 180 190
....*....|....*....|....*....|...
gi 215820660 228 TSGLDSASCFQVVSLMKSLAQGGRTIICTIHQP 260
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
96-277 |
9.33e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKmsCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 175
Cdd:PRK11248 28 ELLVVLGPSGCGKTTLLNLIAGFVPYQ-HGSITLDGKPVEGPGAER--GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 176 vKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTII 254
Cdd:PRK11248 105 -RLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQEtGKQVL 183
|
170 180
....*....|....*....|...
gi 215820660 255 CTIHQPSAKLFeMFDKLYILSQG 277
Cdd:PRK11248 184 LITHDIEEAVF-MATELVLLSPG 205
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
96-258 |
9.80e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 73.76 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 169
Cdd:PRK10908 29 EMAFLTGHSGAGKSTLLKLICGI-ERPSAGKIWFSGhditrlKNREVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:PRK10908 108 GASGDDIRRR-VSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRV 186
|
....*....
gi 215820660 250 GRTIICTIH 258
Cdd:PRK10908 187 GVTVLMATH 195
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
61-239 |
1.19e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 73.66 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSvregpcWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTfr 140
Cdd:cd03248 12 VKFQNVTFA------YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQP-QGGQVLLDGKPISQYE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 141 kmSCYIMQDDMLLPHLTVLEAMMVSANLKLSeKQEVKKELVTEI-----------LTALGLMSCSHTRTALLSGGQRKRL 209
Cdd:cd03248 83 --HKYLHSKVSLVGQEPVLFARSLQDNIAYG-LQSCSFECVKEAaqkahahsfisELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190
....*....|....*....|....*....|
gi 215820660 210 AIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQV 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
99-307 |
1.26e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.77 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAGYRESGMK----GQILVNG--RPRELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKL 170
Cdd:PRK13643 36 ALIGHTGSGKSTLLQHLNGLLQPTEGkvtvGDIVVSStsKQKEIKPVRKKVGVVFQfpESQLFEETVLKDVAFGPQNFGI 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SeKQEVKKeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:PRK13643 116 P-KEKAEK-IAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 250 GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCPTYHNPAD 307
Cdd:PRK13643 194 GQTVVLVTHLMD-DVADYADYVYLLEKGHIISCGTPSDVfqeVDFLKAHELGVPKATHFAD 253
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
99-278 |
1.27e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.87 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRELRTFRKM----SCYIMQDDMLLPHLTVLEAMMVS---ANLKL 170
Cdd:PRK11288 34 ALMGENGAGKSTLLKILSGnYQPDA--GSILIDGQEMRFASTTAAlaagVAIIYQELHLVPEMTVAENLYLGqlpHKGGI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 250
Cdd:PRK11288 112 VNRRLLNYE-AREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEG 190
|
170 180
....*....|....*....|....*...
gi 215820660 251 RTIICTIHQpSAKLFEMFDKLYILSQGQ 278
Cdd:PRK11288 191 RVILYVSHR-MEEIFALCDAITVFKDGR 217
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
94-258 |
1.37e-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: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRelRTFRKMSCYIMQDDML---LPhLTVLEAMMVSANLKL 170
Cdd:TIGR03771 5 KGELLGLLGPNGAGKTTLLRAILGLIPPA-KGTVKVAGASP--GKGWRHIGYVPQRHEFawdFP-ISVAHTVMSGRTGHI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKE---LVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:TIGR03771 81 GWLRRPCVAdfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQELLTELFIELA 160
|
170
....*....|.
gi 215820660 248 QGGRTIICTIH 258
Cdd:TIGR03771 161 GAGTAILMTTH 171
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
88-283 |
2.73e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 73.04 E-value: 2.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 88 LSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgmKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHLTVLE--AM 162
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG--SGSIQFAGQPLEawsAAELARHRAYLSQQQTPPFAMPVFQylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSEKQEVkkelVTEILTALGLMSCSHTRTALLSGG--QRKRLAIALELV---NNP--PVMFFDEPTSGLDSAs 235
Cdd:PRK03695 93 HQPDKTRTEAVASA----LNEVAEALGLDDKLGRSVNQLSGGewQRVRLAAVVLQVwpdINPagQLLLLDEPMNSLDVA- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215820660 236 cfQVV---SLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK03695 168 --QQAaldRLLSELCQQGIAVVMSSHDLNHTL-RHADRVWLLKQGKLLASG 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
96-283 |
3.10e-14 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 72.75 E-value: 3.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyresgM----KGQILVNGR------------------PRELRTFRKMScyiMQDDMLL 153
Cdd:COG1137 30 EIVGLLGPNGAGKTTTFYMIVG-----LvkpdSGRIFLDGEdithlpmhkrarlgigylPQEASIFRKLT---VEDNILA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 phltVLEAmmvsanLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:COG1137 102 ----VLEL------RKLSKKE--REERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDEPFAGVDP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 215820660 234 ASCFQVVSLMKSLAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:COG1137 170 IAVADIQKIIRHLKERGIGVLITDHNVRETL-GICDRAYIISEGKVLAEG 218
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
96-288 |
3.22e-14 |
|
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: 72.56 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRE-LRTFRKMS---CYIMQDDMLLPHLTVLEAMMVSANLKLS 171
Cdd:TIGR03410 27 EVTCVLGRNGVGKTTLLKTLMG-LLPVKSGSIRLDGEDITkLPPHERARagiAYVPQGREIFPRLTVEENLLTGLAALPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 172 EKQEVKKELVtEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL------DSAscfQVVSLMKs 245
Cdd:TIGR03410 106 RSRKIPDEIY-ELFPVLKEML--GRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIqpsiikDIG---RVIRRLR- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 215820660 246 lAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNL 288
Cdd:TIGR03410 179 -AEGGMAIL-LVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
96-283 |
3.24e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 75.07 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---------RPRELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSA 166
Cdd:PRK10070 55 EIFVIMGLSGSGKSTMVRLLNRLIEP-TRGQVLIDGvdiakisdaELREVR--RKKIAMVFQSFALMPHMTVLDNTAFGM 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSEKQEvKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKS 245
Cdd:PRK10070 132 ELAGINAEE-RREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQdELVKL 210
|
170 180 190
....*....|....*....|....*....|....*...
gi 215820660 246 LAQGGRTIICTIHQPSAKLfEMFDKLYILSQGQCIFKG 283
Cdd:PRK10070 211 QAKHQRTIVFISHDLDEAM-RIGDRIAIMQNGEVVQVG 247
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
92-283 |
4.02e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 73.73 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 92 FCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILV----------------NGRPRELRTF---RKMSCYIMQ-DDM 151
Cdd:PRK13631 49 FEKNKIYFIIGNSGSGKSTLVTHFNGLIKSK-YGTIQVgdiyigdkknnhelitNPYSKKIKNFkelRRRVSMVFQfPEY 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 LLPHLTVLEAMMVSAnLKLSEKQEVKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:PRK13631 128 QLFKDTIEKDIMFGP-VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFgLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 215820660 231 LDSASCFQVVSLMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKILKTG 258
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
96-232 |
7.09e-14 |
|
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: 74.99 E-value: 7.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRE---LRTFRKMSCYIMQDDMLLPHlTVLEAMMVSANLKLSE 172
Cdd:TIGR03797 480 EFVAIVGPSGSGKSTLLRLLLGF-ETPESGSVFYDGQDLAgldVQAVRRQLGVVLQNGRLMSG-SIFENIAGGAPLTLDE 557
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 173 KQEVKKEL-VTEILTAL--GLmscsHTRTA----LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:TIGR03797 558 AWEAARMAgLAEDIRAMpmGM----HTVISegggTLSGGQRQRLLIARALVRKPRILLFDEATSALD 620
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
77-278 |
1.20e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 71.25 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKR-GYKTLLKCL-----SGKFcrrelIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPreLRTFRKMSCYIMQDD 150
Cdd:PRK11247 19 SKRyGERTVLNQLdlhipAGQF-----VAVVGRSGCGKSTLLRLLAGL-ETPSAGELLAGTAP--LAEAREDTRLMFQDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 151 MLLPHLTVLEammvsaNLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:PRK11247 91 RLLPWKKVID------NVGLGLKGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 231 LDSASCFQVVSLMKSL-AQGGRTIICTIHQPSAKLfEMFDKLYILSQGQ 278
Cdd:PRK11247 164 LDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAV-AMADRVLLIEEGK 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
94-233 |
1.24e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGrprELRTFRKMS----CYIMQDDMLLPHLTVLEAmmVSANLK 169
Cdd:PRK11432 31 QGTMVTLLGPSGCGKTTVLRLVAGL-EKPTEGQIFIDG---EDVTHRSIQqrdiCMVFQSYALFPHMSLGEN--VGYGLK 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215820660 170 LS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK11432 105 MLgvPKEERKQR-VKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA 169
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
96-278 |
1.32e-13 |
|
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: 73.92 E-value: 1.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNG---RPRELRTFRKMSCYIMQDDMLLPHlTV----------LEAM 162
Cdd:TIGR01842 345 EALAIIGPSGSGKSTLARLIVGI-WPPTSGSVRLDGadlKQWDRETFGKHIGYLPQDVELFPG-TVaeniarfgenADPE 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSEKQEVKKELVTEILTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:TIGR01842 423 KIIEAAKLAGVHELILRLPDGYDTVIG------PGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANA 496
|
170 180 190
....*....|....*....|....*....|....*.
gi 215820660 243 MKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:TIGR01842 497 IKALKARGITVVVITHRPS--LLGCVDKILVLQDGR 530
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
96-232 |
1.33e-13 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 72.57 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfR--KMscyIMQDDMLLPHLTVLEAMmvSAN 167
Cdd:PRK11650 31 EFIVLVGPSGCGKSTLLRMVAGL-ERITSGEIWIGGRvvnelePAD----RdiAM---VFQNYALYPHMSVRENM--AYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 168 LKLS--EKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11650 101 LKIRgmPKAEIEER-VAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLD 166
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
66-248 |
1.37e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 66 LSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP------RELRTF 139
Cdd:PRK10419 9 LSHHYAHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGL-ESPSQGNVSWRGEPlaklnrAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 140 RKMSCYIMQDDM--LLPHLTV----LEAMMVSANLKLSEKQEVKKELVTEILTALGLMScshTRTALLSGGQRKRLAIAL 213
Cdd:PRK10419 88 RRDIQMVFQDSIsaVNPRKTVreiiREPLRHLLSLDKAERLARASEMLRAVDLDDSVLD---KRPPQLSGGQLQRVCLAR 164
|
170 180 190
....*....|....*....|....*....|....*
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 248
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQ 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
88-278 |
1.66e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.28 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 88 LSGKFCRRELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PR-ELRTFRKMSCYIMQ---DDMLLPHLTVLE 160
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGV-DKRAGGEIRLNGKdisPRsPLDAVKKGMAYITEsrrDNGFFPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKLS----------EKQEVKKELVTEILTALGLMSCSHTRTALlSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:PRK09700 361 NMAISRSLKDGgykgamglfhEVDEQRTAENQRELLALKCHSVNQNITEL-SGGNQQKVLISKWLCCCPEVIIFDEPTRG 439
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 215820660 231 LDSASCFQVVSLMKSLAQGGRTIICTihqpSAKLFEMF---DKLYILSQGQ 278
Cdd:PRK09700 440 IDVGAKAEIYKVMRQLADDGKVILMV----SSELPEIItvcDRIAVFCEGR 486
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
96-254 |
1.97e-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: 70.16 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMN-ILAGYRESGmkGQILVNGR----------PRE---LRtfRKMSCYIMQDDMLLPHLTVLEA 161
Cdd:COG4778 38 ECVALTGPSGAGKSTLLKcIYGNYLPDS--GSILVRHDggwvdlaqasPREilaLR--RRTIGYVSQFLRVIPRVSALDV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MMVSAnLKLSEKQEVKKELVTEILTALGL-MSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:COG4778 114 VAEPL-LERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVV 192
|
170
....*....|....
gi 215820660 241 SLMKSLAQGGRTII 254
Cdd:COG4778 193 ELIEEAKARGTAII 206
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
96-232 |
2.08e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 70.89 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGR-----PRELRtfrkmSCYI---MQDDML--LPHLTVLEAMMV 164
Cdd:COG1101 33 DFVTVIGSNGAGKSTLLNAIAGsLPPDS--GSILIDGKdvtklPEYKR-----AKYIgrvFQDPMMgtAPSMTIEENLAL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 165 SAN------LKLSEKQEvKKELVTEILTALGL-----MscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:COG1101 106 AYRrgkrrgLRRGLTKK-RRELFRELLATLGLglenrL---DTKVGLLSGGQRQALSLLMATLTKPKLLLLDEHTAALD 180
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
93-254 |
2.50e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.61 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 93 CRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEammvs 165
Cdd:cd03215 24 RAGEIVGIAGLVGNGQTELAEALFGLR-PPASGEITLDGKPVTRRSPRDAIragiAYVPEDrkrEGLVLDLSVAE----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 166 aNLKLSekqevkkelvteiltalglmscshtrtALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 245
Cdd:cd03215 98 -NIALS---------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE 149
|
....*....
gi 215820660 246 LAQGGRTII 254
Cdd:cd03215 150 LADAGKAVL 158
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
95-302 |
5.20e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.08 E-value: 5.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 95 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG-----RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS---- 165
Cdd:PRK13637 33 GEFVGLIGHTGSGKSTLIQHLNGLLKP-TSGKIIIDGvditdKKVKLSDIRKKVGLVFQ----YPEYQLFEETIEKdiaf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 166 --ANLKLSEkQEVKKElVTEILTALGL-MSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 241
Cdd:PRK13637 108 gpINLGLSE-EEIENR-VKRAMNIVGLdYEDYKDKSPFeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILN 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 242 LMKSLAQG-GRTIICTIH--QPSAKLfemFDKLYILSQGQCIFKGV---VTNLIPYLKGLGLHCP--TY 302
Cdd:PRK13637 186 KIKELHKEyNMTIILVSHsmEDVAKL---ADRIIVMNKGKCELQGTpreVFKEVETLESIGLAVPqvTY 251
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
82-232 |
5.35e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 71.63 E-value: 5.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQI-----LVNGrprelrtfrkmscYIMQD-DMLLPH 155
Cdd:COG0488 328 KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAG-ELEPDSGTVklgetVKIG-------------YFDQHqEELDPD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 156 LTVLEAMmvsanlklseKQEVKKELVTEILTALGLM----SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:COG0488 394 KTVLDEL----------RDGAPGGTEQEVRGYLGRFlfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHL 463
|
.
gi 215820660 232 D 232
Cdd:COG0488 464 D 464
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
54-278 |
6.27e-13 |
|
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: 71.39 E-value: 6.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 54 PKRSAVDiefvELSYSVREGpcwrkrgyktllkclsgkfcrrELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRP 133
Cdd:TIGR02633 271 PHRKRVD----DVSFSLRRG----------------------EILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKP 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 RELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSANLKLSEKQEVKKElvTEILTALGLMSCSHTRTAL------ 200
Cdd:TIGR02633 325 VDIRNpaqaIRAGIAMVPEDrkrHGIVPILGVGKNITLSVLKSFCFKMRIDAA--AELQIIGSAIQRLKVKTASpflpig 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 201 -LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:TIGR02633 403 rLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAII-VVSSELAEVLGLSDRVLVIGEGK 480
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
55-246 |
7.66e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 55 KRSAVDIEFVELSYSVREGPCWRKRGYKTLlKCLSG---KFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG 131
Cdd:PRK15079 5 KKVLLEVADLKVHFDIKDGKQWFWQPPKTL-KAVDGvtlRLYEGETLGVVGESGCGKSTFARAIIGLVKA-TDGEVAWLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 132 R------PRELRTFRKMSCYIMQDDM--LLPHLTVLEamMVSANL-----KLSeKQEVKKElVTEILTALGLMSCSHTRT 198
Cdd:PRK15079 83 KdllgmkDDEWRAVRSDIQMIFQDPLasLNPRMTIGE--IIAEPLrtyhpKLS-RQEVKDR-VKAMMLKVGLLPNLINRY 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 215820660 199 AL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 246
Cdd:PRK15079 159 PHeFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQL 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
96-289 |
7.85e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 69.73 E-value: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGR-P-RELRTFRKMSCYIM-QDDMLLPHLTVLEammvSANL-- 168
Cdd:COG4586 49 EIVGFIGPNGAGKSTTIKMLTGilVPTSG---EVRVLGYvPfKRRKEFARRIGVVFgQRSQLWWDLPAID----SFRLlk 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 ---KLSEKqEVKKEL--VTEILTALGLMscsHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLM 243
Cdd:COG4586 122 aiyRIPDA-EYKKRLdeLVELLDLGELL---DTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFL 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 215820660 244 KSL-AQGGRTIICTIHqpsaklfEMFD------KLYILSQGQCIFKGVVTNLI 289
Cdd:COG4586 198 KEYnRERGTTILLTSH-------DMDDiealcdRVIVIDHGRIIYDGSLEELK 243
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
80-261 |
9.38e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 68.72 E-value: 9.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKST----FMNILAGYRESGMKGQILVNGR--------PRELRTFRKMscyIM 147
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrtFNRLLELNEEARVEGEVRLFGRniyspdvdPIEVRREVGM---VF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 148 QDDMLLPHLTVLEAmmVSANLKLSEKQEVKKELVTEILTAL---GLMSCSHTR----TALLSGGQRKRLAIALELVNNPP 220
Cdd:PRK14267 92 QYPNPFPHLTIYDN--VAIGVKLNGLVKSKKELDERVEWALkkaALWDEVKDRlndyPSNLSGGQRQRLVIARALAMKPK 169
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 221 VMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIHQPS 261
Cdd:PRK14267 170 ILLMDEPTANIDPVGTAKIEELLFELKK-EYTIVLVTHSPA 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
51-288 |
1.14e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 71.29 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 51 SHLPKRSAVDIEFVELSYSvregpcWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVN 130
Cdd:TIGR00958 469 TLAPLNLEGLIEFQDVSFS------YPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQP-TGGQVLLD 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 131 GRPreLRTFRkmSCYIMQDDMLLPHLTVLEAMMVSAN----LKLSEKQEVkkelvteilTALGLMSCSHT---------- 196
Cdd:TIGR00958 542 GVP--LVQYD--HHYLHRQVALVGQEPVLFSGSVRENiaygLTDTPDEEI---------MAAAKAANAHDfimefpngyd 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 197 -----RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKslaQGGRTIICTIHQPSakLFEMFDKL 271
Cdd:TIGR00958 609 tevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS---RASRTVLLIAHRLS--TVERADQI 683
|
250
....*....|....*..
gi 215820660 272 YILSQGQCIFKGVVTNL 288
Cdd:TIGR00958 684 LVLKKGSVVEMGTHKQL 700
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
94-258 |
1.22e-12 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 70.26 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIM---QDDML--------------LPHL 156
Cdd:PRK09536 28 EGSLVGLVGPNGAGKTTLLRAINGTLTPT-AGTVLVAGDDVEALSARAASRRVAsvpQDTSLsfefdvrqvvemgrTPHR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 TvleammvsanlKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASC 236
Cdd:PRK09536 107 S-----------RFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQ 175
|
170 180
....*....|....*....|..
gi 215820660 237 FQVVSLMKSLAQGGRTIICTIH 258
Cdd:PRK09536 176 VRTLELVRRLVDDGKTAVAAIH 197
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
94-232 |
1.44e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.09 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRE------------LRTFrkmscyimQDDMLLPHLTVLE 160
Cdd:PRK11300 30 EQEIVSLIGPNGAGKTTVFNCLTGfYKPTG--GTILLRGQHIEglpghqiarmgvVRTF--------QHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKL----------------SEKQEVkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFF 224
Cdd:PRK11300 100 NLLVAQHQQLktglfsgllktpafrrAESEAL--DRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
....*...
gi 215820660 225 DEPTSGLD 232
Cdd:PRK11300 178 DEPAAGLN 185
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
61-258 |
1.67e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPCWRKRGYKTL-LKCLSGKFcrrelIGIMGPSGAGKSTFM---NIL----------AGYresgmkgQ 126
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNIsFELEEGSF-----VALVGHTGSGKSTLMqhfNALlkpssgtitiAGY-------H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 127 ILVNGRPRELRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSG 203
Cdd:PRK13641 71 ITPETGNKNLKKLRKKVSLVFQfPEAQLFENTVLKDVEFGPkNFGFSEDE--AKEKALKWLKKVGLSEDLISKSPFeLSG 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 204 GQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
96-278 |
1.85e-12 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 67.40 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG---YRESGmkGQILVNG----------RPRE-LrtFrkmscYIMQDDMLLPHLTVLEA 161
Cdd:COG0396 27 EVHAIMGPNGSGKSTLAKVLMGhpkYEVTS--GSILLDGedilelspdeRARAgI--F-----LAFQYPVEIPGVSVSNF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MMVSANLKLSEKQEVKK--ELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASc 236
Cdd:COG0396 98 LRTALNARRGEELSAREflKLLKEKMKELG-LDEDFLDRYVnegFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDA- 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 215820660 237 FQVVS-LMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQ 278
Cdd:COG0396 176 LRIVAeGVNKLRSPDRGILIITHYQ--RILDYIkpDFVHVLVDGR 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
55-283 |
2.03e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 68.09 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 55 KRSAVDIEFVELSYSVREGPcwrkrgyktLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNG-- 131
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSENN---------ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGlLKPQ--SGEIKIDGit 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 132 -RPRELRTFRKMSCYIMQD-DMLLPHLTV-------LEAMMVSanlklsekQEVKKELVTEILTALGLMSCSHTRTALLS 202
Cdd:PRK13632 73 iSKENLKEIRKKIGIIFQNpDNQFIGATVeddiafgLENKKVP--------PKKMKDIIDDLAKKVGMEDYLDKEPQNLS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 203 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQPSAKLfeMFDKLYILSQGQCIF 281
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRkTRKKTLISITHDMDEAI--LADKVIVFSEGKLIA 222
|
..
gi 215820660 282 KG 283
Cdd:PRK13632 223 QG 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
61-283 |
2.26e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.85 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPCWRKRG-YKTLLKCLSGKFcrrelIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNG-------R 132
Cdd:PRK13649 3 INLQNVSYTYQAGTPFEGRAlFDVNLTIEDGSY-----TAFIGHTGSGKSTIMQLLNGLH-VPTQGSVRVDDtlitstsK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 133 PRELRTFRKMSCYIMQ-DDMLLPHLTVLEAMMVSA-NLKLSEKQEVKkeLVTEILTALGLMSCSHTRTAL-LSGGQRKRL 209
Cdd:PRK13649 77 NKDIKQIRKKVGLVFQfPESQLFEETVLKDVAFGPqNFGVSQEEAEA--LAREKLALVGISESLFEKNPFeLSGGQMRRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 210 AIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD-DVANYADFVYVLEKGKLVLSG 227
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
96-283 |
3.13e-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: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG---YRESG----MKGQILVNGRPRElRTfRKMSCYIMQDDMLLPHLTVLEAMMVSANL 168
Cdd:TIGR01978 27 EIHAIMGPNGSGKSTLSKTIAGhpsYEVTSgtilFKGQDLLELEPDE-RA-RAGLFLAFQYPEEIPGVSNLEFLRSALNA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKQEVK------KELVTEILTALGlMSCSHTRTAL---LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:TIGR01978 105 RRSARGEEPldlldfEKLLKEKLALLD-MDEEFLNRSVnegFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 240 VSLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKG 283
Cdd:TIGR01978 184 AEGINRLREPDRSFLIITHYQ--RLLNYIkpDYVHVLLDGRIVKSG 227
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
45-289 |
4.40e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.89 E-value: 4.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 45 TEAQRFSHLPKRSAVDIEF--VELSYSVREGPCwrkrgyktlLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESg 122
Cdd:PRK11176 326 QEKDEGKRVIERAKGDIEFrnVTFTYPGKEVPA---------LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDI- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 123 MKGQILVNG---RPRELRTFRKMSCYIMQDdmllPHL---TVLEAMMVSANLKLSEKQ---EVKKELVTEILTAL--GLM 191
Cdd:PRK11176 396 DEGEILLDGhdlRDYTLASLRNQVALVSQN----VHLfndTIANNIAYARTEQYSREQieeAARMAYAMDFINKMdnGLD 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 192 SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLaQGGRTIICTIHQPSAklFEMFDKL 271
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLST--IEKADEI 548
|
250
....*....|....*...
gi 215820660 272 YILSQGQCIFKGVVTNLI 289
Cdd:PRK11176 549 LVVEDGEIVERGTHAELL 566
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
96-258 |
6.78e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 66.65 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTF---MNIL--------------------AGYRESGMKGQILVNGRPRELRT---FRKMSCYIMQ- 148
Cdd:PRK13651 34 EFIAIIGQTGSGKTTFiehLNALllpdtgtiewifkdeknkkkTKEKEKVLEKLVIQKTRFKKIKKikeIRRRVGVVFQf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 149 DDMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEP 227
Cdd:PRK13651 114 AEYQLFEQTIEKDIIFGPVSMGVSKEEAKK-RAAKYIELVGLDESYLQRSPFeLSGGQKRRVALAGILAMEPDFLVFDEP 192
|
170 180 190
....*....|....*....|....*....|.
gi 215820660 228 TSGLDSASCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:PRK13651 193 TAGLDPQGVKEILEIFDNLNKQGKTIILVTH 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
91-254 |
8.89e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.83 E-value: 8.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 91 KFCRRELIGIMGPSGAGKSTF------MNIL-AGYResgMKGQILVNGR--------PRELRT-----FRK-----MSCY 145
Cdd:COG1117 33 DIPENKVTALIGPSGCGKSTLlrclnrMNDLiPGAR---VEGEILLDGEdiydpdvdVVELRRrvgmvFQKpnpfpKSIY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 146 imqDDmllphltvleammVSANLKLSE--KQEVKKELVTEILTALGL---------MScshtrtAL-LSGGQRKRLAIAL 213
Cdd:COG1117 110 ---DN-------------VAYGLRLHGikSKSELDEIVEESLRKAALwdevkdrlkKS------ALgLSGGQQQRLCIAR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTII 254
Cdd:COG1117 168 ALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIV 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
61-288 |
1.60e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 65.57 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPCWRKRGyktlLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG-------RP 133
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQA----IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKP-TTGTVTVDDitithktKD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 RELRTFRKMSCYIMQ--DDMLLPHLTVLEAMMVSANLKLSEKQevKKELVTEILTALG----LMSCSHTRtalLSGGQRK 207
Cdd:PRK13646 78 KYIRPVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDE--VKNYAHRLLMDLGfsrdVMSQSPFQ---MSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 208 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKGVVT 286
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN-EVARYADEVIVMKEGSIVSQTSPK 231
|
..
gi 215820660 287 NL 288
Cdd:PRK13646 232 EL 233
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
82-307 |
1.93e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAgyRESGMKGQILVNGRPR-----------ELRTFRKMSCYIMQDD 150
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLN--RMNELESEVRVEGRVEffnqniyerrvNLNRLRRQVSMVHPKP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 151 MLLPhLTVLEAMMVSANL----------KLSEKQEVKKELVTEILTALglmscsHTRTALLSGGQRKRLAIALELVNNPP 220
Cdd:PRK14258 98 NLFP-MSVYDNVAYGVKIvgwrpkleidDIVESALKDADLWDEIKHKI------HKSALDLSGGQQQRLCIARALAVKPK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 221 VMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQpsaklfemFDKLYILSQGQCIFKGvVTNLIPYLKGLGLHC 299
Cdd:PRK14258 171 VLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHN--------LHQVSRLSDFTAFFKG-NENRIGQLVEFGLTK 241
|
....*...
gi 215820660 300 PTYHNPAD 307
Cdd:PRK14258 242 KIFNSPHD 249
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
79-288 |
2.75e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.40 E-value: 2.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 79 RGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNG-------RPRELRTFRKMScYIMQDDM 151
Cdd:PRK11831 17 RGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD-HGEILFDGenipamsRSRLYTVRKRMS-MLFQSGA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 LLPHLTVLE--AMMVSANLKLSEkqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:PRK11831 95 LFTDMNVFDnvAYPLREHTQLPA--PLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 230 GLDSASCFQVVSLMKSLAQG-GRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 288
Cdd:PRK11831 173 GQDPITMGVLVKLISELNSAlGVTCVVVSHD-VPEVLSIADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
100-258 |
3.36e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.13 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQD---DMLLPHLTVLEAMMVSAN----LKLSE 172
Cdd:PRK15056 38 LVGVNGSGKSTLFKALMGFVRLA-SGKISILGQPTRQALQKNLVAYVPQSeevDWSFPVLVEDVVMMGRYGhmgwLRRAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 173 KQEvkKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRT 252
Cdd:PRK15056 117 KRD--RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKT 194
|
....*.
gi 215820660 253 IICTIH 258
Cdd:PRK15056 195 MLVSTH 200
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
100-258 |
3.83e-11 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 63.56 E-value: 3.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAgyRESGM-KGQILVNGRP------RELRtfRKMScyIM-QDDMLLPHLTVLEamMVS------ 165
Cdd:COG4604 32 LIGPNGAGKSTLLSMIS--RLLPPdSGEVLVDGLDvattpsRELA--KRLA--ILrQENHINSRLTVRE--LVAfgrfpy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 166 ANLKLSEKQEvkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 245
Cdd:COG4604 104 SKGRLTAEDR---EIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRR 180
|
170
....*....|....
gi 215820660 246 LAQG-GRTIICTIH 258
Cdd:COG4604 181 LADElGKTVVIVLH 194
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
95-258 |
3.87e-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: 65.98 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 95 RELIGIMGPSGAGKSTFMNILAGYRESgMKGQILV--------------NGRPRELRtfrkmscYI---MQDDMLLPHLT 157
Cdd:TIGR03269 310 GEIFGIVGTSGAGKTTLSKIIAGVLEP-TSGEVNVrvgdewvdmtkpgpDGRGRAKR-------YIgilHQEYDLYPHRT 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 VLEAMMVSANLKLSEKQEVKKELVTeiLTALGLmSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGL 231
Cdd:TIGR03269 382 VLDNLTEAIGLELPDELARMKAVIT--LKMVGF-DEEKAEEILdkypdeLSEGERHRVALAQVLIKEPRIVILDEPTGTM 458
|
170 180
....*....|....*....|....*...
gi 215820660 232 DSASCFQVV-SLMKSLAQGGRTIICTIH 258
Cdd:TIGR03269 459 DPITKVDVThSILKAREEMEQTFIIVSH 486
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
96-277 |
5.33e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 65.37 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG---RPRELRTFRKMSCYIMQDDMLL------------PHLT--- 157
Cdd:PRK13657 362 QTVAIVGPTGAGKSTLINLLQRVFDP-QSGRILIDGtdiRTVTRASLRRNIAVVFQDAGLFnrsiednirvgrPDATdee 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 VLEAMMVSANLKLSEKQEVKKElvteilTALGlmscshTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:PRK13657 441 MRAAAERAQAHDFIERKPDGYD------TVVG------ERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEA 508
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 215820660 238 QVVSLMKSLAQgGRTIICTIHQPS----AKLFEMFDKLYILSQG 277
Cdd:PRK13657 509 KVKAALDELMK-GRTTFIIAHRLStvrnADRILVFDNGRVVESG 551
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
96-254 |
5.91e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG--YRESGmkgQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVsA 166
Cdd:COG1129 279 EILGIAGLVGAGRTELARALFGadPADSG---EIRLDGKPVRIRSPRDAIragiAYVPEDrkgEGLVLDLSIRENITL-A 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLK-------LSEKQEvkKELVTEILTALGL-MSCSHTRTALLSGG-QRKrLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:COG1129 355 SLDrlsrgglLDRRRE--RALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK-VVLAKWLATDPKVLILDEPTRGIDVGAKA 431
|
170
....*....|....*..
gi 215820660 238 QVVSLMKSLAQGGRTII 254
Cdd:COG1129 432 EIYRLIRELAAEGKAVI 448
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
96-288 |
8.42e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.81 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRElRTFRKMSC-----YIMQDDMLLPHLTVLEAMMVSanlKL 170
Cdd:PRK09700 32 EIHALLGENGAGKSTLMKVLSGIHEP-TKGTITINNINYN-KLDHKLAAqlgigIIYQELSVIDELTVLENLYIG---RH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQ---------EVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 241
Cdd:PRK09700 107 LTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 215820660 242 LMKSLAQGGRTIICTIHQpSAKLFEMFDKLYILSQGQCIFKGVVTNL 288
Cdd:PRK09700 187 IMNQLRKEGTAIVYISHK-LAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
96-233 |
9.32e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 63.95 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYrESGMKGQILVNGR------PRElrtfRKMScYIMQDDMLLPHLTVLEAmmVSANLK 169
Cdd:PRK10851 29 QMVALLGPSGSGKTTLLRIIAGL-EHQTSGHIRFHGTdvsrlhARD----RKVG-FVFQHYALFRHMTVFDN--IAFGLT 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 170 LSEKQE-----VKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK10851 101 VLPRRErpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
96-282 |
1.25e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.20 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP-RELRTFRkmscyIMQDDM-LLPH-LTVLEAMMVSANLKL-- 170
Cdd:PRK11614 32 EIVTLIGANGAGKTTLLGTLCG-DPRATSGRIVFDGKDiTDWQTAK-----IMREAVaIVPEgRRVFSRMTVEENLAMgg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 --SEKQEVKK--ELVTEILTALglMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 246
Cdd:PRK11614 106 ffAERDQFQEriKWVYELFPRL--HERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 215820660 247 AQGGRTIIcTIHQPSAKLFEMFDKLYILSQGQCIFK 282
Cdd:PRK11614 184 REQGMTIF-LVEQNANQALKLADRGYVLENGHVVLE 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
80-258 |
1.38e-10 |
|
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: 59.77 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRelrtfrkmSCYIMQddmllphltvl 159
Cdd:cd03221 11 GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG-ELEPDEGIVTWGSTVK--------IGYFEQ----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 eammvsanlklsekqevkkelvteiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:cd03221 71 -----------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEAL 109
|
170
....*....|....*....
gi 215820660 240 VSLMKSLaQGgrTIICTIH 258
Cdd:cd03221 110 EEALKEY-PG--TVILVSH 125
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
100-259 |
1.41e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRPRELRT---FRKMSCYIM-QDDMLLPHLTVLEAMMvsanLKLSEKQE 175
Cdd:PRK15439 42 LLGGNGAGKSTLMKIIAGI-VPPDSGTLEIGGNPCARLTpakAHQLGIYLVpQEPLLFPNLSVKENIL----FGLPKRQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 176 VKKELvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIC 255
Cdd:PRK15439 117 SMQKM-KQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVF 195
|
....
gi 215820660 256 TIHQ 259
Cdd:PRK15439 196 ISHK 199
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
96-278 |
1.56e-10 |
|
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: 64.00 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRprELRTFRKMSC-----YIMQDDMLLPHlTVLE--AMMvsan 167
Cdd:COG4618 359 EVLGVIGPSGSGKSTLARLLVGvWPPTA--GSVRLDGA--DLSQWDREELgrhigYLPQDVELFDG-TIAEniARF---- 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 lklsekQEVKKELVTE----------IL-------TALGLMSCShtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSG 230
Cdd:COG4618 430 ------GDADPEKVVAaaklagvhemILrlpdgydTRIGEGGAR------LSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 231 LDSASCFQVVSLMKSLAQGGRTIICTIHQPSAkLFEMfDKLYILSQGQ 278
Cdd:COG4618 498 LDDEGEAALAAAIRALKARGATVVVITHRPSL-LAAV-DKLLVLRDGR 543
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
96-258 |
2.16e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 64.26 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRP--RELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEK 173
Cdd:TIGR01257 1966 ECFGLLGVNGAGKTTTFKMLTG-DTTVTSGDATVAGKSilTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 QEVKKeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 253
Cdd:TIGR01257 2045 EEIEK-VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV 2123
|
....*
gi 215820660 254 ICTIH 258
Cdd:TIGR01257 2124 VLTSH 2128
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
88-295 |
2.31e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.72 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 88 LSGKFCRRELIGIMGPSGAGKS-TFMNILAGYRESGMK---GQILVNGRPRELRTFRKMSCYIMQD----DM-------- 151
Cdd:PRK10261 35 LSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAGGLvqcDKMLLRRRSRQVIELSEQSAAQMRHvrgaDMamifqepm 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 152 --LLPHLTVLEAMMVSANLKLSEKQEvkkELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMF 223
Cdd:PRK10261 115 tsLNPVFTVGEQIAESIRLHQGASRE---EAMVEAKRMLDQVRIPEAQTILsryphqLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 224 FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIFKGVVTNLI-----PYLKGL 295
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFhapqhPYTRAL 268
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
60-278 |
2.52e-10 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 60.59 E-value: 2.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 60 DIEFVELSYSVREGPcwrkrgyKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILagYR-ESGMKGQILVNGRP----- 133
Cdd:cd03244 2 DIEFKNVSLRYRPNL-------PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLAL--FRlVELSSGSILIDGVDiskig 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 -RELRtfRKMSCyIMQDDMLL---------PHLTVLEAMMVSAnLKlsekqEVK-KELVTEILTALGLMSCShtRTALLS 202
Cdd:cd03244 73 lHDLR--SRISI-IPQDPVLFsgtirsnldPFGEYSDEELWQA-LE-----RVGlKEFVESLPGGLDTVVEE--GGENLS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 203 GGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSlAQGGRTIIC------TIHQpsaklfemFDKLYILSQ 276
Cdd:cd03244 142 VGQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTiahrldTIID--------SDRILVLDK 212
|
..
gi 215820660 277 GQ 278
Cdd:cd03244 213 GR 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
96-280 |
3.04e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 63.02 E-value: 3.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEAMMVSANL-- 168
Cdd:PRK13549 32 EIVSLCGENGAGKSTLMKVLSGvYPHGTYEGEIIFEGEELQASNIRdterAGIAIIHQELALVKELSVLENIFLGNEItp 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 -KLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:PRK13549 112 gGIMDYDAMYLR-AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLK 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 215820660 248 QGGRTIICTIHqpsaKLFEMF---DKLYILSQGQCI 280
Cdd:PRK13549 191 AHGIACIYISH----KLNEVKaisDTICVIRDGRHI 222
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
96-232 |
4.02e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 4.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKLSEKQE 175
Cdd:PRK13543 38 EALLVQGDNGAGKTTLLRVLAGLLHVE-SGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHGRRAKQ 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 176 VKkelvTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13543 117 MP----GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
96-257 |
4.60e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 61.66 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKS----TFMNILAGY-RESG---MKGQILVNGRPRELRTFR--KMScYIMQDDM--LLPHLTVLEAMM 163
Cdd:PRK09473 43 ETLGIVGESGSGKSqtafALMGLLAANgRIGGsatFNGREILNLPEKELNKLRaeQIS-MIFQDPMtsLNPYMRVGEQLM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSANL-KLSEKQEVKKELVtEILTALGlMSCSHTRTAL----LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQ 238
Cdd:PRK09473 122 EVLMLhKGMSKAEAFEESV-RMLDAVK-MPEARKRMKMypheFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQ 199
|
170
....*....|....*....
gi 215820660 239 VVSLMKSLAQGGRTIICTI 257
Cdd:PRK09473 200 IMTLLNELKREFNTAIIMI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
85-233 |
5.30e-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: 60.11 E-value: 5.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVngrprELRTFRKMSCYIMQD-DMllphlTVLEAMM 163
Cdd:cd03237 15 LEVEGGSISESEVIGILGPNGIGKTTFIKMLAG-VLKPDEGDIEI-----ELDTVSYKPQYIKADyEG-----TVRDLLS 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:cd03237 84 SITKDFYTHPY-----FKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
94-278 |
5.68e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 5.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGRPRELRTFRKMS----CYIMQD---DMLLPHLTVLEAMMVSA 166
Cdd:PRK13549 287 RGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQAIaqgiAMVPEDrkrDGIVPVMGVGKNITLAA 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSEKQEVKKEL-VTEILTALGLM----SCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVS 241
Cdd:PRK13549 367 LDRFTGGSRIDDAAeLKTILESIQRLkvktASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 215820660 242 LMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 278
Cdd:PRK13549 447 LINQLVQQGVAIIVI----SSELPEvlgLSDRVLVMHEGK 482
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
82-283 |
7.59e-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: 61.74 E-value: 7.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVN----------------GRP----------- 133
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyEPTSGRIIYHvalcekcgyverpskvGEPcpvcggtlepe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 ---------RELRTFRKMSCYIMQDDM-LLPHLTVLEAMMVSanlkLSEKQEVKKELVTEILTALGLMSCSHTRTAL--- 200
Cdd:TIGR03269 93 evdfwnlsdKLRRRIRKRIAIMLQRTFaLYGDDTVLDNVLEA----LEEIGYEGKEAVGRAVDLIEMVQLSHRITHIard 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG-GRTIICTIHQPSAkLFEMFDKLYILSQGQC 279
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEV-IEDLSDKAIWLENGEI 247
|
....
gi 215820660 280 IFKG 283
Cdd:TIGR03269 248 KEEG 251
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
96-280 |
8.21e-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: 61.76 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGMKGQILVNGRPRELR----TFRKMSCYIMQDDMLLPHLTVLEAMMVSANLKL 170
Cdd:TIGR02633 28 ECVGLCGENGAGKSTLMKILSGvYPHGTWDGEIYWSGSPLKASnirdTERAGIVIIHQELTLVPELSVAENIFLGNEITL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SEKQEVKKELV---TEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 246
Cdd:TIGR02633 108 PGGRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 215820660 247 AQGGRTIICTIHqpsaKLFE---MFDKLYILSQGQCI 280
Cdd:TIGR02633 188 KAHGVACVYISH----KLNEvkaVCDTICVIRDGQHV 220
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
81-278 |
9.36e-10 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 61.36 E-value: 9.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 81 YKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkmscyimqddMLLPHltvlE 160
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG-SGRIA---RPAGARV------------LFLPQ----R 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLK--LS---EKQEVKKELVTEILTALGLmscSHTRTAL---------LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:COG4178 435 PYLPLGTLReaLLypaTAEAFSDAELREALEAVGL---GHLAERLdeeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215820660 227 PTSGLDSASCFQVVSLMKSLAQGGrTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:COG4178 512 ATSALDEENEAALYQLLREELPGT-TVISVGHRST--LAAFHDRVLELTGDG 560
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
96-258 |
1.05e-09 |
|
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: 59.69 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRTFRKMscyIMQDDM----------LLPHLT 157
Cdd:cd03236 27 QVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDEFRGSELQNYFTK---LLEGDVkvivkpqyvdLIPKAV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 vleAMMVSANLKLSEKQEVKKELVTeiltALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCF 237
Cdd:cd03236 104 ---KGKVGELLKKKDERGKLDELVD----QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRL 176
|
170 180
....*....|....*....|.
gi 215820660 238 QVVSLMKSLAQGGRTIICTIH 258
Cdd:cd03236 177 NAARLIRELAEDDNYVLVVEH 197
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
96-278 |
1.06e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.17 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGY--RESGmkgQILVNGRPRELRT----FRKMSCYIMQD---DMLLPHLTVLEAMMVSA 166
Cdd:PRK10762 279 EILGVSGLMGAGRTELMKVLYGAlpRTSG---YVTLDGHEVVTRSpqdgLANGIVYISEDrkrDGLVLGMSVKENMSLTA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSE-----KQEVKKELVTEILTALGLMSCSHTRT-ALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK10762 356 LRYFSRaggslKHADEQQAVSDFIRLFNIKTPSMEQAiGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIY 435
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 215820660 241 SLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 278
Cdd:PRK10762 436 QLINQFKAEGLSIILV----SSEMPEvlgMSDRILVMHEGR 472
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
80-256 |
1.14e-09 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 59.40 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTF------MNILAgyRESGMKGQILVNGR----PR----ELRTFRKMscy 145
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsinrMNDLN--PEVTITGSIVYNGHniysPRtdtvDLRKEIGM--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 146 IMQDDMLLPhLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTR---TAL-LSGGQRKRLAIALELVNNPPV 221
Cdd:PRK14239 91 VFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRlhdSALgLSGGQQQRVCIARVLATSPKI 169
|
170 180 190
....*....|....*....|....*....|....*
gi 215820660 222 MFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICT 256
Cdd:PRK14239 170 ILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT 204
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
431-644 |
1.29e-09 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 58.29 E-value: 1.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 431 MLFLMFAALMPTVLTFplemaVFMREHLNYWY------SLKAYYLAKTMADVPFQVVCPVVYCSIVYWMTGQPAETSRFL 504
Cdd:COG0842 11 AMSLLFTALMLTALSI-----AREREQGTLERllvtpvSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVPLRGLSLL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 505 LFSALATATALVAQSLGLLIGAASNSLQVATFVGPVTAIPVLLFSGFFVSFKTIPTYLQWSSYLSYVRYGFEGViltiyg 584
Cdd:COG0842 86 LLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL------ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 585 meRGdltcleercpfrepqSILRALDVEDakLYMDFLVLGIFFLALRLLAYLVLRYRVKS 644
Cdd:COG0842 160 --RA---------------LFLGGAGLAD--VWPSLLVLLAFAVVLLALALRLFRRRLRG 200
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
96-232 |
1.36e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.17 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQILVNGRPRELRTFRKMS------------CYIMQD--DMLlphltvleA 161
Cdd:PRK11701 33 EVLGIVGESGSGKTTLLNALSA-RLAPDAGEVHYRMRDGQLRDLYALSeaerrrllrtewGFVHQHprDGL--------R 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 162 MMVSANLKLSEKqevkkelvteiLTALGLMSCSHTR-TAL-------------------LSGGQRKRLAIALELVNNPPV 221
Cdd:PRK11701 104 MQVSAGGNIGER-----------LMAVGARHYGDIRaTAGdwlerveidaariddlpttFSGGMQQRLQIARNLVTHPRL 172
|
170
....*....|.
gi 215820660 222 MFFDEPTSGLD 232
Cdd:PRK11701 173 VFMDEPTGGLD 183
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
163-303 |
1.62e-09 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 60.13 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:NF000106 109 MIGR*LDLSRKD--ARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDE 186
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 243 MKSLAQGGRTIICTIhQPSAKLFEMFDKLYILSQGQCIFKGVVTNLIPYLKGLGLHCPTYH 303
Cdd:NF000106 187 VRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIRPAH 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
68-248 |
1.71e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 68 YSVREGPCWRKRgyktLLKCLSG-KFC--RRELIGIMGPSGAGKSTFMNILAGYRE--SG---MKGQILVNGRPRELRTF 139
Cdd:PRK11308 15 YPVKRGLFKPER----LVKALDGvSFTleRGKTLAVVGESGCGKSTLARLLTMIETptGGelyYQGQDLLKADPEAQKLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 140 RKMSCYIMQDDM--LLPHLTV---LEAMMVsANLKLSEKQevKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAIAL 213
Cdd:PRK11308 91 RQKIQIVFQNPYgsLNPRKKVgqiLEEPLL-INTSLSAAE--RREKALAMMAKVGLRPEHYDRYPhMFSGGQRQRIAIAR 167
|
170 180 190
....*....|....*....|....*....|....*
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ 248
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQ 202
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
54-300 |
1.94e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 59.04 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 54 PKRSAVDIEFVELSYSVREGPcwrkrgyktLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGY--RESGMKGQILVNG 131
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSKKP---------ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllPDDNPNSKITVDG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 132 RPRELRTF---RKMSCYIMQD-DMLLPHLTVLEAMMVSANLKLSEKQEVKKeLVTEILTALGLMSCSHTRTALLSGGQRK 207
Cdd:PRK13640 72 ITLTAKTVwdiREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIK-IVRDVLADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 208 RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA-QGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKGVVT 286
Cdd:PRK13640 151 RVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEA--NMADQVLVLDDGKLLAQGSPV 228
|
250
....*....|....*..
gi 215820660 287 NLIP---YLKGLGLHCP 300
Cdd:PRK13640 229 EIFSkveMLKEIGLDIP 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
82-300 |
2.49e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 58.56 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 82 KTLLKCLSGKFCRRELIGIMGPSGAGKSTF---MNILAGYREsgmkGQILVNG----RPRELRTFRKMSCYIMQ--DDML 152
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALLIPSE----GKVYVDGldtsDEENLWDIRNKAGMVFQnpDNQI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 153 LPhlTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13633 99 VA--TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 233 SASCFQVVSLMKSL-AQGGRTIICTIH--QPSAKLfemfDKLYILSQGQCIFKGVVTNL---IPYLKGLGLHCP 300
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHymEEAVEA----DRIIVMDSGKVVMEGTPKEIfkeVEMMKKIGLDVP 246
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
100-300 |
2.62e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 58.61 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGRP---RELRTFRKMSCYIMQDDmllphltvlEAMMVSANLKLS----- 171
Cdd:PRK13648 40 IVGHNGSGKSTIAKLMIGI-EKVKSGEIFYNNQAitdDNFEKLRKHIGIVFQNP---------DNQFVGSIVKYDvafgl 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 172 EKQEVK----KELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLA 247
Cdd:PRK13648 110 ENHAVPydemHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVK 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 248 QGGR-TIICTIHQPSAKLFEmfDKLYILSQGQCIFKGVVTNLIPYLKGL---GLHCP 300
Cdd:PRK13648 190 SEHNiTIISITHDLSEAMEA--DHVIVMNKGTVYKEGTPTEIFDHAEELtriGLDLP 244
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
100-283 |
2.89e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 57.15 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAG---YRESgmKGQILVNGR-----PRELRTfrKMSCYIM-QDDMLLPHLTVLEaMMVSANLKL 170
Cdd:cd03217 31 LMGPNGSGKSTLAKTIMGhpkYEVT--EGEILFKGEditdlPPEERA--RLGIFLAfQYPPEIPGVKNAD-FLRYVNEGF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SekqevkkelvteiltalglmscshtrtallsGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGG 250
Cdd:cd03217 106 S-------------------------------GGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEG 154
|
170 180 190
....*....|....*....|....*....|....*
gi 215820660 251 RTIICTIHQpsAKLFEMF--DKLYILSQGQCIFKG 283
Cdd:cd03217 155 KSVLIITHY--QRLLDYIkpDRVHVLYDGRIVKSG 187
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
58-233 |
3.04e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.12 E-value: 3.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 58 AVDIEFVELSYsvregpcwrkRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPREL- 136
Cdd:PRK10790 340 RIDIDNVSFAY----------RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYY-PLTEGEIRLDGRPLSSl 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 137 --RTFRKMSCYIMQDDMLLphltvleAMMVSANLKLSekQEVKKELVTEILTALGLMSCS-------HTRTA----LLSG 203
Cdd:PRK10790 409 shSVLRQGVAMVQQDPVVL-------ADTFLANVTLG--RDISEEQVWQALETVQLAELArslpdglYTPLGeqgnNLSV 479
|
170 180 190
....*....|....*....|....*....|
gi 215820660 204 GQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK10790 480 GQKQLLALARVLVQTPQILILDEATANIDS 509
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
98-254 |
3.06e-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: 59.80 E-value: 3.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 98 IGIMGPSGAGKSTFMNILAGyresgmkgQILVN-GRPRE-------LRTFRKMscyIMQDdmllpHLTVLeammVSANLK 169
Cdd:COG1245 102 TGILGPNGIGKSTALKILSG--------ELKPNlGDYDEepswdevLKRFRGT---ELQD-----YFKKL----ANGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEK-QEVK----------KEL---------VTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:COG1245 162 VAHKpQYVDlipkvfkgtvRELlekvdergkLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSS 241
|
170 180
....*....|....*....|....*
gi 215820660 230 GLDSASCFQVVSLMKSLAQGGRTII 254
Cdd:COG1245 242 YLDIYQRLNVARLIRELAEEGKYVL 266
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
94-278 |
4.74e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.22 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLTVleammvsanlk 169
Cdd:PRK10522 348 RGELLFLIGGNGSGKSTLAMLLTGlYQPQ--SGEILLDGKPvtaEQPEDYRKLFSAVFTDFHLFDQLLG----------- 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 lSEKQEVKKELVTEILTALGL---MSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSglDSASCFQVV---S 241
Cdd:PRK10522 415 -PEGKPANPALVEKWLERLKMahkLELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA--DQDPHFRREfyqV 491
|
170 180 190
....*....|....*....|....*....|....*..
gi 215820660 242 LMKSLAQGGRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:PRK10522 492 LLPLLQEMGKTIFAISHDDH--YFIHADRLLEMRNGQ 526
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
100-279 |
5.31e-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: 55.62 E-value: 5.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYRESGmKGQIlvnGRPRELRTFrkmscYIMQddmllphltvlEAMMVSANLKlsekqevkke 179
Cdd:cd03223 32 ITGPSGTGKSSLFRALAGLWPWG-SGRI---GMPEGEDLL-----FLPQ-----------RPYLPLGTLR---------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 180 lvtEILtalglmscSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLaqgGRTIICTIHQ 259
Cdd:cd03223 82 ---EQL--------IYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKEL---GITVISVGHR 147
|
170 180
....*....|....*....|.
gi 215820660 260 PS-AKLFEMfdKLYILSQGQC 279
Cdd:cd03223 148 PSlWKFHDR--VLDLDGEGGW 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
96-226 |
6.14e-09 |
|
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: 59.04 E-value: 6.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRP---RELRTFRKMSCYIMQDDMLLPHLtvleammvsanlkLS 171
Cdd:COG4615 359 ELVFIVGGNGSGKSTLAKLLTGlYRPES--GEILLDGQPvtaDNREAYRQLFSAVFSDFHLFDRL-------------LG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 215820660 172 EKQEVKKELVTEILTALGLmscSH---------TRTALlSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:COG4615 424 LDGEADPARARELLERLEL---DHkvsvedgrfSTTDL-SQGQRKRLALLVALLEDRPILVFDE 483
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
60-235 |
6.34e-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: 56.27 E-value: 6.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 60 DIEFVELSysVREGPcwrkrGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRES-GMKGQILVNGRP----- 133
Cdd:cd03369 6 EIEVENLS--VRYAP-----DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTL--ILALFRFLeAEEGKIEIDGIDistip 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 134 -RELRtfRKMSCyIMQDDMLLphltvleAMMVSANLKLSEKQEVKkelvtEILTALGLMSCSHTrtalLSGGQRKRLAIA 212
Cdd:cd03369 77 lEDLR--SSLTI-IPQDPTLF-------SGTIRSNLDPFDEYSDE-----EIYGALRVSEGGLN----LSQGQRQLLCLA 137
|
170 180
....*....|....*....|...
gi 215820660 213 LELVNNPPVMFFDEPTSGLDSAS 235
Cdd:cd03369 138 RALLKRPRVLVLDEATASIDYAT 160
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
94-264 |
7.20e-09 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 7.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGMKGQILVNGrprelrtfrkmscyimqddmllphltvleammvsanlklsek 173
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 174 qevkkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS------CFQVVSLMKSLA 247
Cdd:smart00382 39 -----EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllLEELRLLLLLKS 113
|
170
....*....|....*..
gi 215820660 248 QGGRTIICTIHQPSAKL 264
Cdd:smart00382 114 EKNLTVILTTNDEKDLG 130
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
99-288 |
7.40e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 7.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 99 GIMGPSGAGKSTFMNILAG-YRESGmkGQILVNGRPRelrTFR--KMS-----CYIMQDDMLLPHLTVLEammvsaNLKL 170
Cdd:PRK10762 34 ALVGENGAGKSTMMKVLTGiYTRDA--GSILYLGKEV---TFNgpKSSqeagiGIIHQELNLIPQLTIAE------NIFL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 171 SekQEVK--------KELVTE---ILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSASC 236
Cdd:PRK10762 103 G--REFVnrfgridwKKMYAEadkLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtdtETESL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 237 FQVVSLMKslAQGgrtiiCTIHQPSAKLFEMF---DKLYILSQGQCIFKGVVTNL 288
Cdd:PRK10762 181 FRVIRELK--SQG-----RGIVYISHRLKEIFeicDDVTVFRDGQFIAEREVADL 228
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
96-246 |
1.09e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGR------PRELRTFRKMSCYIMQDDM--LLPHLTVLEAMMVSAN 167
Cdd:PRK10261 351 ETLSLVGESGSGKSTTGRALLRLVES-QGGEIIFNGQridtlsPGKLQALRRDIQFIFQDPYasLDPRQTVGDSIMEPLR 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 168 LKLSEKQEVKKELVTEILTALGLMSCSHTRTA-LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL 246
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLLERVGLLPEHAWRYPhEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
61-283 |
1.17e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 56.72 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 61 IEFVELSYSVREGPCWRKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPRELRTFR 140
Cdd:PRK15112 5 LEVRNLSKTFRYRTGWFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPT-SGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 141 KMSC---YIMQD--DMLLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGLMScSHTR--TALLSGGQRKRLAIAL 213
Cdd:PRK15112 84 YRSQrirMIFQDpsTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLP-DHASyyPHMLAPGQKQRLGLAR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 214 ELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSL--AQGGRTIICTIHQPSAKlfEMFDKLYILSQGQCIFKG 283
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMK--HISDQVLVMHQGEVVERG 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
89-254 |
1.20e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.87 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 89 SGKFCRRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQD-DMllphlTVLEAMMV 164
Cdd:COG1245 360 GGEIREGEVLGIVGPNGIGKTTFAKILAGVLKpdEGeVDEDLKISYKPQ----------YISPDyDG-----TVEEFLRS 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 SANLKLSEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMK 244
Cdd:COG1245 425 ANTDDFGSSY-----YKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 499
|
170
....*....|.
gi 215820660 245 SLAQG-GRTII 254
Cdd:COG1245 500 RFAENrGKTAM 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
98-258 |
1.20e-08 |
|
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: 58.02 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 98 IGIMGPSGAGKSTFMNILAGyresgMKGQILVNGRPRELRTFRkmscYIMQDDMLLPHLTVLEAMM-------------- 163
Cdd:TIGR03719 34 IGVLGLNGAGKSTLLRIMAG-----VDKDFNGEARPQPGIKVG----YLPQEPQLDPTKTVRENVEegvaeikdaldrfn 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 -VSANL--------KLSEKQEvkkELvTEILTALGLMSCSHT---------------RTALLSGGQRKRLAIALELVNNP 219
Cdd:TIGR03719 105 eISAKYaepdadfdKLAAEQA---EL-QEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 215820660 220 PVMFFDEPTSGLDSAScfqVVSLMKSLAQGGRTIICTIH 258
Cdd:TIGR03719 181 DMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTH 216
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
91-283 |
1.26e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.55 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 91 KFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNG--------RPRELRTFRKMSCYIMQDDMLLPHLTVLEAM 162
Cdd:PRK13645 33 TFKKNKVTCVIGTTGSGKSTMIQLTNGLIIS-ETGQTIVGDyaipanlkKIKEVKRLRKEIGLVFQFPEYQLFQETIEKD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLKLSE-KQEVKKElVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK13645 112 IAFGPVNLGEnKQEAYKK-VPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFI 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 215820660 241 SLMKSLAQG-GRTIICTIHQPSaKLFEMFDKLYILSQGQCIFKG 283
Cdd:PRK13645 191 NLFERLNKEyKKRIIMVTHNMD-QVLRIADEVIVMHEGKVISIG 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
98-249 |
1.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 98 IGIMGPSGAGKSTFMNILAG--------YRESGMKGQILVNGRPRELRT-FRKMSC----------YImqdDmLLPHL-- 156
Cdd:PRK13409 102 TGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKRFRGTELQNyFKKLYNgeikvvhkpqYV---D-LIPKVfk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 157 -TVLEAmmvsanLKLSEKQEVKKELVTEiltaLGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:PRK13409 178 gKVREL------LKKVDERGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170
....*....|....
gi 215820660 236 CFQVVSLMKSLAQG 249
Cdd:PRK13409 248 RLNVARLIRELAEG 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
84-259 |
1.34e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 55.34 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 84 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR--PRELRTFRKMSCYIMQDDMLLPHLTVLE 160
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGlLNPE--KGEILFERQsiKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKLSEKQevkkelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK13540 94 NCLYDIHFSPGAVG------ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 215820660 241 SLMKSLAQGGRTIICTIHQ 259
Cdd:PRK13540 168 TKIQEHRAKGGAVLLTSHQ 186
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
94-248 |
1.40e-08 |
|
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: 57.77 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKS-TFMNI--LAGYRESGMKGQILVNGR------PRELRTFR--KMSCyIMQDDM--LLPHLTVle 160
Cdd:COG4172 35 AGETLALVGESGSGKSvTALSIlrLLPDPAAHPSGSILFDGQdllglsERELRRIRgnRIAM-IFQEPMtsLNPLHTI-- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 ammvsanlklsEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFF 224
Cdd:COG4172 112 -----------GKQiaEVlrlhrglsGAAARARALELLERVGIPDPERRLdayphqLSGGQRQRVMIAMALANEPDLLIA 180
|
170 180
....*....|....*....|....*..
gi 215820660 225 DEPTSGLD---SAscfQVVSLMKSLAQ 248
Cdd:COG4172 181 DEPTTALDvtvQA---QILDLLKDLQR 204
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
78-283 |
1.43e-08 |
|
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: 55.62 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 78 KRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGRPR---ELRTFrkmscyimqddmLL 153
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGiYPPD--SGTVTVRGRVSsllGLGGG------------FN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 154 PHLTVLE-AMMVSANLKLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:cd03220 97 PELTGREnIYLNGRLLGLSRKE--IDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 215820660 233 SAscFQ--VVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:cd03220 175 AA--FQekCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
96-232 |
2.95e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyrESGM-KGQI-----LVNGR-----PRE-------------------LRTFRKMSCY 145
Cdd:PRK11147 30 ERVCLVGRNGAGKSTLMKILNG--EVLLdDGRIiyeqdLIVARlqqdpPRNvegtvydfvaegieeqaeyLKRYHDISHL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 146 IMQD--DMLLPHLTVLEAMMVSANLKLSEKQevkkelVTEILTALGLMScsHTRTALLSGGQRKRLAIALELVNNPPVMF 223
Cdd:PRK11147 108 VETDpsEKNLNELAKLQEQLDHHNLWQLENR------INEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNPDVLL 179
|
....*....
gi 215820660 224 FDEPTSGLD 232
Cdd:PRK11147 180 LDEPTNHLD 188
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
96-260 |
3.18e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGyRESGMKGQilvngrprelrtfrkmSCYIMQDDMLLPHLTVLEAmmvsanlkLSEKQE 175
Cdd:COG2401 57 EIVLIVGASGSGKSTLLRLLAG-ALKGTPVA----------------GCVDVPDNQFGREASLIDA--------IGRKGD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 176 VKkeLVTEILTALGLMSCS--HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQ-GGRT 252
Cdd:COG2401 112 FK--DAVELLNAVGLSDAVlwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGIT 189
|
....*...
gi 215820660 253 IICTIHQP 260
Cdd:COG2401 190 LVVATHHY 197
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
100-232 |
3.57e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYrESGMKGQILVNGR---PRELRTF-----RKMScYIMQDDMLLPHLTVleammvSANLKLS 171
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGL-TRPQKGRIVLNGRvlfDAEKGIClppekRRIG-YVFQDARLFPHYKV------RGNLRYG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 172 EKqEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK11144 101 MA-KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
84-278 |
4.80e-08 |
|
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: 53.63 E-value: 4.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 84 LLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyrESG-MKGQILVNGRprelrtfrkMScYIMQddmllphltvlEAM 162
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG--ELEkLSGSVSVPGS---------IA-YVSQ-----------EPW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 MVSANLK-----LSEKQEVKKELV---------TEILTAlGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPT 228
Cdd:cd03250 77 IQNGTIRenilfGKPFDEERYEKVikacalepdLEILPD-GDLTEIGEKGINLSGGQKQRISLARAVYSDADIYLLDDPL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 229 SGLDSascfQVVS-LMKSLAQG----GRTIICTIHQPSakLFEMFDKLYILSQGQ 278
Cdd:cd03250 156 SAVDA----HVGRhIFENCILGlllnNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
96-286 |
5.73e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 54.26 E-value: 5.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRE-SGMKGQILVNGR-----PRELRTfrKMSCYI-MQDDMLLPHLTVLEAMMVSANL 168
Cdd:CHL00131 34 EIHAIMGPNGSGKSTLSKVIAGHPAyKILEGDILFKGEsildlEPEERA--HLGIFLaFQYPIEIPGVSNADFLRLAYNS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKQEVKK------ELVTEILTALGLMSCSHTRTAL--LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:CHL00131 112 KRKFQGLPELdpleflEIINEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 241 SLMKSLAQGGRTIICTIHQPsaKLFEMF--DKLYILSQGQCIFKGVVT 286
Cdd:CHL00131 192 EGINKLMTSENSIILITHYQ--RLLDYIkpDYVHVMQNGKIIKTGDAE 237
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
100-259 |
7.74e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 54.26 E-value: 7.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYRESgMKGQI------LVNG-RPRELRTFRKMSCYIMQddmlLPHLTVLEAMMVS------A 166
Cdd:PRK13634 38 IIGHTGSGKSTLLQHLNGLLQP-TSGTVtigervITAGkKNKKLKPLRKKVGIVFQ----FPEHQLFEETVEKdicfgpM 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 167 NLKLSEKQevKKELVTEILTALGLMSCSHTRTAL-LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKS 245
Cdd:PRK13634 113 NFGVSEED--AKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYK 190
|
170
....*....|....*
gi 215820660 246 LAQ-GGRTIICTIHQ 259
Cdd:PRK13634 191 LHKeKGLTTVLVTHS 205
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
201-274 |
1.26e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 51.59 E-value: 1.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 215820660 201 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPsaKLFEMFDKLYIL 274
Cdd:cd03227 78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLP--ELAELADKLIHI 153
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
94-232 |
1.35e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRE--SG-MKGQILVNGRPRelrtfrkmscYIMQDdmllPHLTVlEAMMVSANLKL 170
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAGVLKpdEGeVDPELKISYKPQ----------YIKPD----YDGTV-EDLLRSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 171 SEKQevkkeLVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK13409 429 GSSY-----YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
94-248 |
2.06e-07 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 52.78 E-value: 2.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKS----TFMNIL-AGYRESGmkGQILVNGRPRELRTFR-KMSCYIMQD--DMLLPHLTVleAMMVS 165
Cdd:PRK10418 28 RGRVLALVGGSGSGKSltcaAALGILpAGVRQTA--GRVLLDGKPVAPCALRgRKIATIMQNprSAFNPLHTM--HTHAR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 166 ANLKLSEKQEVKKELVtEILTALGLmscSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:PRK10418 104 ETCLALGKPADDATLT-AALEAVGL---ENAARVLklypfeMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARI 179
|
....*....
gi 215820660 240 VSLMKSLAQ 248
Cdd:PRK10418 180 LDLLESIVQ 188
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
201-254 |
2.17e-07 |
|
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: 54.06 E-value: 2.17e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTII 254
Cdd:COG5265 495 LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLV 548
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
96-248 |
2.37e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKS-TFMNIL-------AGYRESGMK--GQILVNGRPRELRTFR--KMScYIMQDDMllphltvleamm 163
Cdd:PRK15134 36 ETLALVGESGSGKSvTALSILrllpsppVVYPSGDIRfhGESLLHASEQTLRGVRgnKIA-MIFQEPM------------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 VSAN-LKLSEKQ--EV--------KKELVTEILTALGLMSCSHTRTAL------LSGGQRKRLAIALELVNNPPVMFFDE 226
Cdd:PRK15134 103 VSLNpLHTLEKQlyEVlslhrgmrREAARGEILNCLDRVGIRQAAKRLtdyphqLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180
....*....|....*....|..
gi 215820660 227 PTSGLDSASCFQVVSLMKSLAQ 248
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQ 204
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
77-283 |
3.39e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 52.01 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 77 RKRGYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAG-YRESgmKGQILVNGR---PRELRTfrkmscyIMQddml 152
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGiLEPT--SGRVEVNGRvsaLLELGA-------GFH---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 153 lPHLTVLE-AMMVSANLKLSeKQEVkKELVTEIL--TALG--LmscsHT--RTalLSGGQRKRLAIALELVNNPPVMFFD 225
Cdd:COG1134 101 -PELTGREnIYLNGRLLGLS-RKEI-DEKFDEIVefAELGdfI----DQpvKT--YSSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 226 EPTSGLDSAscFQ--VVSLMKSLAQGGRTIICTIHQPSAkLFEMFDKLYILSQGQCIFKG 283
Cdd:COG1134 172 EVLAVGDAA--FQkkCLARIRELRESGRTVIFVSHSMGA-VRRLCDRAIWLEKGRLVMDG 228
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
80-258 |
4.00e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 51.91 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYReSGMKGQILVNGRPRELRTFRKMSCYI--MQDDMLLPHLT 157
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM-TPAHGHVWLDGEHIQHYASKEVARRIglLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 158 VLEAMMVSANLK----LSEKQEVKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PRK10253 97 TVQELVARGRYPhqplFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176
|
170 180
....*....|....*....|....*.
gi 215820660 234 ASCFQVVSLMKSL-AQGGRTIICTIH 258
Cdd:PRK10253 177 SHQIDLLELLSELnREKGYTLAAVLH 202
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
96-278 |
5.97e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 51.66 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPR------ELRtfRKMSCYIMQDDMLLPHLTVLEAMMVSANLK 169
Cdd:PRK13650 34 EWLSIIGHNGSGKSTTVRLIDGLLEAE-SGQIIIDGDLLteenvwDIR--HKIGMVFQNPDNQFVGATVEDDVAFGLENK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKkELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:PRK13650 111 GIPHEEMK-ERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDD 189
|
170 180 190
....*....|....*....|....*....|..
gi 215820660 250 -GRTIICTIHQpsakLFE--MFDKLYILSQGQ 278
Cdd:PRK13650 190 yQMTVISITHD----LDEvaLSDRVLVMKNGQ 217
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
201-267 |
6.76e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 51.32 E-value: 6.76e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQgGRTIICTIH--QPSAKLFEM 267
Cdd:PRK14243 152 LSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKE-QYTIIIVTHnmQQAARVSDM 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
100-232 |
1.87e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 100 IMGPSGAGKSTFMNILAGYRESGmKGQILvngRPRELRTfrkmsCYIMQD---DMLLPhLTVLEAMMVSANlklsekqeV 176
Cdd:PRK09544 35 LLGPNGAGKSTLVRVVLGLVAPD-EGVIK---RNGKLRI-----GYVPQKlylDTTLP-LTVNRFLRLRPG--------T 96
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 177 KKElvtEILTALGLMSCSHTRTA---LLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:PRK09544 97 KKE---DILPALKRVQAGHLIDApmqKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
96-258 |
1.94e-06 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 50.01 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAG--YRESGMkgqILVNGRPRELRT---FRKMSCYIMQD-DMLLPHLTV-------LEam 162
Cdd:PRK13635 34 EWVAIVGHNGSGKSTLAKLLNGllLPEAGT---ITVGGMVLSEETvwdVRRQVGMVFQNpDNQFVGATVqddvafgLE-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 163 mvsaNLKLSEKQEVKKelVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSL 242
Cdd:PRK13635 109 ----NIGVPREEMVER--VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLET 182
|
170
....*....|....*..
gi 215820660 243 MKSL-AQGGRTIICTIH 258
Cdd:PRK13635 183 VRQLkEQKGITVLSITH 199
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
96-283 |
2.49e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRPrelrtfrkmsCYIMQDDMLLPHLTVLEAM------MVSANLK 169
Cdd:PRK10789 342 QMLGICGPTGSGKSTLLSLIQRHFDVS-EGDIRFHDIP----------LTKLQLDSWRSRLAVVSQTpflfsdTVANNIA 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 LSEKQEVKKEL--------VTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQV 239
Cdd:PRK10789 411 LGRPDATQQEIehvarlasVHDDILRLpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQI 490
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 215820660 240 vslMKSLAQGG--RTIICTIHQPSAkLFEMfDKLYILSQGQCIFKG 283
Cdd:PRK10789 491 ---LHNLRQWGegRTVIISAHRLSA-LTEA-SEILVMQHGHIAQRG 531
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
90-251 |
3.41e-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: 47.95 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 90 GKFCRRELIGIMGPSGAGKSTFMNILAGYREsgmkgqilvngrPRElrtfrkmscyimqDDMLLPHLTVLeammvsanlk 169
Cdd:cd03222 20 GVVKEGEVIGIVGPNGTGKTTAVKILAGQLI------------PNG-------------DNDEWDGITPV---------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 170 lsekqeVKKELVTeiltalglmscshtrtalLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQG 249
Cdd:cd03222 65 ------YKPQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
|
..
gi 215820660 250 GR 251
Cdd:cd03222 121 GK 122
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
85-246 |
3.55e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 48.94 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRPRELRTF----RKMSCYIMQDDMLLPHLTVLE 160
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE-FEGKVKIDGELLTAENVwnlrRKIGMVFQNPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 161 AMMVSANLKLSEKQEVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV 240
Cdd:PRK13642 102 DVAFGMENQGIPREEMIKR-VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180
|
....*.
gi 215820660 241 SLMKSL 246
Cdd:PRK13642 181 RVIHEI 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
63-278 |
4.06e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 49.66 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 63 FVELSYSVREGpcwrkrgyktllkclsgkfcrrELIGIMGPSGAGKSTFMNILAGYRESgMKGQILVNGRprelrTFRKM 142
Cdd:PRK15439 279 FRNISLEVRAG----------------------EILGLAGVVGAGRTELAETLYGLRPA-RGGRIMLNGK-----EINAL 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 143 SCYIMQDDML--LP-----HLTVLEAMM---VSA------NLKLSEKQEvkKELVTEILTALGLmSCSHTRTAL--LSGG 204
Cdd:PRK15439 331 STAQRLARGLvyLPedrqsSGLYLDAPLawnVCAlthnrrGFWIKPARE--NAVLERYRRALNI-KFNHAEQAArtLSGG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 215820660 205 QRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTihqpSAKLFE---MFDKLYILSQGQ 278
Cdd:PRK15439 408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFI----SSDLEEieqMADRVLVMHQGE 480
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
80-232 |
4.56e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.55 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 80 GYKTLLKCLSGKFCRRELIGIMGPSGAGKSTFMNILAGyRESGMKGQIlvngrprELRTFRKMSCYIMQDDMLLPHLTVL 159
Cdd:TIGR03719 333 GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG-QEQPDSGTI-------EIGETVKLAYVDQSRDALDPNKTVW 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 EA-------MMV------------SANLKLSEKQEvkkelvteiltalglmscshtRTALLSGGQRKRLAIALELVNNPP 220
Cdd:TIGR03719 405 EEisggldiIKLgkreipsrayvgRFNFKGSDQQK---------------------KVGQLSGGERNRVHLAKTLKSGGN 463
|
170
....*....|..
gi 215820660 221 VMFFDEPTSGLD 232
Cdd:TIGR03719 464 VLLLDEPTNDLD 475
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
195-278 |
4.92e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.34 E-value: 4.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 195 HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIcTIHQPSAKLFEMFDKLYIL 274
Cdd:PRK10982 386 RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGII-IISSEMPELLGITDRILVM 464
|
....
gi 215820660 275 SQGQ 278
Cdd:PRK10982 465 SNGL 468
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
58-295 |
5.35e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 48.97 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 58 AVDiefvELSYSVREGpcwrkrgyktllkclsgkfcrrELIGIMGPSGAGKS----TFMNiLAGYRESGMKGQILVNGR- 132
Cdd:PRK11022 22 AVD----RISYSVKQG----------------------EVVGIVGESGSGKSvsslAIMG-LIDYPGRVMAEKLEFNGQd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 133 -----PRELRTFRKMS-CYIMQDDM--LLPHLTVLEAMMVSANLKLSEKQEVKKELVTEILTALGL---MSCSHTRTALL 201
Cdd:PRK11022 75 lqrisEKERRNLVGAEvAMIFQDPMtsLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 202 SGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCIF 281
Cdd:PRK11022 155 SGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
250
....*....|....*....
gi 215820660 282 KGVVTNLI-----PYLKGL 295
Cdd:PRK11022 235 TGKAHDIFraprhPYTQAL 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
94-232 |
8.65e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRP---RELRTFRK---MScyimQDDMLLPHLTVLEAMMVSAN 167
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLTGLLPAS-EGEAWLFGQPvdaGDIATRRRvgyMS----QAFSLYGELTVRQNLELHAR 365
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 215820660 168 L-KLSEKQevKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLD 232
Cdd:NF033858 366 LfHLPAAE--IAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
85-261 |
1.13e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 46.16 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 85 LKCLSGKFCRRELIGIMGPSGAGKSTFmnILAGYRESGMKgqILVNGRPRelrtfrkmscyimqddmllphltvleammV 164
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLYASGKA--RLISFLPK-----------------------------F 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 165 SANLKLSEKQevkkeLVTEILTALGLMSCSHtRTALLSGGQRKRLAIALEL-VNNPPVMF-FDEPTSGLDSASCFQVVSL 242
Cdd:cd03238 58 SRNKLIFIDQ-----LQFLIDVGLGYLTLGQ-KLSTLSGGELQRVKLASELfSEPPGTLFiLDEPSTGLHQQDINQLLEV 131
|
170
....*....|....*....
gi 215820660 243 MKSLAQGGRTIICTIHQPS 261
Cdd:cd03238 132 IKGLIDLGNTVILIEHNLD 150
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
98-235 |
2.17e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.42 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 98 IGIMGPSGAGKSTFMNILAGY-RESgmkgqilvNGrprELRTFRKMSC-YIMQDDMLLPHLTVLEAMM------------ 163
Cdd:PRK11819 36 IGVLGLNGAGKSTLLRIMAGVdKEF--------EG---EARPAPGIKVgYLPQEPQLDPEKTVRENVEegvaevkaaldr 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 164 ---VSANL--------KLSEKQEvkkELvTEILTALGL-------------MSC--SHTRTALLSGGQRKRLAIALELVN 217
Cdd:PRK11819 105 fneIYAAYaepdadfdALAAEQG---EL-QEIIDAADAwdldsqleiamdaLRCppWDAKVTKLSGGERRRVALCRLLLE 180
|
170
....*....|....*...
gi 215820660 218 NPPVMFFDEPTSGLDSAS 235
Cdd:PRK11819 181 KPDMLLLDEPTNHLDAES 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
94-280 |
3.01e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 47.09 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RRELIGIMGPSGAGKSTFMNILAGYRESG-MKGQILVNGRPRELRTFR----KMSCYIMQDDMLLPHLTVLEammvsaNL 168
Cdd:NF040905 26 EGEIHALCGENGAGKSTLMKVLSGVYPHGsYEGEILFDGEVCRFKDIRdseaLGIVIIHQELALIPYLSIAE------NI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 169 KLSEKQ---------EVKKElVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGL---DSAsc 236
Cdd:NF040905 100 FLGNERakrgvidwnETNRR-ARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALneeDSA-- 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 215820660 237 fQVVSLMKSL-AQGGRTIIctIhqpSAKLFEMF---DKLYILSQGQCI 280
Cdd:NF040905 177 -ALLDLLLELkAQGITSII--I---SHKLNEIRrvaDSITVLRDGRTI 218
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
160-261 |
5.27e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 160 EAMMVSANLKLSEKQEV----KKELVTEILTAL--GLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDS 233
Cdd:PTZ00265 533 ELIEMRKNYQTIKDSEVvdvsKKVLIHDFVSALpdKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDN 612
|
90 100
....*....|....*....|....*....
gi 215820660 234 ASCFQVVSLMKSL-AQGGRTIICTIHQPS 261
Cdd:PTZ00265 613 KSEYLVQKTINNLkGNENRITIIIAHRLS 641
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
94-278 |
7.59e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 7.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 94 RR-ELIGIMGPSGAGKSTF-MNILA---GYRESGmkgQILVNGRPRELRTF--------------RKMSCYIMQDDML-- 152
Cdd:NF040905 284 RRgEIVGIAGLMGAGRTELaMSVFGrsyGRNISG---TVFKDGKEVDVSTVsdaidaglayvtedRKGYGLNLIDDIKrn 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 153 --LPHLTvleamMVSANLKLSEKQEVKkeLVTEILTALGLMSCS-HTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTS 229
Cdd:NF040905 361 itLANLG-----KVSRRGVIDENEEIK--VAEEYRKKMNIKTPSvFQKVGNLSGGNQQKVVLSKWLFTDPDVLILDEPTR 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 215820660 230 GLDSASCFQVVSLMKSLAQGGRTIIcTIhqpSAKLFE---MFDKLYILSQGQ 278
Cdd:NF040905 434 GIDVGAKYEIYTIINELAAEGKGVI-VI---SSELPEllgMCDRIYVMNEGR 481
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
201-235 |
1.02e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 45.79 E-value: 1.02e-04
10 20 30
....*....|....*....|....*....|....*
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAS 235
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS 1393
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
258-315 |
1.76e-04 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 44.51 E-value: 1.76e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 215820660 258 HQPSAKLFEMFDKLYILSQGQCI-FKGVVTNLIPYLKGLGLHCPTYHNPADFIIEVASG 315
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKGGLTvYHGPVKKVEEYFAGLGINVPERVNPPDHFIDILEG 59
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
201-259 |
1.83e-04 |
|
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: 43.47 E-value: 1.83e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLD---SASCFQvVSLMKSLAQGGRTIICTIHQ 259
Cdd:cd03290 141 LSGGQRQRICVARALYQNTNIVFLDDPFSALDihlSDHLMQ-EGILKFLQDDKRTLVLVTHK 201
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
201-305 |
2.07e-04 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.02 E-value: 2.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPSAKLFEMFDKLYILSQGQCI 280
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
90 100 110
....*....|....*....|....*....|
gi 215820660 281 FKGVVTNLI-----PYLKGLGLHCPTYHNP 305
Cdd:PRK15093 239 ETAPSKELVttphhPYTQALIRAIPDFGSA 268
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
197-277 |
3.14e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 197 RTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVV-SLMKSLAQGGRTIICT--IHqpsakLFEMFDKLYI 273
Cdd:PLN03232 737 RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDELKGKTRVLVTnqLH-----FLPLMDRIIL 811
|
....
gi 215820660 274 LSQG 277
Cdd:PLN03232 812 VSEG 815
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
201-258 |
4.11e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 43.66 E-value: 4.11e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 201 LSGGQRKRLAIALELVN---NPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
96-261 |
4.72e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 96 ELIGIMGPSGAGKSTFMNILAGYRESGmKGQILVNGRprelrtfrkmSCYIMQDDMLLPHLTVLEAMMVSAnLKLSEKQE 175
Cdd:PRK13545 51 EIVGIIGLNGSGKSTLSNLIAGVTMPN-KGTVDIKGS----------AALIAISSGLNGQLTGIENIELKG-LMMGLTKE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 176 VKKELVTEILTALGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIIC 255
Cdd:PRK13545 119 KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFF 198
|
....*.
gi 215820660 256 TIHQPS 261
Cdd:PRK13545 199 ISHSLS 204
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
201-272 |
7.72e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.05 E-value: 7.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRK------RLAIALELVNNPPVMFFDEPTSGLDSASC-FQVVSLMKS-LAQGGRTIICTIHQPsaKLFEMFDKLY 272
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIeESLAEIIEErKSQKNFQLIVITHDE--ELVDAADHIY 193
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
200-261 |
7.85e-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: 41.99 E-value: 7.85e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 215820660 200 LLSGGQRK---RLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIHQPS 261
Cdd:pfam13304 236 ELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
175-254 |
2.54e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.77 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 175 EVKKELVTEILTA-LGLMSCSHTRTALLSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTI 253
Cdd:PRK10938 109 EVKDPARCEQLAQqFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITL 188
|
.
gi 215820660 254 I 254
Cdd:PRK10938 189 V 189
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
201-258 |
2.68e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.15 E-value: 2.68e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 215820660 201 LSGGQRKRLAIALEL---VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTIH 258
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
70-152 |
3.22e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.92 E-value: 3.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 70 VREGPCWRKR-GYKTLLKCLSGKFCRRELIGIMGPSGAGKS----TFMNILagyreSGMKGQILVNGRP------RELRt 138
Cdd:PTZ00243 1310 VFEGVQMRYReGLPLVLRGVSFRIAPREKVGIVGRTGSGKStlllTFMRMV-----EVCGGEIRVNGREigayglRELR- 1383
|
90
....*....|....
gi 215820660 139 fRKMScYIMQDDML 152
Cdd:PTZ00243 1384 -RQFS-MIPQDPVL 1395
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
201-278 |
3.70e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRKRLAIALELVNNPPVMFFDEPTSGLDSAScfqVVSLMKSLA--QGGrtiICTIHQPSAKLFEMFDKLYILSQGQ 278
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA---VEALIQGLVlfQGG---VLMVSHDEHLISGSVDELWVVSEGK 701
|
|
| NK |
cd02019 |
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ... |
97-116 |
4.41e-03 |
|
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.
Pssm-ID: 238977 [Multi-domain] Cd Length: 69 Bit Score: 36.16 E-value: 4.41e-03
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
201-276 |
6.13e-03 |
|
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: 38.78 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 201 LSGGQRKRLAIALEL----VNNPPVMFFDEPTSGLDSASCFQVVSLMKSLAQGGRtIICTIHQPsaKLFEMFDKLYILSQ 276
Cdd:cd03272 159 LSGGQKSLVALALIFaiqkCDPAPFYLFDEIDAALDAQYRTAVANMIKELSDGAQ-FITTTFRP--ELLEVADKFYGVKF 235
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
184-290 |
6.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 39.81 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 215820660 184 ILTALGLMSCSHTRT-ALLSGGQRKRLAIA----LELVNnppVMF-FDEPTSGLDSASCFQVVSLMKSLAQGGRTIICTI 257
Cdd:PRK00635 459 ILIDLGLPYLTPERAlATLSGGEQERTALAkhlgAELIG---ITYiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVE 535
|
90 100 110
....*....|....*....|....*....|....
gi 215820660 258 HQpsAKLFEMFDKLYILSQGQCIFKG-VVTNLIP 290
Cdd:PRK00635 536 HD--EQMISLADRIIDIGPGAGIFGGeVLFNGSP 567
|
|
| |
