|
Name |
Accession |
Description |
Interval |
E-value |
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
49-636 |
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: 840.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEYLGDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLT 128
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLTYTAHMRMKNATVQ-QKMERVENVLRDMNLTDCQNTLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKkEKRERVDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 208 GLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRLCPFFDKLGpdFRVPESYNPAD 287
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVPFFSDLG--HPCPENYNPAD 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 288 FVMSEISISPETEQEDVTRIEYLIHEYQNSDIGTQMLKKTRTAVDEFGGYGD-DEDDGESRYNSTFGTQFEILLKRSLRT 366
Cdd:TIGR00955 274 FYVQVLAVIPGSENESRERIEKICDSFAVSDIGRDMLVNTNLWSGKAGGLVKdSENMEGIGYNASWWTQFYALLKRSWLS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 367 TFRDPLLLRVRFAQILATAILVGIVNWRVELKGPTIQNLEGVMYNCARDMTFLFYFPSVNVITSELPVFLREHKSNIYSV 446
Cdd:TIGR00955 354 VLRDPLLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFLTNMTFQNVFPVINVFTAELPVFLRETRSGLYRV 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 447 EAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTSFLVFVFVCITLTWVAVSIAYVGACIFGDEGLVVTFMPMFVLP 526
Cdd:TIGR00955 434 SAYFLAKTIAELPLFIILPALFTSITYWMIGLRSGATHFLTFLFLVTLVANVATSFGYLISCAFSSTSMALTVGPPFVIP 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 527 MLVFGGFYVNANSIPVYYQYVSFVSWFKHGFEALEANQWKEIDKISgcdlinPLNATTTGYCPASdGPGILTRRGID-TP 605
Cdd:TIGR00955 514 FLLFGGFFINSDSIPVYFKWLSYLSWFRYGNEGLLINQWSDVDNIE------CTSANTTGPCPSS-GEVILETLSFRnAD 586
|
570 580 590
....*....|....*....|....*....|.
gi 808355238 606 LYANVLILFMSFFVYRIIGLVALKIRVRFAK 636
Cdd:TIGR00955 587 LYLDLIGLVILIFFFRLLAYFALRIRIRRKR 617
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
51-629 |
2.30e-81 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 269.83 E-value: 2.30e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNGveYLGDVTVNGKKITKQKMRQMcAYVQQVDLFCGTLTV 129
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNN--FTGTILANNRKPTKQILKRT-GFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 REQLTYTAHMRMKNA-TVQQKMERVENVLRDMNLTDCQNTLIGiPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSG 208
Cdd:PLN03211 158 RETLVFCSLLRLPKSlTKQEKILVAESVISELGLTKCENTIIG-NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 209 LDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRLCPFFDKLG--PDFrvpeSYNPA 286
Cdd:PLN03211 237 LDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGfsPSF----PMNPA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 287 DFVMS------EISISPETEQEDVTriEYLIHEYQnsdigTQMLKKTRTAVD---------EFGGYGDDEDDGESRYN-- 349
Cdd:PLN03211 313 DFLLDlangvcQTDGVSEREKPNVK--QSLVASYN-----TLLAPKVKAAIEmshfpqanaRFVGSASTKEHRSSDRIsi 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 350 STFGTQFEILLKRSLRTTFRDPL-LLRVrfAQILATAILVGIVNWRVELKgpTIQNLEGVMYNCArdmTFLFYFPSVN-- 426
Cdd:PLN03211 386 STWFNQFSILLQRSLKERKHESFnTLRV--FQVIAAALLAGLMWWHSDFR--DVQDRLGLLFFIS---IFWGVFPSFNsv 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 427 -VITSELPVFLREHKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTSFLVFVFVciTLTWVAVSIAY- 504
Cdd:PLN03211 459 fVFPQERAIFVKERASGMYTLSSYFMARIVGDLPMELILPTIFLTVTYWMAGLKPELGAFLLTLLV--LLGYVLVSQGLg 536
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 505 --VGACIFgDEGLVVTFMPMFVLPMLVFGGFYVnaNSIPVYYQYVSFVSWFKHGFEALEANQW---KEIDKISGCDLINP 579
Cdd:PLN03211 537 laLGAAIM-DAKKASTIVTVTMLAFVLTGGFYV--HKLPSCMAWIKYISTTFYSYRLLINVQYgegKRISSLLGCSLPHG 613
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 808355238 580 LNATTTGYcpasdgpgILTRRGIDTPLYANVLILFMSFFVYRIIGLVALK 629
Cdd:PLN03211 614 SDRASCKF--------VEEDVAGQISPATSVSVLIFMFVGYRLLAYLALR 655
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
33-261 |
7.83e-71 |
|
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: 227.43 E-value: 7.83e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 33 TIAWSGLVATVPQA-GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdTNGVEYLGDVTVNGKKITKQKMR 111
Cdd:cd03213 3 TLSFRNLTVTVKSSpSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGR-RTGLGVSGEVLINGRPLDKRSFR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 112 QMCAYVQQVDLFCGTLTVREQLTYTAHMRmknatvqqkmervenvlrdmnltdcqntligipnrmkGISIGEKKRLAFAC 191
Cdd:cd03213 82 KIIGYVPQDDILHPTLTVRETLMFAAKLR-------------------------------------GLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 192 EILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
11-636 |
3.34e-70 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 247.71 E-value: 3.34e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 11 DATSKSTMITVDTGDGSEKGRKTIAWSGLVATVPQAGGGRKeVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTN 90
Cdd:TIGR00956 737 DLTDESDDVNDEKDMEKESGEDIFHWRNLTYEVKIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTT 815
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 91 GVEYLGDVTVNGKKITKQKMRQMcAYVQQVDLFCGTLTVREQLTYTAHMRM-KNATVQQKMERVENVLRDMNLTDCQNTL 169
Cdd:TIGR00956 816 GVITGGDRLVNGRPLDSSFQRSI-GYVQQQDLHLPTSTVRESLRFSAYLRQpKSVSKSEKMEYVEEVIKLLEMESYADAV 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 170 IGIPNrmKGISIGEKKRLAFACEILTDPK-ILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHK 248
Cdd:TIGR00956 895 VGVPG--EGLNVEQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEFDR 972
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 249 VCFMATG-KTVYHGAVDRLCP----FFDKLGPDfRVPESYNPADFVMSEISISPETEqedvTRIEYliHE-YQNSDIGTQ 322
Cdd:TIGR00956 973 LLLLQKGgQTVYFGDLGENSHtiinYFEKHGAP-KCPEDANPAEWMLEVIGAAPGAH----ANQDY--HEvWRNSSEYQA 1045
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 323 MLKKTRTAVDEFGGY-GDDEDDGESRYNSTFGTQFEILLKRSLRTTFRDPLLLRVRFAQILATAILVGIVNWRVelkGPT 401
Cdd:TIGR00956 1046 VKNELDRLEAELSKAeDDNDPDALSKYAASLWYQFKLVLWRTFQQYWRTPDYLYSKFFLTIFAALFIGFTFFKV---GTS 1122
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 402 IQNLEGVMYncARDMTFLFYFPSVN-----VITSELPVFLREHKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMA 476
Cdd:TIGR00956 1123 LQGLQNQMF--AVFMATVLFNPLIQqylppFVAQRDLYEVRERPSRTFSWLAFIAAQITVEIPYNLVAGTIFFFIWYYPV 1200
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 477 GLVASVT---------------SFLVFVFV------CITLTWVAVSIAYVGacifgdeGLVVTFmpmfvlpMLVFGGFYV 535
Cdd:TIGR00956 1201 GFYWNASktgqvhergvlfwllSTMFFLYFstlgqmVISFNPNADNAAVLA-------SLLFTM-------CLSFCGVLA 1266
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 536 NANSIP---VYYQYVSFVSWFkhgFEALEANQWKEID---------------------------KISGCDLINPLNATTT 585
Cdd:TIGR00956 1267 PPSRMPgfwIFMYRCSPFTYL---VQALLSTGLADVPvtckvkelltfnppsgqtcgeymkpylENAGGYLLNPNATDSC 1343
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 808355238 586 GYCPASDGPGILTRRGIDTPLYANVLILFMSFFVYRIIGLVALKIRVRFAK 636
Cdd:TIGR00956 1344 SFCQYSYTNDFLEPISSKYSGRWRNFGIFIAFIFFNIIATVFFYWLARVPK 1394
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
51-261 |
2.59e-69 |
|
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: 224.46 E-value: 2.59e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEYLGDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLTVR 130
Cdd:cd03234 20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 131 EQLTYTAHMRMKNATVQ-QKMERVEnvlrDMNLTDCQNTLIGiPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:cd03234 100 ETLTYTAILRLPRKSSDaIRKKRVE----DVLLRDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808355238 210 DAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
50-556 |
1.25e-61 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 222.80 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGveYL-GDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLT 128
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGG--YIeGDIRISGFPKKQETFARISGYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLTYTAHMRM-KNATVQQKMERVENVLRDMNLTDCQNTLIGIPNrMKGISIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:PLN03140 970 VRESLIYSAFLRLpKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPG-VTGLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 208 GLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMAT-GKTVYHGAVDR----LCPFFDKLGPDFRVPES 282
Cdd:PLN03140 1049 GLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRgGQVIYSGPLGRnshkIIEYFEAIPGVPKIKEK 1128
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 283 YNPADFVMSEISISPEteqedvTRIEYLIHEYQNSdigTQMLKKTRTAVDEFGG--YGDDEDDGESRYNSTFGTQFEILL 360
Cdd:PLN03140 1129 YNPATWMLEVSSLAAE------VKLGIDFAEHYKS---SSLYQRNKALVKELSTppPGASDLYFATQYSQSTWGQFKSCL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 361 KRSLRTTFRDPLLLRVRFAQILATAILVGIVNWRVELKGPTIQNLE---GVMYNCArdmtflfYFPSVN-------VITS 430
Cdd:PLN03140 1200 WKQWWTYWRSPDYNLVRFFFTLAAALMVGTIFWKVGTKRSNANDLTmviGAMYAAV-------LFVGINncstvqpMVAV 1272
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 431 ELPVFLREHKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTSFLVFVFVCIT--LTW-------VAVS 501
Cdd:PLN03140 1273 ERTVFYRERAAGMYSALPYAIAQVVCEIPYVLIQTTYYTLIVYAMVAFEWTAAKFFWFYFISFFsfLYFtyygmmtVSLT 1352
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 502 IAYVGACIFGdeglvVTFMPMFVLpmlvFGGFYVNANSIP---VYYQYVSFVSWFKHG 556
Cdd:PLN03140 1353 PNQQVAAIFA-----AAFYGLFNL----FSGFFIPRPKIPkwwVWYYWICPVAWTVYG 1401
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-261 |
1.45e-51 |
|
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: 176.28 E-value: 1.45e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 34 IAWSGLVATVPQAGGgRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeYLGDVTVNGKKITKQKMRQm 113
Cdd:cd03232 4 LTWKNLNYTVPVKGG-KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGV-ITGEILINGRPLDKNFQRS- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 114 CAYVQQVDLFCGTLTVREQLTYTAHMRmknatvqqkmervenvlrdmnltdcqntligipnrmkGISIGEKKRLAFACEI 193
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLR-------------------------------------GLSVEQRKRLTIGVEL 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 194 LTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMA-TGKTVYHG 261
Cdd:cd03232 124 AAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHQPSASIFEKFDRLLLLKrGGKTVYFG 192
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
49-266 |
1.07e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 1.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQ--KMRQMCAYVQQVDLF 123
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLlrpTS------GEVRVLGEDVARDpaEVRRRIGYVPQEPAL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTDPKILFCD 203
Cdd:COG1131 85 YPDLTVRENLRFFA--RLYGLPRKEARERIDELLELFGLTDAADR------KVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355238 204 EPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYL-EEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
51-566 |
4.12e-45 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 172.99 E-value: 4.12e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA------HLDTNGVeylgdVTVNG---KKITKQKmRQMCAYVQQVD 121
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdgfHIGVEGV-----ITYDGitpEEIKKHY-RGDVVYNAETD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTLTVREQLTYTAHM-----RMKNATVQQKMERVENV-LRDMNLTDCQNTLIGipNRM-KGISIGEKKRLAFACEIL 194
Cdd:TIGR00956 148 VHFPHLTVGETLDFAARCktpqnRPDGVSREEYAKHIADVyMATYGLSHTRNTKVG--NDFvRGVSGGERKRVSIAEASL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLANKGK-TIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRLCPFFDKL 273
Cdd:TIGR00956 226 GGAKIQCWDNATRGLDSATALEFIRALKTSANILDtTPLVAIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAKQYFEKM 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 274 GpdFRVPESYNPADFVMSEIS------------ISPETEQEDVTRieyliheYQNSDIGTQMLK------------KTRT 329
Cdd:TIGR00956 306 G--FKCPDRQTTADFLTSLTSpaerqikpgyekKVPRTPQEFETY-------WRNSPEYAQLMKeideyldrcsesDTKE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 330 AVDEFGGYG-DDEDDGESRYNSTFGTQFEILLKRSLRTTFRDPLLLRVRFAQILATAILVGIVNWRVELKGPTIQNLEGV 408
Cdd:TIGR00956 377 AYRESHVAKqSKRTRPSSPYTVSFSMQVKYCLARNFLRMKGNPSFTLFMVFGNIIMALILSSVFYNLPKNTSDFYSRGGA 456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 409 MYncardMTFLFY-FPSVNVITS---ELPVFLREHKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTS 484
Cdd:TIGR00956 457 LF-----FAILFNaFSSLLEIASmyeARPIVEKHRKYALYHPSADAIASIISEIPFKIIESVVFNIILYFMVNFRRTAGR 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 485 FLVFVFVCITLTWVAVSIAYVGACIFGDEGLVVTFMPMFVLPMLVFGGFYVNANSIPVYYQYVSFVSWFKHGFEALEANQ 564
Cdd:TIGR00956 532 FFFYLLILFICTLAMSHLFRSIGAVTKTLSEAMTPAAILLLALSIYTGFAIPRPSMLGWSKWIYYVNPLAYAFESLMVNE 611
|
..
gi 808355238 565 WK 566
Cdd:TIGR00956 612 FH 613
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
359-563 |
1.10e-38 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 141.64 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 359 LLKRSLRTTFRDPLLLRVRFAQILATAILVGIVNWRVELKGPTIQNLeGVMYNCARDMTFLFYFPSVNVITSELPVFLRE 438
Cdd:pfam01061 1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRP-GLLFFSILFNAFSALSGISPVFEKERGVLYRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 439 HKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTSFLVFVFVCITLTWVAVSIAYVGACIFGDEGLVVT 518
Cdd:pfam01061 80 LASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFFLFLLVLLLTALAASSLGLFISALAPSFEDASQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 808355238 519 FMPMFVLPMLVFGGFYVNANSIPVYYQYVSFVSWFKHGFEALEAN 563
Cdd:pfam01061 160 LGPLVLLPLLLLSGFFIPIDSMPVWWQWIYYLNPLTYAIEALRAN 204
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
49-267 |
3.33e-37 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 138.84 E-value: 3.33e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK---MRQMCAYVQQVDLFcG 125
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDS---GSILIDGEDVRKEPreaRRQIGVLPDERGLY-D 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:COG4555 88 RLTVRENIRYFA--ELYGLFDEELKKRIEELIELLGLEEFLDRRVG------ELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRLC 267
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIM-QEVEALCDRVVILHKGKVVAQGSLDELR 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
47-256 |
8.64e-37 |
|
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: 136.44 E-value: 8.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQ---KMRQMCAYV-QQVDL 122
Cdd:cd03225 10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLG---PTSGEVLVDGKDLTKLslkELRRKVGLVfQNPDD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 -FCGTlTVREQLTYTA-HMRMKNATVQqkmERVENVLRDMNLTDCQN----TLigipnrmkgiSIGEKKRLAFACEILTD 196
Cdd:cd03225 87 qFFGP-TVEEEVAFGLeNLGLPEEEIE---ERVEEALELVGLEGLRDrspfTL----------SGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGK 256
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL-DLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
45-256 |
2.05e-36 |
|
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: 135.70 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKMRQMCAYV------- 117
Cdd:cd03255 11 GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDR---PTSGEVRVDGTDISKLSEKELAAFRrrhigfv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 118 -QQVDLFcGTLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMkgiSIGEKKRLAFACEILTD 196
Cdd:cd03255 88 fQSFNLL-PDLTALENVELP--LLLAGVPKKERRERAEELLERVGLGDRLNHY---PSEL---SGGQQQRVAIARALAND 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLA-NKGKTIIVVLHQPSstVFRMFHKVCFMATGK 256
Cdd:cd03255 159 PKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPE--LAEYADRIIELRDGK 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
47-267 |
2.83e-35 |
|
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: 132.63 E-value: 2.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQ--KMRQMCAYVQQVD 121
Cdd:cd03263 11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrpTS------GTAYINGYSIRTDrkAARQSLGYCPQFD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTLTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTLIgipnrmKGISIGEKKRLAFACEILTDPKILF 201
Cdd:cd03263 85 ALFDELTVREHLRFYA--RLKGLPKSEIKEEVELLLRVLGLTDKANKRA------RTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRLC 267
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDE-AEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
45-258 |
4.83e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 132.09 E-value: 4.83e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDT-NGveylGDVTVNGKKITKQKMRQMCA-------Y 116
Cdd:COG1136 15 GTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRpTS----GEVLIDGQDISSLSERELARlrrrhigF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 V-QQVDLFcGTLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMkgiSIGEKKRLAFACEILT 195
Cdd:COG1136 91 VfQFFNLL-PELTALENVALP--LLLAGVSRKERRERARELLERVGLGDRLDHR---PSQL---SGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLA-NKGKTIIVVLHQPSstVFRMFHKVCFMATGKTV 258
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNrELGTTIVMVTHDPE--LAARADRVIRLRDGRIV 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
48-258 |
1.09e-33 |
|
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: 127.76 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtnGVEYLGDVTVNGKKITKQKMRQMCAYV-QQVDLFCGT 126
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGL---IKESSGSILLNGKPIKAKERRKSIGYVmQDVDYQLFT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYtahmRMKNATvqQKMERVENVLRDMNLtdcqntligipNRMK-----GISIGEKKRLAFACEILTDPKILF 201
Cdd:cd03226 87 DSVREELLL----GLKELD--AGNEQAETVLKDLDL-----------YALKerhplSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTV 258
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDY-EFLAKVCDRVLLLANGAIV 205
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
53-564 |
1.10e-33 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 138.06 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEYLGDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLTVREQ 132
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSLKVSGEITYNGYRLNEFVPRKTSAYISQNDVHVGVMTVKET 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 133 LTYTAH---------------MRMKNATV-----------QQKMERVEN------VLRDMNLTDCQNTLIGiPNRMKGIS 180
Cdd:PLN03140 260 LDFSARcqgvgtrydllselaRREKDAGIfpeaevdlfmkATAMEGVKSslitdyTLKILGLDICKDTIVG-DEMIRGIS 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 181 IGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGK-TIIVVLHQPSSTVFRMFHKVCFMATGKTVY 259
Cdd:PLN03140 339 GGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEaTVLMSLLQPAPETFDLFDDIILLSEGQIVY 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 260 HGAVDRLCPFFDKLGpdFRVPESYNPADFvMSEISISPETEQEDVTR--------IEYLIHEYQNSDIGTQMLKKTRTAV 331
Cdd:PLN03140 419 QGPRDHILEFFESCG--FKCPERKGTADF-LQEVTSKKDQEQYWADRnkpyryisVSEFAERFKSFHVGMQLENELSVPF 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 332 DEFggYGDDEDDGESRYNSTFGTQFEILLKRSLRTTFRDPLLLRVRFAQILATAILVGIVNWRVELKgpTIQNLEGVMYN 411
Cdd:PLN03140 496 DKS--QSHKAALVFSKYSVPKMELLKACWDKEWLLMKRNAFVYVFKTVQIIIVAAIASTVFLRTEMH--TRNEEDGALYI 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 412 CARDMTFLFY----FPSVNVITSELPVFLREHKSNIYSVEAYFLAKSLAELPQYTILPMIYGTIIYWMAGLVASVTSFLV 487
Cdd:PLN03140 572 GALLFSMIINmfngFAELALMIQRLPVFYKQRDLLFHPPWTFTLPTFLLGIPISIIESVVWVVITYYSIGFAPEASRFFK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 488 FVFVCITLTWVAVSI--AYVGAC---IFGDEGLVVTFMPMFVLpmlvfGGFYVNANSIPVYYQYVSFVSWFKHGFEALEA 562
Cdd:PLN03140 652 QLLLVFLIQQMAAGIfrLIASVCrtmIIANTGGALVLLLVFLL-----GGFILPKGEIPNWWEWAYWVSPLSYGFNALAV 726
|
..
gi 808355238 563 NQ 564
Cdd:PLN03140 727 NE 728
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
49-256 |
2.02e-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: 125.97 E-value: 2.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNGKKITKQ--KMRQMCAYVQQVDLFCGT 126
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKP---DSGEIKVLGKDIKKEpeEVKRRIGYLPEEPSLYEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYtahmrmknatvqqkmervenvlrdmnltdcqntligipnrmkgiSIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03230 88 LTVRENLKL--------------------------------------------SGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGK 256
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHIL-EEAERLCDRVAILNNGR 172
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
49-273 |
1.22e-32 |
|
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: 125.52 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGVEYL--GDVTVNGKKITK---QKMRQMCAYV-QQVD- 121
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLL-----NGLLKPtsGEVLVDGKDITKknlRELRRKVGLVfQNPDd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 -LFCGTltVREQLTYT-AHMRMKNATVQqkmERVENVLRDMNLTDCQNTligIPNRmkgISIGEKKRLAFACEILTDPKI 199
Cdd:COG1122 87 qLFAPT--VEEDVAFGpENLGLPREEIR---ERVEEALELVGLEHLADR---PPHE---LSGGQKQRVAIAGVLAMEPEV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRLCPFFDKL 273
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDL-DLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
49-266 |
1.91e-31 |
|
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: 122.40 E-value: 1.91e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITK------QKMRQMCAYV-Q 118
Cdd:COG1127 16 GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLlrpDS------GEILVDGQDITGlsekelYELRRRIGMLfQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 119 QVDLFcGTLTVRE--QLTYTAHMRMKNATVQqkmERVENVLRDMNLTDCQNTLigiPNRmkgISIGEKKRLAFACEILTD 196
Cdd:COG1127 90 GGALF-DSLTVFEnvAFPLREHTDLSEAEIR---ELVLEKLELVGLPGAADKM---PSE---LSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDS-AFAIADRVAVLADGKIIAEGTPEEL 229
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
47-261 |
5.44e-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: 5.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNG-VEylGDVTVNG--KKITKQKMRQMCAYVQQVDL 122
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALAnRTEGNVsVE--GDIHYNGipYKEFAEKYPGEIIYVSEEDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTYTAhmrmknatvqqkmervenvlrdmnltDCQNtligipNRM-KGISIGEKKRLAFACEILTDPKILF 201
Cdd:cd03233 94 HFPTLTVRETLDFAL--------------------------RCKG------NEFvRGISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVlKTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
47-266 |
1.68e-30 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 127.26 E-value: 1.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNG---KKITKQKMRQMCAYV-QQVDL 122
Cdd:COG2274 484 PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEP---TSGRILIDGidlRQIDPASLRRQIGVVlQDVFL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTltVREQLTYTAhmrmKNATvqqkMERVENVLRDMNLTD--CQ-----NTLIGipNRMKGISIGEKKRLAFACEILT 195
Cdd:COG2274 561 FSGT--IRENITLGD----PDAT----DEEIIEAARLAGLHDfiEAlpmgyDTVVG--EGGSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPsSTVfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRL-STI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
49-266 |
3.25e-30 |
|
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: 118.76 E-value: 3.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITK------QKMRQMCAYV-QQVD 121
Cdd:cd03261 11 GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDS---GEVLIDGEDISGlseaelYRLRRRMGMLfQSGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFcGTLTVREQLTYTAHM------RMKNATVQQKMERVEnvlrdmnltdcqntLIGIPNRMKG-ISIGEKKRLAFACEIL 194
Cdd:cd03261 88 LF-DSLTVFENVAFPLREhtrlseEEIREIVLEKLEAVG--------------LRGAEDLYPAeLSGGMKKRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03261 153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLkKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
49-264 |
1.02e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 117.88 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQkmRQMCAYV-QQVDLFC 124
Cdd:COG1121 17 GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLlppTS------GTVRLFGKPPRRA--RRRIGYVpQRAEVDW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GT-LTVRE--QLTYTAHMRM-KNATVQQKmERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKIL 200
Cdd:COG1121 89 DFpITVRDvvLMGRYGRRGLfRRPSRADR-EAVDEALERVGLEDLADRPIG------ELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMAtGKTVYHGAVD 264
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDL-GAVREYFDRVLLLN-RGLVAHGPPE 223
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
54-207 |
1.32e-29 |
|
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: 114.28 E-value: 1.32e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdTNGVEylGDVTVNGKKITKQKMRQM---CAYVQQVDLFCGTLTVR 130
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGL-LSPTE--GTILLDGQDLTDDERKSLrkeIGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 131 EQLTYTAHMRMKNATVQQkmERVENVLRDMNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKD--ARAEEALEKLGLGDLADRPVG--ERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
47-256 |
3.09e-29 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 114.02 E-value: 3.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNG---KKITKQKMRQMCAYV-QQVDL 122
Cdd:cd03228 11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDP---TSGEILIDGvdlRDLDLESLRKNIAYVpQDPFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTltVREqltytahmrmknatvqqkmerveNVLrdmnltdcqntligipnrmkgiSIGEKKRLAFACEILTDPKILFC 202
Cdd:cd03228 88 FSGT--IRE-----------------------NIL----------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSStvFRMFHKVCFMATGK 256
Cdd:cd03228 121 DEATSALDPETEALILEALRALA-KGKTVIVIAHRLST--IRDADRIIVLDDGR 171
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
49-261 |
4.89e-29 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 114.94 E-value: 4.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNGKKITKqkMRQMCAYVQQVDLFCGT-- 126
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKP---TSGSIRVFGKPLEK--ERKRIGYVPQRRSIDRDfp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVRE--QLTYTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:cd03235 85 ISVRDvvLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIG------ELSGGQQQRVLLARALVQDPDLLLLDE 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 205 PTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVcFMATGKTVYHG 261
Cdd:cd03235 159 PFAGVDPKTQEDIYELLRELRREGMTILVVTHDL-GLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
49-261 |
7.11e-29 |
|
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: 114.21 E-value: 7.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGeVLALMGGSGAGKTTLMNILAHLdTNGVEylGDVTVNGKKITK--QKMRQMCAYVQQVDLFCGT 126
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATL-TPPSS--GTIRIDGQDVLKqpQKLRRRIGYLPQEFGVYPN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03264 87 FTVREFLDYIA--WLKGIPSKEVKARVDEVLELVNLGDRAKK------KIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 207 SGLDAfmASEV-VRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03264 159 AGLDP--EERIrFRNLLSELGEDRIVILSTHI-VEDVESLCNQVAVLNKGKLVFEG 211
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
37-266 |
1.81e-28 |
|
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: 114.13 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 37 SGLVATVPQaGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNGKKITKQKMRQMCAY 116
Cdd:COG1124 5 RNLSVSYGQ-GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERP---WSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 VQQV--DLFcGTL----TVREQLTYT-AHMRMKNAtvqqkMERVENVLRDMNLTDcqNTLIGIPNRMkgiSIGEKKRLAF 189
Cdd:COG1124 81 VQMVfqDPY-ASLhprhTVDRILAEPlRIHGLPDR-----EERIAELLEQVGLPP--SFLDRYPHQL---SGGQRQRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 190 ACEILTDPKILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDL-AVVAHLCDRVAVMQNGRIVEELTVADL 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
49-256 |
2.20e-28 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 111.18 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITK---QKMRQMCAYVQQvdlfcg 125
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLK---PTSGEILIDGKDIAKlplEELRRRIGYVPQ------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 tltvreqltytahmrmknatvqqkmervenvlrdmnltdcqntligipnrmkgISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:cd00267 81 -----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGK 256
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDP-ELAELAADRVIVLKDGK 157
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
49-256 |
2.74e-28 |
|
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: 112.62 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDT-NGveylGDVTVNGKKITKQK-----MRQMCAYV-QQVD 121
Cdd:cd03262 11 GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEpDS----GTIIIDGLKLTDDKknineLRQKVGMVfQQFN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFcGTLTVREQLTYtAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILF 201
Cdd:cd03262 87 LF-PHLTVLENITL-APIKVKGMSKAEAEERALELLEKVGLADKADAY---PAQLSG---GQQQRVAIARALAMNPKVML 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQpsstvfrM-F-----HKVCFMATGK 256
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHE-------MgFarevaDRVIFMDDGR 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
49-238 |
5.11e-28 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 111.80 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQK--MRQMCAYV-QQVDLFcG 125
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLP---PSAGEVLWNGEPIRDARedYRRRLAYLgHADGLK-P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtaHMRMKNatVQQKMERVENVLRDMNLTDCQNTLIGIpnrmkgISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:COG4133 89 ELTVRENLRF--WAALYG--LRADREAIDEALEAVGLAGLADLPVRQ------LSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQP 238
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTHQP 191
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
33-266 |
6.17e-28 |
|
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: 118.72 E-value: 6.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 33 TIAWSGLVATVPqagGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNGveylGDVTVNGKKITK---Q 108
Cdd:COG4987 333 SLELEDVSFRYP---GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDPQS----GSITLGGVDLRDldeD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 109 KMRQMCAYV-QQVDLFCGTltVREQLTYTAhmrmKNATvqqkMERVENVLRDMNLTDcqnTLIGIPNRM--------KGI 179
Cdd:COG4987 406 DLRRRIAVVpQRPHLFDTT--LRENLRLAR----PDAT----DEELWAALERVGLGD---WLAALPDGLdtwlgeggRRL 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 180 SIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPssTVFRMFHKVCFMATGKTVY 259
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRL--AGLERMDRILVLEDGRIVE 549
|
....*..
gi 808355238 260 HGAVDRL 266
Cdd:COG4987 550 QGTHEEL 556
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
46-266 |
1.52e-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: 1.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 46 AGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNgveYLGDVTVNGKKITKQKM---RQMCAYV-QQVD 121
Cdd:COG4988 345 SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPP---YSGSILINGVDLSDLDPaswRRQIAWVpQNPY 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGtlTVREQLTYTAHmrmkNATvqqkMERVENVLRDMNLTD--CQ-----NTLIGipNRMKGISIGEKKRLAFACEIL 194
Cdd:COG4988 422 LFAG--TIRENLRLGRP----DAS----DEELEAALEAAGLDEfvAAlpdglDTPLG--EGGRGLSGGQAQRLALARALL 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSSTVFrmFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG4988 490 RDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ--ADRILVLDDGRIVEQGTHEEL 558
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
45-266 |
1.59e-27 |
|
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: 110.60 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMN-ILAHLDTNGveylGDVTVNGKKITKQKMRQMC----AYVQQ 119
Cdd:cd03224 7 NAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLLPPRS----GSIRFDGRDITGLPPHERAragiGYVPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 V-DLFcGTLTVREQLTYTAHMRmKNATVQQKMERVEN---VLRDMnltdcQNTLIGipnRMKGisiGEKKRLAFACEILT 195
Cdd:cd03224 83 GrRIF-PELTVEENLLLGAYAR-RRAKRKARLERVYElfpRLKER-----RKQLAG---TLSG---GEQQMLAIARALMS 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVlHQPSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03224 150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLV-EQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
49-261 |
1.73e-27 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 110.38 E-value: 1.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK--MRQMCAYVQQVDLFcGT 126
Cdd:cd03268 11 GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS---GEITFDGKSYQKNIeaLRRIGALIEAPGFY-PN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMRMKnatvqqKMERVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03268 87 LTARENLRLLARLLGI------RKKRIDEVLDVVGLKDSAK------KKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSE-IQKVADRIGIINKGKLIEEG 208
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
38-266 |
1.97e-27 |
|
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: 116.54 E-value: 1.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 38 GLVATVPQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGveylgDVTVNGKKITK------QK 109
Cdd:COG1123 265 NLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLrpTSG-----SILFDGKDLTKlsrrslRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 110 MRQMCAYVQQvD----LFCgTLTVREQLTYTAHMRmKNATVQQKMERVENVLRDMNL-TDCQNTLigiPNRMKGisiGEK 184
Cdd:COG1123 340 LRRRVQMVFQ-DpyssLNP-RMTVGDIIAEPLRLH-GLLSRAERRERVAELLERVGLpPDLADRY---PHELSG---GQR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 185 KRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAV 263
Cdd:COG1123 411 QRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHD-LAVVRYIADRVAVMYDGRIVEDGPT 489
|
...
gi 808355238 264 DRL 266
Cdd:COG1123 490 EEV 492
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
49-256 |
9.82e-27 |
|
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: 107.27 E-value: 9.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKITKQKMRQMCAYV-QQVDLFcG 125
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEepDSGSILIDGEDLTDLEDELPPLRRRIGMVfQDFALF-P 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtahmrmknatvqqkmervenvlrdmnltdcqntligipnrmkGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:cd03229 90 HLTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808355238 206 TSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPSStVFRMFHKVCFMATGK 256
Cdd:cd03229 128 TSALDPITRREVRALLKSLqAQLGITVVLVTHDLDE-AARLADRVVVLRDGK 178
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
48-258 |
3.58e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.34 E-value: 3.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNG---KKITKQKMRQMCAYV-QQVDL 122
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFyDPTS----GRILIDGvdiRDLTLESLRRQIGVVpQDTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcgTLTVREQLTYTAhmrmKNATvqqkMERVENVLRD-------MNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILT 195
Cdd:COG1132 426 F--SGTIRENIRYGR----PDAT----DEEVEEAAKAaqahefiEALPDGYDTVVG--ERGVNLSGGQRQRIAIARALLK 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPsSTVfRMFHKVCFMATGKTV 258
Cdd:COG1132 494 DPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRL-STI-RNADRILVLDDGRIV 553
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
49-261 |
7.65e-26 |
|
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: 105.44 E-value: 7.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGV--EYLGDVTVNGKKITKQKMRQMcAYVQQVDLFCGT 126
Cdd:cd03269 11 GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMI-----LGIilPDSGEVLFDGKPLDIAARNRI-GYLPEERGLYPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03269 85 MKVIDQLVYLA--QLKGLKKEEARRRIDEWLERLELSEYANK------RVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQ-MELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
45-266 |
7.11e-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: 103.43 E-value: 7.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGVEY--LGDVTVNGKKITK------QKMRQMCAY 116
Cdd:cd03258 12 GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCI-----NGLERptSGSVLVDGTDLTLlsgkelRKARRRIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 V-QQVDLFcGTLTVREQLTY---TAHMRMKNATvqqkmERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACE 192
Cdd:cd03258 87 IfQHFNLL-SSRTVFENVALpleIAGVPKAEIE-----ERVLELLELVGLEDKADAY---PAQLSG---GQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 193 ILTDPKILFCDEPTSGLDAFMASEVVRALLDLaNK--GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDI-NRelGLTIVLITHE-MEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
47-266 |
8.08e-25 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.45 E-value: 8.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEYLGDVTVNGKKITKQKMRQM---CAYVQQ--VD 121
Cdd:COG1123 15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRgrrIGMVFQdpMT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGtLTVREQLTYTahMRMKNATVQQKMERVENVLRdmnltdcqntLIGIPNRMK----GISIGEKKRLAFACEILTDP 197
Cdd:COG1123 95 QLNP-VTVGDQIAEA--LENLGLSRAEARARVLELLE----------AVGLERRLDryphQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDL-GVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
49-264 |
8.87e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 104.81 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLM----NILAHlDTngveylGDVTVNGKKITKQKMRQMcayvqqvdlfc 124
Cdd:COG4152 12 GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIriilGILAP-DS------GEVLWDGEPLDPEDRRRI----------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTL----------TVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTLIgipnrmKGISIGEKKRLAFACEIL 194
Cdd:COG4152 74 GYLpeerglypkmKVGEQLVYLA--RLKGLSKAEAKRRADEWLERLGLGDRANKKV------EELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVD 264
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMEL-VEELCDRIVIINKGRKVLSGSVD 214
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
52-266 |
1.34e-24 |
|
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: 103.00 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNGKKITK---QKMRQMCAYVQQ-VDLFCGT 126
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFyDPTS----GEILLDGVDIRDlnlRWLRSQIGLVSQePVLFDGT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 ltVREQLTYTAHmrmkNATvqqkMERVENVLRD-------MNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILTDPKI 199
Cdd:cd03249 93 --IAENIRYGKP----DAT----DEEVEEAAKKanihdfiMSLPDGYDTLVG--ERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 200 LFCDEPTSGLDAfmASE-VVRALLDLANKGKTIIVVLHQPSSTvfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03249 161 LLLDEATSALDA--ESEkLVQEALDRAMKGRTTIVIAHRLSTI--RNADLIAVLQNGQVVEQGTHDEL 224
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
53-264 |
1.48e-24 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 102.52 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVE--YLGDVTVNGKKITKQKMRQMCAY-----VQQVDLFcG 125
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIS-----GFLrpTSGSVLFDGEDITGLPPHEIARLgigrtFQIPRLF-P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAHMRMKNATVQQKM--------ERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDP 197
Cdd:cd03219 89 ELTVLENVMVAAQARTGSGLLLARArreerearERAEELLERVGLADLADRPAG------ELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVD 264
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV-VMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
45-236 |
1.68e-24 |
|
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: 102.16 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQkmRQMCAYVQQVDLFC 124
Cdd:cd03293 11 GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLER---PTSGEVLVDGEPVTGP--GPDRGYVFQQDALL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDE 204
Cdd:cd03293 86 PWLTVLDNVALG--LELQGVPKAEARERAEELLELVGLSGFENAY---PHQLSG---GMRQRVALARALAVDPDVLLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 205 PTSGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWREtGKTVLLVTH 190
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
51-266 |
3.35e-24 |
|
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: 101.53 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVtvNGKKITKQKMRQMCAYVQQVD-LFCGTl 127
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFydPQKGQILIDGI--DIRDISRKSLRSMIGVVLQDTfLFSGT- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 tVREQLTYtahmrmknATVQQKMERVENVLRD-------MNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILTDPKIL 200
Cdd:cd03254 93 -IMENIRL--------GRPNATDEEVIEAAKEagahdfiMKLPNGYDTVLG--ENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLaNKGKTIIVVLHQPSSTVFRmfHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKNA--DKILVLDDGKIIEEGTHDEL 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
49-261 |
3.97e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 99.82 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQKMRQ---MCAYVQQVdlfcg 125
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS---GEILLDGKDLASLSPKElarKIAYVPQA----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 tltvreqltytahmrmknatvqqkMERVeNVLrdmNLTDCQ-NTLIGipnrmkgisiGEKKRLAFACEILTDPKILFCDE 204
Cdd:cd03214 82 ------------------------LELL-GLA---HLADRPfNELSG----------GERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 205 PTSGLDAFMASEVVRALLDLAN-KGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDL-NLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
49-261 |
4.27e-24 |
|
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: 100.67 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDT-NGveylGDVTVNGKKITKQKMRQM-CAYV-QQVDLFcG 125
Cdd:cd03259 11 GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDS----GEILIDGRDVTGVPPERRnIGMVfQDYALF-P 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYT-AHMRMKNATVQQkmeRVENVLRdmnltdcqntLIGIPNRMK----GISIGEKKRLAFACEILTDPKIL 200
Cdd:cd03259 86 HLTVAENIAFGlKLRGVPKAEIRA---RVRELLE----------LVGLEGLLNryphELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQEE-ALALADRIAVMNEGRIVQVG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
33-241 |
7.11e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 105.83 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 33 TIAWSGLVATVPqaggGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtnGVEYLGDVTVNGKKIT---KQK 109
Cdd:TIGR02857 321 SLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGF---VDPTEGSIAVNGVPLAdadADS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 110 MRQMCAYVQQVD-LFCGTLTvreqltytAHMRMknATVQQKMERVENVLRDMNLTDC-------QNTLIGipNRMKGISI 181
Cdd:TIGR02857 394 WRDQIAWVPQHPfLFAGTIA--------ENIRL--ARPDASDAEIREALERAGLDEFvaalpqgLDTPIG--EGGAGLSG 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 182 GEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANkGKTIIVVLHQPSST 241
Cdd:TIGR02857 462 GQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALA 520
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
47-261 |
1.21e-23 |
|
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: 99.89 E-value: 1.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNG-VEYLGDVTVNGKKITKQKMRQMCAYVQQvDLF 123
Cdd:cd03257 14 GGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLkpTSGsIIFDGKDLLKLSRRLRKIRRKEIQMVFQ-DPM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 ---CGTLTVREQL--TYTAHMRM-----KNATVQQKMERVENVLRDMNLtdcqntligIPNRMKGisiGEKKRLAFACEI 193
Cdd:cd03257 93 sslNPRMTIGEQIaePLRIHGKLskkeaRKEAVLLLLVGVGLPEEVLNR---------YPHELSG---GQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 194 LTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDL-GVVAKIADRVAVMYAGKIVEEG 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
49-266 |
1.86e-23 |
|
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: 99.29 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMN-ILAHLDTNGveylGDVTVNGKKITKQKMRQMC----AYVQQV-DL 122
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLLPPRS----GSIRFDGEDITGLPPHRIArlgiGYVPEGrRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcGTLTVREQLTYTAHMRMKNATVQQKMERVEN---VLRDMnltdcQNTLIGipnRMKGisiGEKKRLAFACEILTDPKI 199
Cdd:COG0410 90 F-PSLTVEENLLLGAYARRDRAEVRADLERVYElfpRLKER-----RRQRAG---TLSG---GEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVV---LHQpsstVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVeqnARF----ALEIADRAYVLERGRIVLEGTAAEL 223
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
51-242 |
3.16e-23 |
|
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: 98.84 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNG---KKITKQKMRQMCAYV-QQVDLF-- 123
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFyDVSS----GSILIDGqdiREVTLDSLRRAIGVVpQDTVLFnd 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 -------CGTLTVREQLTYTAhmrmknATVQQKMERVenvlrdMNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILTD 196
Cdd:cd03253 90 tigynirYGRPDATDEEVIEA------AKAAQIHDKI------MRFPDGYDTIVG--ERGLKLSGGEKQRVAIARAILKN 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSSTV 242
Cdd:cd03253 156 PPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIV 200
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
47-261 |
6.14e-23 |
|
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: 98.07 E-value: 6.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNG---KKITKQKMRQMCAYVQQ-VD 121
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFyDVDS----GRILIDGhdvRDYTLASLRRQIGLVSQdVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGtlTVREQLTYTAHmrmkNATvqqkMERVENVLRD-------MNLTDCQNTLIGipNRMKGISIGEKKRLAFACEIL 194
Cdd:cd03251 87 LFND--TVAENIAYGRP----GAT----REEVEEAARAanahefiMELPEGYDTVIG--ERGVKLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 195 TDPKILFCDEPTSGLDAfmASE-VVRALLDLANKGKTIIVVLHQpSSTVfRMFHKVCFMATGKTVYHG 261
Cdd:cd03251 155 KDPPILILDEATSALDT--ESErLVQAALERLMKNRTTFVIAHR-LSTI-ENADRIVVLEDGKIVERG 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
45-236 |
1.82e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.08 E-value: 1.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQkmRQMCAYVQQVDlfc 124
Cdd:COG1116 18 PTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEK---PTSGEVLVDGKPVTGP--GPDRGVVFQEP--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 gTL----TVREQLTYtaHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:COG1116 90 -ALlpwlTVLDNVAL--GLELRGVPKAERRERARELLELVGLAGFEDAY---PHQLSG---GMRQRVAIARALANDPEVL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLH 236
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTH 197
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
48-236 |
7.25e-22 |
|
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: 95.49 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKeVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA---HLDTngveylGDVTVNGKKITKQKMRQMCAY-----VQQ 119
Cdd:COG0411 15 GGLV-AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITgfyRPTS------GRILFDGRDITGLPPHRIARLgiartFQN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFcGTLTVREQLTYTAHMRMKNATVQQK-------------MERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKR 186
Cdd:COG0411 88 PRLF-PELTVLENVLVAAHARLGRGLLAALlrlprarreereaRERAEELLERVGLADRADEPAG------NLSYGQQRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 808355238 187 LAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLH 236
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEH 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
45-256 |
4.47e-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: 90.74 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVTVNgkKITKQKMRQMCAYV-QQVD 121
Cdd:cd03246 9 RYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlrPTSGRVRLDGADIS--QWDPNELGDHVGYLpQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTLTvreqltytahmrmknatvqqkmervENVLrdmnltdcqntligipnrmkgiSIGEKKRLAFACEILTDPKILF 201
Cdd:cd03246 87 LFSGSIA-------------------------ENIL----------------------SGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSstVFRMFHKVCFMATGK 256
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE--TLASADRILVLEDGR 172
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
63-261 |
5.05e-21 |
|
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: 91.97 E-value: 5.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PGEVLALMGGSGAGKTTLMNILAHLDT--NGVEYLGDVTVNG--KKITKQKMRQMCAYV-QQVDLFcGTLTVREQLTYTa 137
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKpdGGTIVLNGTVLFDsrKKINLPPQQRKIGLVfQQYALF-PHLNVRENLAFG- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 138 hmrMKNATVQQKMERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEV 217
Cdd:cd03297 100 ---LKRKRNREDRISVDELLDLLGLDHLLNRYPA------QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 808355238 218 VRALLDL-ANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03297 171 LPELKQIkKNLNIPVIFVTHDLSE-AEYLADRIVVMEDGRLQYIG 214
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
48-238 |
6.45e-21 |
|
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: 96.66 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAH-LDTNGveylGDVTVNGKKITKQKMRQMCAYV----QQVDL 122
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGlLDPLQ----GEVTLDGVPVSSLDQDEVRRRVsvcaQDAHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcGTlTVREQLTYTAhmrmKNATVQQKME-----RVENVLRDmnLTDCQNTLIGipNRMKGISIGEKKRLAFACEILTDP 197
Cdd:TIGR02868 421 F-DT-TVRENLRLAR----PDATDEELWAalervGLADWLRA--LPDGLDTVLG--EGGARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDlANKGKTIIVVLHQP 238
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
49-266 |
6.63e-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: 6.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD-------TNGVEYLGDVTVNGKKITKQKMRQMCAYV-QQV 120
Cdd:cd03260 11 GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgapDEGEVLLDGKDIYDLDVDVLELRRRVGMVfQKP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFcgTLTVREQLTYTA-HMRMKNAtvQQKMERVENVLRDMNLTDCQNtligipNRMK--GISIGEKKRLAFACEILTDP 197
Cdd:cd03260 91 NPF--PGSIYDNVAYGLrLHGIKLK--EELDERVEEALRKAALWDEVK------DRLHalGLSGGQQQRLCLARALANEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKgKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQ-AARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
49-261 |
6.94e-21 |
|
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: 91.66 E-value: 6.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQKM--RQMCAYVQQVDLF 123
Cdd:cd03266 16 KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLlepDA------GFATVDGFDVVKEPAeaRRRLGFVSDSTGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVREQLTYTAHMR-MKNATVQQKMERVENVLRDMNLTDcqntligipNRMKGISIGEKKRLAFACEILTDPKILFC 202
Cdd:cd03266 90 YDRLTARENLEYFAGLYgLKGDELTARLEELADRLGMEELLD---------RRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 203 DEPTSGLDAFMAS---EVVRALLDLankGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03266 161 DEPTTGLDVMATRalrEFIRQLRAL---GKCILFSTHI-MQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
64-256 |
7.19e-21 |
|
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: 91.32 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK------MRQMCAYVQQVDLFCGTLTVREQLTYTa 137
Cdd:cd03292 27 GEFVFLVGPSGAGKSTLLKLIYKEELPTS---GTIRVNGQDVSDLRgraipyLRRKIGVVFQDFRLLPDRNVYENVAFA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 138 hMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNrmkGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEV 217
Cdd:cd03292 103 -LEVTGVPPREIRKRVPAALELVGLSHKHRAL---PA---ELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 218 VRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGK 256
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHA-KELVDTTRHRVIALERGK 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
48-236 |
1.30e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 87.80 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQKMRQMCAYVQQVdlfcG 125
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLY-----GEERPtsGQVLVNGQDLSRLKRREIPYLRRRI----G 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 T----------LTVREQLTYTahMRMKNATVQQKMERVENVLRdmnltdcqntLIGIPNRMKGI----SIGEKKRLAFAC 191
Cdd:COG2884 83 VvfqdfrllpdRTVYENVALP--LRVTGKSRKEIRRRVREVLD----------LVGLSDKAKALphelSGGEQQRVAIAR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 808355238 192 EILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATH 195
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
49-266 |
1.47e-19 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 87.98 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQKMRQ-----MCAYVQQVD 121
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIV-----GLVKPdsGKILLDGQDITKLPMHKrarlgIGYLPQEAS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFcGTLTVREQLtyTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTligipnrmKGISI--GEKKRLAFACEILTDPKI 199
Cdd:cd03218 86 IF-RKLTVEENI--LAVLEIRGLSKKEREEKLEELLEEFHITHLRKS--------KASSLsgGERRRVEIARALATNPKF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTvFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03218 155 LLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRET-LSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
64-261 |
2.05e-19 |
|
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: 87.16 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKM--RQMCAYVQQVDLFcGTLTVREQLTYTAHMRM 141
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFET---PQSGRVLINGVDVTAAPPadRPVSMLFQENNLF-AHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 142 KNATVQQkmERVENVLRDMNLtdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRAL 221
Cdd:cd03298 100 KLTAEDR--QAIEVALARVGL---AGLEKRLPGELSG---GERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 808355238 222 LDL-ANKGKTIIVVLHQPSSTVfRMFHKVCFMATGKTVYHG 261
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAK-RLAQRVVFLDNGRIAAQG 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
48-266 |
3.68e-19 |
|
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: 87.24 E-value: 3.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVTVNGKKITK-QKMRQMCAYV-QQVDLF 123
Cdd:cd03256 11 PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLvePTSGSVLIDGTDINKLKGKAlRQLRRQIGMIfQQFNLI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 cGTLTVRE-----QLTYTAHMR--MKNATVQQKmERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTD 196
Cdd:cd03256 91 -ERLSVLEnvlsgRLGRRSTWRslFGLFPKEEK-QRALAALERVGLLDKAYQ------RADQLSGGQQQRVAIARALMQQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLA-NKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03256 163 PKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQV-DLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
51-236 |
4.18e-19 |
|
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: 87.00 E-value: 4.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQKMRqmcaYVQQVDLFCGT---- 126
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTS---GEVRVAGLVPWKRRKK----FLRRIGVVFGQktql 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 ---LTVREQLTYTAHM-RMKNATVQQKMERVENVLrdmNLTDcqntLIGIPNRMkgISIGEKKRLAFACEILTDPKILFC 202
Cdd:cd03267 107 wwdLPVIDSFYLLAAIyDLPPARFKKRLDELSELL---DLEE----LLDTPVRQ--LSLGQRMRAEIAAALLHEPEILFL 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 203 DEPTSGLDAFmASEVVRALLDLANK--GKTIIVVLH 236
Cdd:cd03267 178 DEPTIGLDVV-AQENIRNFLKEYNRerGTTVLLTSH 212
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
51-261 |
1.00e-18 |
|
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: 84.29 E-value: 1.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNgveyLGDVTVNGKKIT---KQKMRQMCAYVQQVDLFCGT 126
Cdd:cd03247 15 QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTgDLKPQ----QGEITLDGVPVSdleKALSSLISVLNQRPYLFDTT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LtvreqltytahmrMKNatvqqkmervenvlrdmnltdcqntlIGIPnrmkgISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03247 91 L-------------RNN--------------------------LGRR-----FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 207 SGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSStvFRMFHKVCFMATGKTVYHG 261
Cdd:cd03247 127 VGLDPITERQLLSLIFEVL-KDKTLIWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
49-237 |
1.81e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 85.14 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKITKQKMRQMCAYV-QQVDLFcG 125
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEeiTSGDLIVDGLKVNDPKVDERLIRQEAGMVfQQFYLF-P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK09493 91 HLTALENVMF-GPLRVRGASKEEAEKQARELLAKVGLAERAHHY---PSELSG---GQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHE 195
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
51-239 |
1.92e-18 |
|
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: 84.56 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVTVngKKITKQKMRQMCAYVQQ-VDLFCGTL 127
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLykPTSGSVLLDGTDI--RQLDPADLRRNIGYVPQdVTLFYGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 tvREQLTytahMRMKNATVQQKMERVEN------VLRDMNLTDCQntligIPNRMKGISIGEKKRLAFACEILTDPKILF 201
Cdd:cd03245 95 --RDNIT----LGAPLADDERILRAAELagvtdfVNKHPNGLDLQ-----IGERGRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 808355238 202 CDEPTSGLDafMASE--VVRALLDLAnKGKTIIVVLHQPS 239
Cdd:cd03245 164 LDEPTSAMD--MNSEerLKERLRQLL-GDKTLIIITHRPS 200
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
53-261 |
2.90e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.73 E-value: 2.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNGveylGDVTVNGKKITK---QKMRQMCAYV-QQVDLFCGTL 127
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTrAWDPQQ----GEILLNGQPIADyseAALRQAISVVsQRVHLFSATL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 tvREQLTYTAHmrmkNATVQQKMERVENV-LRDMnLTDCQ--NTLIGIPNRMkgISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:PRK11160 431 --RDNLLLAAP----NASDEALIEVLQQVgLEKL-LEDDKglNAWLGEGGRQ--LSGGEQRRLGIARALLHDAPLLLLDE 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 205 PTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQpsSTVFRMFHKVCFMATGKTVYHG 261
Cdd:PRK11160 502 PTEGLDAETERQILELLAEHA-QNKTVLMITHR--LTGLEQFDRICVMDNGQIIEQG 555
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
47-266 |
4.80e-18 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 83.69 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtnGVEYLGDVTVNGKKIT---KQKMRQMCAYVQQVD-L 122
Cdd:cd03252 11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRF---YVPENGRVLVDGHDLAladPAWLRRQVGVVLQENvL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTYTAhmrmknatvqQKMERVENVLR-------DMNLTDCQNTLIGipNRMKGISIGEKKRLAFACEILT 195
Cdd:cd03252 88 FNRSIRDNIALADPG----------MSMERVIEAAKlagahdfISELPEGYDTIVG--EQGAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQpSSTVfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHR-LSTV-KNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
44-261 |
6.61e-18 |
|
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: 82.97 E-value: 6.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 44 PQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKkitkqkmrqmcayvqqVD 121
Cdd:cd03220 28 RKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLA-----GIYPPdsGTVTVRGR----------------VS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 L-------FCGTLTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEIL 194
Cdd:cd03220 87 SllglgggFNPELTGRENIYLNG--RLLGLSRKEIDEKIDEIIEFSELGDFIDL------PVKTYSSGMKARLAFAIATA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHG 261
Cdd:cd03220 159 LEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSS-IKRLCDRALVLEKGKIRFDG 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
49-236 |
7.13e-18 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 84.75 E-value: 7.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQ--KMRQMCAYVQQvdlfcgT 126
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTS---GTARVAGYDVVREprKVRRSIGIVPQ------Y 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMRMKNATV----QQKMERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFC 202
Cdd:TIGR01188 75 ASVDEDLTGRENLEMMGRLYglpkDEAEERAEELLELFELGEAADRPVG------TYSGGMRRRLDIAASLIHQPDVLFL 148
|
170 180 190
....*....|....*....|....*....|....
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:TIGR01188 149 DEPTTGLDPRTRRAIWDYIRALKEEGVTILLTTH 182
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
49-236 |
9.60e-18 |
|
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: 82.42 E-value: 9.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGveylgDVTVNGKKITKQ--KMRQMCAYVQQvdlfc 124
Cdd:cd03265 11 GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLlkPTSG-----RATVAGHDVVREprEVRRRIGIVFQ----- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 gTLTVREQLTYTAHM----RMKNATVQQKMERVENVLRDMNLTDCQNTLIgipnrmKGISIGEKKRLAFACEILTDPKIL 200
Cdd:cd03265 81 -DLSVDDELTGWENLyihaRLYGVPGAERRERIDELLDFVGLLEAADRLV------KTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 201 FCDEPTSGLDAFMAS---EVVRALLDlaNKGKTIIVVLH 236
Cdd:cd03265 154 FLDEPTIGLDPQTRAhvwEYIEKLKE--EFGMTILLTTH 190
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
49-265 |
1.02e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 83.24 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGveYL----GDVTVNGKKITKQKMRQMCAY--V--QQV 120
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLT-----G--ELtpssGEVRLNGRPLAAWSPWELARRraVlpQHS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DL-FcgTLTVRE--QLTYTAHMRMK---NATVQQKMERVenvlrdmnltDCQ-------NTLIGipnrmkgisiGEKKRL 187
Cdd:COG4559 85 SLaF--PFTVEEvvALGRAPHGSSAaqdRQIVREALALV----------GLAhlagrsyQTLSG----------GEQQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 188 AFA---CEILTD----PKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVfrMF-HKVCFMATGKTVY 259
Cdd:COG4559 143 QLArvlAQLWEPvdggPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAA--QYaDRILLLHQGRLVA 220
|
....*.
gi 808355238 260 HGAVDR 265
Cdd:COG4559 221 QGTPEE 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
48-266 |
2.12e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 85.78 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNIL--AHLDTNGVeylgdVTVNG---KKITKQKMRQMCAYV-QQVD 121
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLqrVFDPQSGR-----ILIDGtdiRTVTRASLRRNIAVVfQDAG 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFcgTLTVREQL-----TYT-AHMR--MKNATVQQKMERVEnvlrdmnltDCQNTLIGIPNRMkgISIGEKKRLAFACEI 193
Cdd:PRK13657 420 LF--NRSIEDNIrvgrpDATdEEMRaaAERAQAHDFIERKP---------DGYDTVVGERGRQ--LSGGERQRLAIARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355238 194 LTDPKILFCDEPTSGLDAfmASEV-VRALLDLANKGKTIIVVLHQpSSTVfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK13657 487 LKDPPILILDEATSALDV--ETEAkVKAALDELMKGRTTFIIAHR-LSTV-RNADRILVFDNGRVVESGSFDEL 556
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
49-237 |
2.12e-17 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 2.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKIT--KQKMRQM-CAYVQQVDLFCG 125
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSE---GSIVVNGQTINlvRDKDGQLkVADKNQLRLLRT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLT-VREQLTYTAHM----RMKNATVQ----QKMERVENVLRDMNLtdcqntlIGIPNRMKG-----ISIGEKKRLAFAC 191
Cdd:PRK10619 93 RLTmVFQHFNLWSHMtvleNVMEAPIQvlglSKQEARERAVKYLAK-------VGIDERAQGkypvhLSGGQQQRVSIAR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 808355238 192 EILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHE 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
49-236 |
3.41e-17 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 83.61 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQK--MRQMcAYV-QQVDLF 123
Cdd:COG3842 16 GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIA-----GFETPdsGRILLDGRDVTGLPpeKRNV-GMVfQDYALF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 cGTLTVREQLTYtaHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCD 203
Cdd:COG3842 90 -PHLTVAENVAF--GLRMRGVPKAEIRARVAELLELVGLEGLADRY---PHQLSG---GQQQRVALARALAPEPRVLLLD 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 808355238 204 EPTSGLDAF----MASEVVRALLDLankGKTIIVVLH 236
Cdd:COG3842 161 EPLSALDAKlreeMREELRRLQREL---GITFIYVTH 194
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
52-236 |
3.51e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMnilahLDTNGV--EYLGDVTVNGKKITKQK-----MRQMCAYV-QQVD-- 121
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLF-----LHFNGIlkPTSGEVLIKGEPIKYDKkslleVRKTVGIVfQNPDdq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTltVREQLTY-TAHMRMKNATVQqkmERVENVLRDMNLTDCQNTligIPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:PRK13639 91 LFAPT--VEEDVAFgPLNLGLSKEEVE---KRVKEALKAVGMEGFENK---PPHHLSG---GQKKRVAIAGILAMKPEII 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTH 195
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
45-236 |
3.58e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.60 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKMRQMC---AYVQQVD 121
Cdd:PRK11231 9 TVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLT---PQSGTVFLGDKPISMLSSRQLArrlALLPQHH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTLTVREQLTY--TAHM----RMK---NATVQQKMERVE-NVLRDMNLTDcqntligipnrmkgISIGEKKRLAFAC 191
Cdd:PRK11231 86 LTPEGITVRELVAYgrSPWLslwgRLSaedNARVNQAMEQTRiNHLADRRLTD--------------LSGGQRQRAFLAM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 808355238 192 EILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLH 196
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
49-236 |
3.73e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTngveYLGDVTVNGKKITKQKMRQMCAYV----QQVDL- 122
Cdd:PRK13548 13 GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSgELSP----DSGEVRLNGRPLADWSPAELARRRavlpQHSSLs 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcgTLTVREqltyTAHM-RMKNATVQQKMERVenVLRDMNLTDCQN-------TLIGipnrmkgisiGEKKRLAFAcEIL 194
Cdd:PRK13548 89 F--PFTVEE----VVAMgRAPHGLSRAEDDAL--VAAALAQVDLAHlagrdypQLSG----------GEQQRVQLA-RVL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 808355238 195 T-------DPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:PRK13548 150 AqlwepdgPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLH 199
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
34-239 |
4.68e-17 |
|
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: 80.94 E-value: 4.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 34 IAWSGLVATVPQaGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKqkM--- 110
Cdd:COG4181 9 IELRGLTKTVGT-GAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTS---GTVRLAGQDLFA--Lded 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 111 ------RQMCAYVQQVDLFCGTLTVREQLTYTAHMR-MKNAtvqqkMERVENVLRDMNLTDcqntligipnRM----KGI 179
Cdd:COG4181 83 ararlrARHVGFVFQSFQLLPTLTALENVMLPLELAgRRDA-----RARARALLERVGLGH----------RLdhypAQL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 180 SIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPS 239
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPA 208
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
49-236 |
5.06e-17 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 79.39 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGV--EYLGDVTVNGKKITKQK-----MRQMCAYV-QQV 120
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHL-----NGLlrPQSGAVLIDGEPLDYSRkglleRRQRVGLVfQDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 D--LFcgTLTVREQLTYTA-HMRMKNATVQqkmERVENVLRDMNLTDCQNTLIGIpnrmkgISIGEKKRLAFACEILTDP 197
Cdd:TIGR01166 78 DdqLF--AADVDQDVAFGPlNLGLSEAEVE---RRVREALTAVGASGLRERPTHC------LSGGEKKRVAIAGAVAMRP 146
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILRRLRAEGMTVVISTH 185
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
62-266 |
8.04e-17 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 80.56 E-value: 8.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 62 EPGEVLALMGGSGAGKTTLMNILAHLDT--NGVEYLGDVTVNGKK-ITKQK-----MRQMCAYV-QQVDLFCGTlTVREQ 132
Cdd:PRK11264 27 KPGEVVAIIGPSGSGKTTLLRCINLLEQpeAGTIRVGDITIDTARsLSQQKglirqLRQHVGFVfQNFNLFPHR-TVLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 133 LTyTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAF 212
Cdd:PRK11264 106 II-EGPVIVKGEPKEEATARARELLAKVGLAGKETSY---PRRLSG---GQQQRVAIARALAMRPEVILFDEPTSALDPE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 808355238 213 MASEVVRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK11264 179 LVGEVLNTIRQLAQEKRTMVIVTHE-MSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
49-238 |
9.16e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 9.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngveyL----GDVTVNGKKITKQKMRQMCAYVQQVDLFC 124
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGL-------LppaaGTIKLDGGDIDDPDVAEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTAHMRmknatvQQKMERVENVLRDMNLTDcqntLIGIPNRMkgISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:PRK13539 86 PALTVAENLEFWAAFL------GGEELDIAAALEAVGLAP----LAHLPFGY--LSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 808355238 205 PTSGLDAfmASevVRALLDL----ANKGKTIIVVLHQP 238
Cdd:PRK13539 154 PTAALDA--AA--VALFAELirahLAQGGIVIAATHIP 187
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
49-276 |
1.16e-16 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 81.80 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK--MRQMCAYVQQVDLFCGT 126
Cdd:PRK13536 52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDA---GKITVLGVPVPARArlARARIGVVPQFDNLDLE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQL-TYTAHMRMKNATVQQKMERVENVLRDMNLTDCqntligipnRMKGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK13536 129 FTVRENLlVFGRYFGMSTREIEAVIPSLLEFARLESKADA---------RVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 206 TSGLDA---FMASEVVRALLdlaNKGKTIIVVLHQPSSTVfRMFHKVCFMATGKTVYHGAVDRL------CPFFDKLGPD 276
Cdd:PRK13536 200 TTGLDPharHLIWERLRSLL---ARGKTILLTTHFMEEAE-RLCDRLCVLEAGRKIAEGRPHALidehigCQVIEIYGGD 275
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
53-236 |
1.39e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 82.76 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVE--YLGDVTVNGKKI----TKQKMRQMCAYVQQ-VDLFcG 125
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILS-----GVYqpDSGEILLDGEPVrfrsPRDAQAAGIAIIHQeLNLV-P 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLtYTAHMRMKNATVQQK--MERVENVLRDMNLT-DcqntligiPN-RMKGISIGEKKRLAFACEILTDPKILF 201
Cdd:COG1129 93 NLSVAENI-FLGREPRRGGLIDWRamRRRARELLARLGLDiD--------PDtPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 202 CDEPTSGLDafmASEVVRaLLD----LANKGKTIIVVLH 236
Cdd:COG1129 164 LDEPTASLT---EREVER-LFRiirrLKAQGVAIIYISH 198
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
63-266 |
2.29e-16 |
|
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: 80.93 E-value: 2.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PG-EVLALMGGSGAGKTTLMNILAHLDT--NGVEYLGDVTVN--GKKITKQKMRQMCAYV-QQVDLFcGTLTVREQLTYT 136
Cdd:TIGR02142 21 PGqGVTAIFGRSGSGKTTLIRLIAGLTRpdEGEIVLNGRTLFdsRKGIFLPPEKRRIGYVfQEARLF-PHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 137 ahmrMKNATVQQKMERVENVLRDMNLtdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASE 216
Cdd:TIGR02142 100 ----MKRARPSERRISFERVIELLGI---GHLLGRLPGRLSG---GEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 808355238 217 VVRALLDLANK-GKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQE-VLRLADRVVVLEDGRVAAAGPIAEV 219
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
53-238 |
2.79e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 78.28 E-value: 2.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQ------KMR-QMCAYVQQVDLFCG 125
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSS---GEVSLVGQPLHQMdeearaKLRaKHVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAHMRMKNAtvQQKMERVENVLRDMNLTDcqnTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK10584 102 TLNALENVELPALLRGESS--RQSRNGAKALLEQLGLGK---RLDHLPAQLSG---GEQQRVALARAFNGRPDVLFADEP 173
|
170 180 190
....*....|....*....|....*....|....
gi 808355238 206 TSGLDAFMASEVVRALLDLANK-GKTIIVVLHQP 238
Cdd:PRK10584 174 TGNLDRQTGDKIADLLFSLNREhGTTLILVTHDL 207
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
53-293 |
3.46e-16 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 78.15 E-value: 3.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKIT--KQKMRQMcAYV-QQVDLFcGT 126
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFikpDS------GKILLNGKDITnlPPEKRDI-SYVpQNYALF-PH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03299 86 MTVYKNIAYG--LKKRKVDKKEIERKVLEIAEMLGIDHLLNRK---PETLSG---GEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 207 SGLDAfMASEVVRALLDLANK--GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGavdrlcpffdKLGPDFRVPESYN 284
Cdd:cd03299 158 SALDV-RTKEKLREELKKIRKefGVTVLHVTHD-FEEAWALADKVAIMLNGKLIQVG----------KPEEVFKKPKNEF 225
|
....*....
gi 808355238 285 PADFVMSEI 293
Cdd:cd03299 226 VAEFLGFNN 234
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
49-266 |
4.13e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 4.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNilaHLdtNGV--EYLGDVTVNGKKITKQKMRQMCAYV----QQVDL 122
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFR---HF--NGIlkPTSGSVLIRGEPITKENIREVRKFVglvfQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTY-TAHMRMKNATVQQkmeRVENVLRDMNLTDCQNTligIPNRMKGisiGEKKRLAFACEILTDPKILF 201
Cdd:PRK13652 90 QIFSPTVEQDIAFgPINLGLDEETVAH---RVSSALHMLGLEELRDR---VPHHLSG---GEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQ-LDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
62-266 |
4.58e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 62 EPGEVLALMGGSGAGKTTLMN-ILAHLdtngvEYLGDVTVNG---KKITKQKMRQMCAYV-QQVDLFCGTLtvREQLTyt 136
Cdd:PRK11174 374 PAGQRIALVGPSGAGKTSLLNaLLGFL-----PYQGSLKINGielRELDPESWRKHLSWVgQNPQLPHGTL--RDNVL-- 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 137 ahMRMKNATVQQkmerVENVLRDMN-------LTDCQNTLIGipNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK11174 445 --LGNPDASDEQ----LQQALENAWvseflplLPQGLDTPIG--DQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 210 DAFMASEVVRALLDlANKGKTIIVVLHQPSSTvfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK11174 517 DAHSEQLVMQALNA-ASRRQTTLMVTHQLEDL--AQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
49-228 |
5.81e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 77.76 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQKM----RQMCAYV-QQV 120
Cdd:COG1137 14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLvkpDS------GRIFLDGEDITHLPMhkraRLGIGYLpQEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFCGtLTVREQLtyTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTligipnrmKGISI--GEKKRLAFACEILTDPK 198
Cdd:COG1137 88 SIFRK-LTVEDNI--LAVLELRKLSKKEREERLEELLEEFGITHLRKS--------KAYSLsgGERRRVEIARALATNPK 156
|
170 180 190
....*....|....*....|....*....|
gi 808355238 199 ILFCDEPTSGLDAFMASEVVRALLDLANKG 228
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERG 186
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
49-236 |
6.01e-16 |
|
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: 77.76 E-value: 6.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQKM--RQMCAYVQQVDLFcGT 126
Cdd:cd03296 13 GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDS---GTILFGGEDATDVPVqeRNVGFVFQHYALF-RH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMRMKNATV--QQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDE 204
Cdd:cd03296 89 MTVFDNVAFGLRVKPRSERPpeAEIRAKVHELLKLVQLDWLADRY---PAQLSG---GQRQRVALARALAVEPKVLLLDE 162
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 205 PTSGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHDElHVTTVFVTH 195
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
48-266 |
7.72e-16 |
|
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: 77.34 E-value: 7.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEYL-GDVTVNGKKITKQ---KMRQMCAYV-QQVDL 122
Cdd:cd03295 11 GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRL----IEPTsGEIFIDGEDIREQdpvELRRKIGYViQQIGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcgtltvreqltytAHMRMKN--ATV--------QQKMERVENVLRDMNLtDCQNTLIGIPNRMKGisiGEKKRLAFACE 192
Cdd:cd03295 87 F-------------PHMTVEEniALVpkllkwpkEKIRERADELLALVGL-DPAEFADRYPHELSG---GQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 193 ILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSSTvFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEA-FRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
49-264 |
8.51e-16 |
|
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: 77.43 E-value: 8.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGVE---YLGDVTVNGKKITK---QKMRQMCAYV--QQV 120
Cdd:COG1119 14 GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLI-----TGDLpptYGNDVRLFGERRGGedvWELRKRIGLVspALQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFCGTLTVREQ-LT--YTAHMRMKNATVQQKmERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDP 197
Cdd:COG1119 89 LRFPRDETVLDVvLSgfFDSIGLYREPTDEQR-ERARELLELLGLAHLADRPFG------TLSQGEQRRVLIARALVKDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKG-KTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVD 264
Cdd:COG1119 162 ELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEE-IPPGITHVLLLKDGRVVAAGPKE 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
49-236 |
1.16e-15 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 76.51 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITK--QKMRQMCAYVQQVDLFcGT 126
Cdd:cd03300 11 GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTS---GEILLDGKDITNlpPHKRPVNTVFQNYALF-PH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:cd03300 87 LTVFENIAFG--LRLKKLPKAEIKERVAEALDLVQLEGYANRK---PSQLSG---GQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|.
gi 808355238 207 SGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElGITFVFVTH 189
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
51-236 |
1.45e-15 |
|
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: 75.64 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNGVEylGDVTVNGKKITKqkmrqmcayvqqvdlfcgtLTV 129
Cdd:cd03217 13 KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMgHPKYEVTE--GEILFKGEDITD-------------------LPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 REQltytAHMRMKNAtVQQKME----RVENVLRDMNltdcqntligipnrmKGISIGEKKRlafaCEILT----DPKILF 201
Cdd:cd03217 72 EER----ARLGIFLA-FQYPPEipgvKNADFLRYVN---------------EGFSGGEKKR----NEILQllllEPDLAI 127
|
170 180 190
....*....|....*....|....*....|....*
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITH 162
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
49-236 |
3.13e-15 |
|
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: 74.98 E-value: 3.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGkkiTKQKMRQMCAYVQQVDLFcGT 126
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEepTSGRIYIGGRDVTD---LPPKDRDIAMVFQNYALY-PH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMR-MKNATVQQKMERVENVLRDMNLTDcqntligipNRMKGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:cd03301 87 MTVYDNIAFGLKLRkVPKDEIDERVREVAELLQIEHLLD---------RKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190
....*....|....*....|....*....|....*
gi 808355238 206 TSGLDAF----MASEVVRALLDLankGKTIIVVLH 236
Cdd:cd03301 158 LSNLDAKlrvqMRAELKRLQQRL---GTTTIYVTH 189
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
52-258 |
3.27e-15 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 73.62 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA---HLDTngveylGDVTVNGKKITkqkmrqmcayvqqvdlfcgTLT 128
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSglyKPDS------GEILVDGKEVS-------------------FAS 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREqltytAHmRMKNATVQQkmervenvlrdmnltdcqntligipnrmkgISIGEKKRLAFACEILTDPKILFCDEPTSG 208
Cdd:cd03216 69 PRD-----AR-RAGIAMVYQ------------------------------LSVGERQMVEIARALARNARLLILDEPTAA 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 808355238 209 LDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTV 258
Cdd:cd03216 113 LTPAEVERLFKVIRRLRAQGVAVIFISHRL-DEVFEIADRVTVLRDGRVV 161
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
50-266 |
4.13e-15 |
|
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: 76.63 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVA---EPGEVLALMGGSGAGKTTLMNILAHL-DTNGVEYlGDVTVNGKKITKQKMRQM-------CAYVQ 118
Cdd:COG0444 14 RRGVVKAVDGVSfdvRRGETLGLVGESGSGKSTLARAILGLlPPPGITS-GEILFDGEDLLKLSEKELrkirgreIQMIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 119 Q--------VdlfcgtLTVREQL--TYTAHMRMKNAtvqQKMERVENVLRDMNLTDcqntligiPNRMKG-----ISIGE 183
Cdd:COG0444 93 QdpmtslnpV------MTVGDQIaePLRIHGGLSKA---EARERAIELLERVGLPD--------PERRLDrypheLSGGM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 184 KKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVV---LhqpsSTVFRMFHKVCFMATGKTVY 259
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFIthdL----GVVAEIADRVAVMYAGRIVE 231
|
....*..
gi 808355238 260 HGAVDRL 266
Cdd:COG0444 232 EGPVEEL 238
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
53-239 |
6.89e-15 |
|
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: 72.57 E-value: 6.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGveylgdvtvNGKkITKQKMRQMcAYVQQVDLFC-GTLtvRE 131
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG---------SGR-IGMPEGEDL-LFLPQRPYLPlGTL--RE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 132 QLTYTAHMrmknatvqqkmervenVLrdmnltdcqntligipnrmkgiSIGEKKRLAFACEILTDPKILFCDEPTSGLDA 211
Cdd:cd03223 83 QLIYPWDD----------------VL----------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180
....*....|....*....|....*....
gi 808355238 212 fmasEVVRALLDLANK-GKTIIVVLHQPS 239
Cdd:cd03223 125 ----ESEDRLYQLLKElGITVISVGHRPS 149
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
52-261 |
9.75e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 74.88 E-value: 9.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGV--EYLGDVTVNGKKITKQ-----KMRQMCAYV-QQVDLF 123
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNL-----NGIlkPSSGRILFDGKPIDYSrkglmKLRESVGMVfQDPDNQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVREQLTYTA-HMRMKNATVQqkmERVENVLRDMNLTDCQNTligiPNRMkgISIGEKKRLAFACEILTDPKILFC 202
Cdd:PRK13636 95 LFSASVYQDVSFGAvNLKLPEDEVR---KRVDNALKRTGIEHLKDK----PTHC--LSFGQKKRVAIAGVLVMEPKVLVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:PRK13636 166 DEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHD-IDIVPLYCDNVFVMKEGRVILQG 224
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
49-211 |
1.13e-14 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 73.28 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMN-ILAHLDTnGVEYLGDVTVNGKKITKQKM--RQMcAYVQQVDLFCG 125
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSP-AFSASGEVLLNGRRLTALPAeqRRI-GILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAHMRMKNAtvqQKMERVENVLRDMNLTDCQN----TLIGipnrmkgisiGEKKRLAFACEILTDPKILF 201
Cdd:COG4136 90 HLSVGENLAFALPPTIGRA---QRRARVEQALEEAGLAGFADrdpaTLSG----------GQRARVALLRALLAEPRALL 156
|
170
....*....|
gi 808355238 202 CDEPTSGLDA 211
Cdd:COG4136 157 LDEPFSKLDA 166
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
52-236 |
1.60e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 74.39 E-value: 1.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLmniLAHLdtNGVeYL---GDVTVNGKKITK---QKMRQMCAYV-QQVD--L 122
Cdd:PRK13647 19 KALKGLSLSIPEGSKTALLGPNGAGKSTL---LLHL--NGI-YLpqrGRVKVMGREVNAeneKWVRSKVGLVfQDPDdqV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTltVREQLTY-TAHMRMKNATVQqkmERVENVLRDMNLTDCQNTligIPNRMkgiSIGEKKRLAFACEILTDPKILF 201
Cdd:PRK13647 93 FSST--VWDDVAFgPVNMGLDKDEVE---RRVEEALKAVRMWDFRDK---PPYHL---SYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 202 CDEPTSGLDAfMASEVVRALLD-LANKGKTIIVVLH 236
Cdd:PRK13647 162 LDEPMAYLDP-RGQETLMEILDrLHNQGKTVIVATH 196
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-263 |
1.74e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 73.79 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEYL------GDVTVNGKKITKQ---KMRQMCAYVQQ 119
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRL----IELYpearvsGEVYLDGQDIFKMdviELRRRVQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFCGTLTVREQLTYTAHMRMKNATVQQKMERVENVLRDMNLTD-CQNTLIGIPNRMKGisiGEKKRLAFACEILTDPK 198
Cdd:PRK14247 90 IPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWDeVKDRLDAPAGKLSG---GQQQRLCIARALAFQPE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 199 ILFCDEPTSGLDAFMASEVVRALLDLaNKGKTIIVVLHQPSSTVfRMFHKVCFMATGKTVYHGAV 263
Cdd:PRK14247 167 VLLADEPTANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAA-RISDYVAFLYKGQIVEWGPT 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
49-236 |
2.28e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.72 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKITKqkmRQMcAYV-QQVDLFcG 125
Cdd:COG3839 14 GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEdpTSGEILIGGRDVTDLPPKD---RNI-AMVfQSYALY-P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtaHMRMKNATVQQKMERVENVLRDMNLTDCqntLigipNRM-KGISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:COG3839 89 HMTVYENIAF--PLKLRKVPKAEIDRRVREAAELLGLEDL---L----DRKpKQLSGGQRQRVALGRALVREPKVFLLDE 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 205 PTSGLDAF----MASEVVRALLDLankGKTIIVVLH 236
Cdd:COG3839 160 PLSNLDAKlrveMRAEIKRLHRRL---GTTTIYVTH 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
51-238 |
2.40e-14 |
|
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: 75.99 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDtngvEYLGDvtvNGKKITKQKMRQMCAYV-------QQVDLF 123
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD----QYEPT---SGRIIYHVALCEKCGYVerpskvgEPCPVC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVRE------QLTYTAHMRMKNATVQQKM------ERV-ENVLRDMN---------------LTDcqntLIGIPNR 175
Cdd:TIGR03269 86 GGTLEPEEvdfwnlSDKLRRRIRKRIAIMLQRTfalygdDTVlDNVLEALEeigyegkeavgravdLIE----MVQLSHR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 176 MKGI----SIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLA-NKGKTIIVVLHQP 238
Cdd:TIGR03269 162 ITHIardlSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWP 229
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
49-255 |
2.57e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 73.27 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTN-GVEYLGDVTVNGKKI------TKQKMRQMCAYVQQV 120
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMnDLNpEVTITGSIVYNGHNIysprtdTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFcgTLTVREQLTYTahMRMKNATVQQKM-ERVENVLRDMNLTDcqntliGIPNRMK----GISIGEKKRLAFACEILT 195
Cdd:PRK14239 96 NPF--PMSIYENVVYG--LRLKGIKDKQVLdEAVEKSLKGASIWD------EVKDRLHdsalGLSGGQQQRVCIARVLAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKgKTIIVVLH--QPSStvfRMFHKVCFMATG 255
Cdd:PRK14239 166 SPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRsmQQAS---RISDRTGFFLDG 223
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
51-266 |
3.00e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 76.30 E-value: 3.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNGKKITKQK----MRQMCAYVQQVDLFCG 125
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLyQPTG----GQVLLDGVPLVQYDhhylHRQVALVGQEPVLFSG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 tlTVREQLTYtahmrmknATVQQKMERVENVLRD-------MNLTDCQNTLIGipnrMKG--ISIGEKKRLAFACEILTD 196
Cdd:TIGR00958 570 --SVRENIAY--------GLTDTPDEEIMAAAKAanahdfiMEFPNGYDTEVG----EKGsqLSGGQKQRIAIARALVRK 635
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 197 PKILFCDEPTSGLDAfmasEVVRALLDLAN-KGKTIIVVLHQpSSTVfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:TIGR00958 636 PRVLILDEATSALDA----ECEQLLQESRSrASRTVLLIAHR-LSTV-ERADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
49-276 |
3.17e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 73.69 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQ--KMRQMCAYVQQVDLFCGT 126
Cdd:PRK13537 18 GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDA---GSISLCGEPVPSRarHARQRVGVVPQFDNLDPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:PRK13537 95 FTVRENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADA------KVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 207 SGLDA---FMASEVVRALLdlaNKGKTIIVVLHQPSSTVfRMFHKVCFMATGKTVYHGAVDRL------CPFFDKLGPD 276
Cdd:PRK13537 167 TGLDPqarHLMWERLRSLL---ARGKTILLTTHFMEEAE-RLCDRLCVIEEGRKIAEGAPHALieseigCDVIEIYGPD 241
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
55-236 |
3.59e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 55 RNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKIT----KQKMRQ---McayVQQ----VD 121
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILY-----GLYQPdsGEILIDGKPVRirspRDAIALgigM---VHQhfmlVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 lfcgTLTVREQL------TYTAHMRMKNATvqqkmERVENVLRDMNLT-DcqntligiPNRM-KGISIGEKKRLafacEI 193
Cdd:COG3845 94 ----NLTVAENIvlglepTKGGRLDRKAAR-----ARIRELSERYGLDvD--------PDAKvEDLSVGEQQRV----EI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 808355238 194 L----TDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:COG3845 153 LkalyRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITH 199
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
45-266 |
3.99e-14 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 73.96 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTL---MNILAHLDTngveylGDVTVNGKKITK------QKMRQMCA 115
Cdd:COG1135 12 PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLircINLLERPTS------GSVLVDGVDLTAlserelRAARRKIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 116 YV-QQVDLFcGTLTVREQLTYTahmrMKNATV--QQKMERVENVLRdmnltdcqntLIGIPNRMKG----ISIGEKKRLA 188
Cdd:COG1135 86 MIfQHFNLL-SSRTVAENVALP----LEIAGVpkAEIRKRVAELLE----------LVGLSDKADAypsqLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 189 FACEILTDPKILFCDEPTSGLDafmaSEVVRALLDL---ANK--GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAV 263
Cdd:COG1135 151 IARALANNPKVLLCDEATSALD----PETTRSILDLlkdINRelGLTIVLITHE-MDVVRRICDRVAVLENGRIVEQGPV 225
|
...
gi 808355238 264 DRL 266
Cdd:COG1135 226 LDV 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
39-273 |
4.63e-14 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 72.42 E-value: 4.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 39 LVATVPQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEY--LGDVTVNGKkitkqkmrqmCAY 116
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIA-----GILEptSGRVEVNGR----------VSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 VqqVDL---FCGTLTVREQLTYTAH-MRMKNATVQQKMERVENV--LRDmnltdcqntLIGIPnrMKGISIGEKKRLAFA 190
Cdd:COG1134 92 L--LELgagFHPELTGRENIYLNGRlLGLSRKEIDEKFDEIVEFaeLGD---------FIDQP--VKTYSSGMRARLAFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 191 CEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPsSTVFRMFHKVCFMATGKTVYHGAVDRLCPFF 270
Cdd:COG1134 159 VATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSM-GAVRRLCDRAIWLEKGRLVMDGDPEEVIAAY 237
|
...
gi 808355238 271 DKL 273
Cdd:COG1134 238 EAL 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
51-239 |
7.14e-14 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.46 E-value: 7.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTV-NGKKIT--KQKmrqmcAYVQQvdlfcGTL 127
Cdd:COG4178 376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGS---GRIARpAGARVLflPQR-----PYLPL-----GTL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 tvREQLTYTAHMRmknatvQQKMERVENVLRDMNLTDCQNTLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:COG4178 443 --REALLYPATAE------AFSDAELREALEAVGLGHLAERLDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATS 514
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 208 GLDAFMASEVVRALLDlANKGKTIIVVLHQPS 239
Cdd:COG4178 515 ALDEENEAALYQLLRE-ELPGTTVISVGHRST 545
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
49-233 |
7.74e-14 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 73.26 E-value: 7.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDT--NGVEYLGDVTVNGKKITKQkmRQMcAYV-QQVDLFcG 125
Cdd:COG1118 13 GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETpdSGRIVLNGRDLFTNLPPRE--RRV-GFVfQHYALF-P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtaHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFAcEIL-TDPKILFCDE 204
Cdd:COG1118 89 HMTVAENIAF--GLRVRPPSKAEIRARVEELLELVQLEGLADRY---PSQLSG---GQRQRVALA-RALaVEPEVLLLDE 159
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 205 PTSGLDAFMASEV---VRALLDlANKGKTIIV 233
Cdd:COG1118 160 PFGALDAKVRKELrrwLRRLHD-ELGGTTVFV 190
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
49-258 |
1.05e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.41 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLM---NILAHLDTNG-VEylGDVTVNGKKITKQKM-----RQMCAYVQQ 119
Cdd:PRK14267 15 GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArVE--GEVRLFGRNIYSPDVdpievRREVGMVFQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFCGTLTVREQLTYTAHMrmkNATVQQKME---RVENVLRDMNLTD-CQNTLIGIPNRMKGisiGEKKRLAFACEILT 195
Cdd:PRK14267 93 YPNPFPHLTIYDNVAIGVKL---NGLVKSKKEldeRVEWALKKAALWDeVKDRLNDYPSNLSG---GQRQRLVIARALAM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKgKTIIVVLHQPSSTVfRMFHKVCFMATGKTV 258
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAA-RVSDYVAFLYLGKLI 227
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
50-238 |
1.93e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHldtngvEYLGDVTVNGKKITKQKMRQMCAYVQQVDlfcgtltv 129
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG------ALKGTPVAGCVDVPDNQFGREASLIDAIG-------- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 reqltytahmrmKNATVQQKMErvenVLRDMNLTDCQNTLigipNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:COG2401 108 ------------RKGDFKDAVE----LLNAVGLSDAVLWL----RRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190
....*....|....*....|....*....|
gi 808355238 210 DAFMASEVVRALLDLANK-GKTIIVVLHQP 238
Cdd:COG2401 168 DRQTAKRVARNLQKLARRaGITLVVATHHY 197
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
51-238 |
2.08e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 70.48 E-value: 2.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLD---TNGveylgDVTVNGKKITKQKmrqmcayvqqVD----- 121
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMgHPKyevTSG-----SILLDGEDILELS----------PDerara 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 -LFCGT--------LTVREQLT--YTAHmRMKNATVQQKMERVENVLRDMnltdcqntliGIPNRM------KGISIGEK 184
Cdd:COG0396 78 gIFLAFqypveipgVSVSNFLRtaLNAR-RGEELSAREFLKLLKEKMKEL----------GLDEDFldryvnEGFSGGEK 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 185 KRLafacEILT----DPKILFCDEPTSGLD--AF-MASEVVRAlldLANKGKTIIVVLHQP 238
Cdd:COG0396 147 KRN----EILQmlllEPKLAILDETDSGLDidALrIVAEGVNK---LRSPDRGILIITHYQ 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
49-236 |
2.17e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.79 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAH---LDTngveylGDVTVnGKKITKqkmrqmcAYV-QQVDLFC 124
Cdd:COG0488 326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGelePDS------GTVKL-GETVKI-------GYFdQHQEELD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTAhmrmKNATVQQkmerVENVLRDMNLT-DCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCD 203
Cdd:COG0488 392 PDKTVLDELRDGA----PGGTEQE----VRGYLGRFLFSgDDAFKPVG------VLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190
....*....|....*....|....*....|....*
gi 808355238 204 EPTSGLDafMASevVRALLD-LAN-KGkTIIVVLH 236
Cdd:COG0488 458 EPTNHLD--IET--LEALEEaLDDfPG-TVLLVSH 487
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
49-307 |
2.31e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 71.67 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDtNGVEylGDVTVNGKKITKQKMRQ--MCAYVQQVDLFcGT 126
Cdd:PRK11432 17 GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLE-KPTE--GQIFIDGEDVTHRSIQQrdICMVFQSYALF-PH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTahMRMKNATVQQKMERVENVLRdmnLTDcqntLIGIPNR-MKGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK11432 93 MSLGENVGYG--LKMLGVPKEERKQRVKEALE---LVD----LAGFEDRyVDQISGGQQQRVALARALILKPKVLLFDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 206 TSGLDAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRLcpffdklgpdFRVPESYN 284
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHD-QSEAFAVSDTVIVMNKGKIMQIGSPQEL----------YRQPASRF 232
|
250 260
....*....|....*....|...
gi 808355238 285 PADFvMSEISISPETEQEDVTRI 307
Cdd:PRK11432 233 MASF-MGDANIFPATLSGDYVDI 254
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
52-266 |
2.60e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.78 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEY--LGDVTVNGK---KITKQKMRQMCAY-VQQVDLFCG 125
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIA-----GIVPpdSGTLEIGGNpcaRLTPAKAHQLGIYlVPQEPLLFP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYtahmRMKNAtvQQKMERVENVLRDMNLT---DCQNTLIGIPNR-----MKGisigekkrlafaceILTDP 197
Cdd:PRK15439 100 NLSVKENILF----GLPKR--QASMQKMKQLLAALGCQldlDSSAGSLEVADRqiveiLRG--------------LMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPE-IRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
64-238 |
3.10e-13 |
|
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: 69.06 E-value: 3.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK--MRQMCAYVQQVDLFCGTLTVREQLTYtahMRM 141
Cdd:cd03231 26 GEALQVTGPNGSGKTTLLRILAGLSPPLA---GRVLLNGGPLDFQRdsIARGLLYLGHAPGIKTTLSVLENLRF---WHA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 142 KNATvqqkmERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRAL 221
Cdd:cd03231 100 DHSD-----EQVEEALARVGLNGFEDRPVA------QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*..
gi 808355238 222 LDLANKGKTIIVVLHQP 238
Cdd:cd03231 169 AGHCARGGMVVLTTHQD 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
49-236 |
3.27e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 3.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTV-NGKKItkqkmrqmcAYVQQVDLFCGTL 127
Cdd:COG0488 9 GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELE---PDSGEVSIpKGLRI---------GYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 TVREQLtYTAHMRMKNatVQQKMERVENVLRDMN-----LTDCQNTL------------------IGIPN-----RMKGI 179
Cdd:COG0488 77 TVLDTV-LDGDAELRA--LEAELEELEAKLAEPDedlerLAELQEEFealggweaearaeeilsgLGFPEedldrPVSEL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 180 SIGEKKRLAFACEILTDPKILFCDEPTSGLDAfmasEVVRALLD-LANKGKTIIVVLH 236
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDL----ESIEWLEEfLKNYPGTVLVVSH 207
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
53-256 |
3.32e-13 |
|
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: 69.42 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngveYL---GDVTVNGKKITKQK----MRQMCAYVQQVDLFCG 125
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENF------YQpqgGQVLLDGKPISQYEhkylHSKVSLVGQEPVLFAR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 tlTVREQLTY----TAHMRMKNAtvQQKMERVENVlrdMNLTDCQNTLIGipnrMKG--ISIGEKKRLAFACEILTDPKI 199
Cdd:cd03248 103 --SLQDNIAYglqsCSFECVKEA--AQKAHAHSFI---SELASGYDTEVG----EKGsqLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDlANKGKTIIVVLHQpSSTVFRMfHKVCFMATGK 256
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHR-LSTVERA-DQILVLDGGR 225
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
45-238 |
3.81e-13 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.45 E-value: 3.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLG--DV-TVNGKKITKQKmRQMCAYVQQ 119
Cdd:PRK10535 15 PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDkpTSGTYRVAgqDVaTLDADALAQLR-REHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFCGTLTVREQLTYTAhmRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKI 199
Cdd:PRK10535 94 RYHLLSHLTAAQNVEVPA--VYAGLERKQRLLRAQELLQRLGLEDRVEYQ---PSQLSG---GQQQRVSIARALMNGGQV 165
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQP 238
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDP 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
50-232 |
4.08e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 70.89 E-value: 4.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVA---EPGEVLALMGGSGAGKTTLMNILAhldtnGVeyL----GDVTVNGKKITKQKMrqmcAYVQQVDL 122
Cdd:COG4586 31 EYREVEAVDDISftiEPGEIVGFIGPNGAGKSTTIKMLT-----GI--LvptsGEVRVLGYVPFKRRK----EFARRIGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGT-------LTVREQLTYTAHM-RMKNATVQQKMERVENVLrdmNLTDcqntLIGIPNRMkgISIGEKKRlafaCEI- 193
Cdd:COG4586 100 VFGQrsqlwwdLPAIDSFRLLKAIyRIPDAEYKKRLDELVELL---DLGE----LLDTPVRQ--LSLGQRMR----CELa 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 808355238 194 ---LTDPKILFCDEPTSGLDAfMASEVVRALLDLANK--GKTII 232
Cdd:COG4586 167 aalLHRPKILFLDEPTIGLDV-VSKEAIREFLKEYNRerGTTIL 209
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
31-266 |
5.92e-13 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 69.34 E-value: 5.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 31 RKTIAWSGLVATVPQagggrkEVIRNVSGVAEPGEVLALMGGSGAGKTtlMNILAHLDT--NGVEYL-GDVTVNGKKITK 107
Cdd:PRK10418 2 PQQIELRNIALQAAQ------PLVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGIlpAGVRQTaGRVLLDGKPVAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 108 QKMR-QMCAYVQQV--DLFCGTLTVREQLTYTAHMRMKNATVQQKMErvenVLRDMNLTDCQNTLIGIPNRMKGisiGEK 184
Cdd:PRK10418 74 CALRgRKIATIMQNprSAFNPLHTMHTHARETCLALGKPADDATLTA----ALEAVGLENAARVLKLYPFEMSG---GML 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 185 KRLAFACEILTDPKILFCDEPTSGLDAfmaseVVRA-LLDL-----ANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTV 258
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDV-----VAQArILDLlesivQKRALGMLLVTHD-MGVVARLADDVAVMSHGRIV 220
|
....*...
gi 808355238 259 YHGAVDRL 266
Cdd:PRK10418 221 EQGDVETL 228
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
53-256 |
6.04e-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: 67.46 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQKMRQM----CAYV---QQVDLF 123
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALF-----GLRPPasGEITLDGKPVTRRSPRDAiragIAYVpedRKREGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVREQLTYTAHMRMKNatvQQKmervenvlrdmnltdcqntligipnrmkgisigekkrLAFACEILTDPKILFCD 203
Cdd:cd03215 90 VLDLSVAENIALSSLLSGGN---QQK-------------------------------------VVLARWLARDPRVLILD 129
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 204 EPTSGLDAFMASEVVRALLDLANKGKTIIVVlhqpSST---VFRMFHKVCFMATGK 256
Cdd:cd03215 130 EPTRGVDVGAKAEIYRLIRELADAGKAVLLI----SSEldeLLGLCDRILVMYEGR 181
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
45-236 |
8.73e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 68.30 E-value: 8.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKIT------KQKMR-QMCAYV 117
Cdd:PRK11629 16 QEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDT---PTSGDVIFNGQPMSklssaaKAELRnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 118 QQVDLFCGTLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDP 197
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMP--LLIGKKKPAEINSRALEMLAAVGLEHRAN------HRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLH 236
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH 204
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
54-240 |
1.13e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 1.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL-DTNGVEYLGDvTVNGKKITKQKMRQMCAYV-QQVDLFCGTLT--- 128
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFyDIDEGEILLD-GHDLRDYTLASLRNQVALVsQNVHLFNDTIAnni 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 --------VREQLTYTAHMrmknATVQQKMERVENVLrdmnltdcqNTLIGipnrMKGISI--GEKKRLAFACEILTDPK 198
Cdd:PRK11176 438 ayarteqySREQIEEAARM----AYAMDFINKMDNGL---------DTVIG----ENGVLLsgGQRQRIAIARALLRDSP 500
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 808355238 199 ILFCDEPTSGLDAfmASE-VVRALLDLANKGKTIIVVLHQPSS 240
Cdd:PRK11176 501 ILILDEATSALDT--ESErAIQAALDELQKNRTSLVIAHRLST 541
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
49-234 |
1.69e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 67.60 E-value: 1.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHlDTNGVEylGDVTVNGKKITK----QKMRQMCAYVQQVDLFC 124
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG-DPRATS--GRIVFDGKDITDwqtaKIMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTAHMRMKNaTVQQKMERVENVLRDMNLTDCQntligipnRMKGISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:PRK11614 93 SRMTVEENLAMGGFFAERD-QFQERIKWVYELFPRLHERRIQ--------RAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190
....*....|....*....|....*....|
gi 808355238 205 PTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
49-236 |
2.08e-12 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 67.42 E-value: 2.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL---DTngveylGDVTVNGKKITKQKMRQMC---AYVQQVDL 122
Cdd:COG4604 12 GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLlppDS------GEVLVDGLDVATTPSRELAkrlAILRQENH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVRE------------QLTytahmrmknatvQQKMERVENVLRDMNLTDCQN----TLIGipnrmkgisiGEKKR 186
Cdd:COG4604 86 INSRLTVRElvafgrfpyskgRLT------------AEDREIIDEAIAYLDLEDLADryldELSG----------GQRQR 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808355238 187 lAF-ACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLAN-KGKTIIVVLH 236
Cdd:COG4604 144 -AFiAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLH 194
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
53-236 |
2.09e-12 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 66.75 E-value: 2.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEYL-GDVTVNGKKITK---QKMRQMCAYV-QQVDLFCGtl 127
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRL----VELSsGSILIDGVDISKiglHDLRSRISIIpQDPVLFSG-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 TVREQL----TYTAhmrmknatvqqkmERVENVLRDMNLTDCQNTLIG-----IPNRMKGISIGEKKRLAFACEILTDPK 198
Cdd:cd03244 93 TIRSNLdpfgEYSD-------------EELWQALERVGLKEFVESLPGgldtvVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 199 ILFCDEPTSGLDafMASE-VVRALLDLANKGKTIIVVLH 236
Cdd:cd03244 160 ILVLDEATASVD--PETDaLIQKTIREAFKDCTVLTIAH 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
54-266 |
2.14e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 69.29 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVE-YLGDVTVNGKKITK-------QKMRQMCAYVQQVDLFCG 125
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRL----IEpTRGQVLIDGVDIAKisdaelrEVRRKKIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLtdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK10070 120 HMTVLDNTAFG--MELAGINAEERREKALDALRQVGL---ENYAHSYPDELSG---GMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
46-236 |
3.41e-12 |
|
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: 70.04 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 46 AGGGRKEVIRNVSGVaEPGEVLALMGGSGAGKTTLMNILAHlDTNGVEylGDVTVNGKKITKQ--KMRQMCAYVQQVDLF 123
Cdd:TIGR01257 1948 SGTSSPAVDRLCVGV-RPGECFGLLGVNGAGKTTTFKMLTG-DTTVTS--GDATVAGKSILTNisDVHQNMGYCPQFDAI 2023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVREQLTYTAHMRmknATVQQKMERVEN-VLRDMNLTDCQNTLIGIpnrmkgISIGEKKRLAFACEILTDPKILFC 202
Cdd:TIGR01257 2024 DDLLTGREHLYLYARLR---GVPAEEIEKVANwSIQSLGLSLYADRLAGT------YSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190
....*....|....*....|....*....|....
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
45-266 |
3.90e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 66.46 E-value: 3.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKeVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKIT----KQKMRQMCAYVQQV 120
Cdd:PRK10895 11 KAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISllplHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFCGTLTVREQLTYTAHMRmKNATVQQKMERVENVLRDMNLTDCQNTLigipnrMKGISIGEKKRLAFACEILTDPKIL 200
Cdd:PRK10895 87 ASIFRRLSVYDNLMAVLQIR-DDLSAEQREDRANELMEEFHIEHLRDSM------GQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVfrmfhKVC----FMATGKTVYHGAVDRL 266
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-----AVCerayIVSQGHLIAHGTPTEI 224
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
51-266 |
4.68e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 4.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVE-YLGDVTVNGK---------KITKQKMRQMCAYV-QQ 119
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRL----IEiYDSKIKVDGKvlyfgkdifQIDAIKLRKEVGMVfQQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFcGTLTVREQLTYTahmrMKNATVQQKMER---VENVLRDMNL-TDCQNTLIGIPNRMKGisiGEKKRLAFACEILT 195
Cdd:PRK14246 99 PNPF-PHLSIYDNIAYP----LKSHGIKEKREIkkiVEECLRKVGLwKEVYDRLNSPASQLSG---GQQQRLTIARALAL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKgKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQ-VARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
49-236 |
6.32e-12 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 67.42 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEYLGdvtVNGKKITK--QKMRQMCAYVQQVDLFcGT 126
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIR---FHGTDVSRlhARDRKVGFVFQHYALF-RH 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTY-----TAHMRMKNATVQQKMERvenvLRDM-NLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:PRK10851 89 MTVFDNIAFgltvlPRRERPNAAAIKAKVTQ----LLEMvQLAHLADRY---PAQLSG---GQKQRVALARALAVEPQIL 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGK-TIIVVLH 236
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTH 195
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
62-262 |
6.46e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 66.19 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 62 EPGEVLALMGGSGAGKTTLMNILAHLDTNG------VEYLGDVTVNGKKITK--QKMRQMCAYV-QQVDLfCGTLTVREQ 132
Cdd:PRK09984 28 HHGEMVALLGPSGSGKSTLLRHLSGLITGDksagshIELLGRTVQREGRLARdiRKSRANTGYIfQQFNL-VNRLSVLEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 133 -----LTYTAHMR--MKNATVQQKMERVENVLRdmnltdcqntlIGIPN----RMKGISIGEKKRLAFACEILTDPKILF 201
Cdd:PRK09984 107 vligaLGSTPFWRtcFSWFTREQKQRALQALTR-----------VGMVHfahqRVSTLSGGQQQRVAIARALMQQAKVIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGA 262
Cdd:PRK09984 176 ADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQ-VDYALRYCERIVALRQGHVFYDGS 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
55-265 |
7.75e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 7.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 55 RNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HL--DTNGVEY------LGDVTVNGKKITKQKMRQMCAYVQQ--VDLF 123
Cdd:PRK11701 23 RDVSFDLYPGEVLGIVGESGSGKTTLLNALSaRLapDAGEVHYrmrdgqLRDLYALSEAERRRLLRTEWGFVHQhpRDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLT----VREQLTYTA--HMRMKNATVQQKMERVEnvlrdmnltdcqntlIGiPNRM----KGISIGEKKRLAFACEI 193
Cdd:PRK11701 103 RMQVSaggnIGERLMAVGarHYGDIRATAGDWLERVE---------------ID-AARIddlpTTFSGGMQQRLQIARNL 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 194 LTDPKILFCDEPTSGLDAfmaseVVRA-LLDL-----ANKGKTIIVVLHQPSstVFRMF-HKVCFMATGKTVYHGAVDR 265
Cdd:PRK11701 167 VTHPRLVFMDEPTGGLDV-----SVQArLLDLlrglvRELGLAVVIVTHDLA--VARLLaHRLLVMKQGRVVESGLTDQ 238
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
61-266 |
9.20e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 65.37 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 61 AEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGK--KITKQKMRQMCAYVQQVDLFcGTLTVREQLTYTAH 138
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNGQdhTTTPPSRRPVSMLFQENNLF-SHLTVAQNIGLGLN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 139 MRMKnATVQQKmERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVV 218
Cdd:PRK10771 98 PGLK-LNAAQR-EKLHAIARQMGIEDLLARL---PGQLSG---GQRQRVALARCLVREQPILLLDEPFSALDPALRQEML 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 219 RALLDL-ANKGKTIIVVLHQ--------PSSTVfrmfhkvcfMATGKTVYHGAVDRL 266
Cdd:PRK10771 170 TLVSQVcQERQLTLLMVSHSledaariaPRSLV---------VADGRIAWDGPTDEL 217
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
49-236 |
9.37e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.89 E-value: 9.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQ--KMRQMCAYVQQVDLFc 124
Cdd:PRK09452 25 DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIA-----GFETPdsGRIMLDGQDITHVpaENRHVNTVFQSYALF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDPKILFCDE 204
Cdd:PRK09452 99 PHMTVFENVAFG--LRMQKTPAAEITPRVMEALRMVQLEEFAQ------RKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 205 PTSGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKlGITFVFVTH 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
47-266 |
1.13e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 67.42 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKT-TLMNILAHLDTNGVEYL-GDVTVNGKKI---TKQKMR-----QMCAY 116
Cdd:PRK15134 18 QQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPVVYPsGDIRFHGESLlhaSEQTLRgvrgnKIAMI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 VQQVDLFCGTL-TVREQL--TYTAH--MRMKNATVQ--QKMERVenvlrdmNLTDCQNTLIGIPNRMKGisiGEKKRLAF 189
Cdd:PRK15134 98 FQEPMVSLNPLhTLEKQLyeVLSLHrgMRREAARGEilNCLDRV-------GIRQAAKRLTDYPHQLSG---GERQRVMI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 190 ACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSI-VRKLADRVAVMQNGRCVEQNRAATL 244
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
41-256 |
1.34e-11 |
|
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: 64.03 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 41 ATVPQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMN-ILAHLDTNGveylGDVTVNGKkitkqkmrqmCAYVQQ 119
Cdd:cd03250 8 FTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEKLS----GSVSVPGS----------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VD-LFCGtlTVREQLTYTAHMRmknatvqqkMERVENVLR------DM-NLTDCQNTLIGIpnrmKGISI--GEKKRLAF 189
Cdd:cd03250 74 EPwIQNG--TIRENILFGKPFD---------EERYEKVIKacalepDLeILPDGDLTEIGE----KGINLsgGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 190 ACEILTDPKILFCDEPTSGLDAFMASEVV-RALLDLANKGKTIIVVLHQPSstVFRMFHKVCFMATGK 256
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQ--LLPHADQIVVLDNGR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
45-266 |
1.88e-11 |
|
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: 67.02 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKT-TLMNILAHLDTNGVEYLGDVTVNGKKITKQKMRQMC-------AY 116
Cdd:COG4172 17 GQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgnriAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 117 VQQ--------VdlfcgtLTVREQL--TYTAHMRMKNATVQQK----MERVenvlrdmnltdcqntliGIPN---RMKG- 178
Cdd:COG4172 97 IFQepmtslnpL------HTIGKQIaeVLRLHRGLSGAAARARalelLERV-----------------GIPDperRLDAy 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 179 ---ISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMAT 254
Cdd:COG4172 154 phqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHD-LGVVRRFADRVAVMRQ 232
|
250
....*....|..
gi 808355238 255 GKTVYHGAVDRL 266
Cdd:COG4172 233 GEIVEQGPTAEL 244
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
46-258 |
2.80e-11 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 64.32 E-value: 2.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 46 AGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKMRQMCAYVQQVDL-FC 124
Cdd:PRK10419 20 GKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLES---PSQGNVSWRGEPLAKLNRAQRKAFRRDIQMvFQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTL-------TVREQLTYTA-HMRMKNATVQQkmERVENVLRDMNLTDcqNTLIGIPNRMKGisiGEKKRLAFACEILTD 196
Cdd:PRK10419 97 DSIsavnprkTVREIIREPLrHLLSLDKAERL--ARASEMLRAVDLDD--SVLDKRPPQLSG---GQLQRVCLARALAVE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTV 258
Cdd:PRK10419 170 PKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
53-268 |
3.09e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 3.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-----HLDTNGVEYLGDVTVNGK---KITKQKMRQMCAYVQQVDLFC 124
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgGGAPRGARVTGDVTLNGEplaAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVRE--QLTYTAHMRMKNATVQqkmervenvlRDMNLTDCQNTLIG----IPNRMKGISIGEKKRLAFA-------- 190
Cdd:PRK13547 96 FAFSAREivLLGRYPHARRAGALTH----------RDGEIAWQALALAGatalVGRDVTTLSGGELARVQFArvlaqlwp 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 191 -CEILTDPKILFCDEPTSGLDafMAS-----EVVRALLDLANKGKTIIVvlHQPSSTVfRMFHKVCFMATGKTVYHGAV- 263
Cdd:PRK13547 166 pHDAAQPPRYLLLDEPTAALD--LAHqhrllDTVRRLARDWNLGVLAIV--HDPNLAA-RHADRIAMLADGAIVAHGAPa 240
|
....*
gi 808355238 264 DRLCP 268
Cdd:PRK13547 241 DVLTP 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
53-261 |
4.31e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 4.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTL---MNILAHLDTNGVEYL---------------GDVTVNGKKITKQKMRQMC 114
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFiehLNALLLPDTGTIEWIfkdeknkkktkekekVLEKLVIQKTRFKKIKKIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 115 AYVQQV---------DLFcgTLTVREQLTYTAhMRMkNATVQQKMERVENVLRdmnltdcqntLIGIP-NRMK----GIS 180
Cdd:PRK13651 102 EIRRRVgvvfqfaeyQLF--EQTIEKDIIFGP-VSM-GVSKEEAKKRAAKYIE----------LVGLDeSYLQrspfELS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 181 IGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYH 260
Cdd:PRK13651 168 GGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDN-VLEWTKRTIFFKDGKIIKD 246
|
.
gi 808355238 261 G 261
Cdd:PRK13651 247 G 247
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
49-240 |
7.69e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 64.65 E-value: 7.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKIT----KQKMRQMCAYV----Q 118
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALF-----GADPAdsGEIRLDGKPVRirspRDAIRAGIAYVpedrK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 119 QVDLFcGTLTVREQLTYTAHMRMKNA-TVQQKMER--VENVLRDMNL-TDCQNTLIGipnrmkGISIGEKKRLAFACEIL 194
Cdd:COG1129 338 GEGLV-LDLSIRENITLASLDRLSRGgLLDRRRERalAEEYIKRLRIkTPSPEQPVG------NLSGGNQQKVVLAKWLA 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVlhqpSS 240
Cdd:COG1129 411 TDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVI----SS 452
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
56-236 |
7.93e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.11 E-value: 7.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGVEYL--GDVTVNGKKITKQ---KMRQMCAYV-QQVD-LFCGTlT 128
Cdd:PRK13635 25 DVSFSVYEGEWVAIVGHNGSGKSTLAKLL-----NGLLLPeaGTITVGGMVLSEEtvwDVRRQVGMVfQNPDnQFVGA-T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLTYTahmrMKNATV--QQKMERVENVLRDMNLTDcqnTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:PRK13635 99 VQDDVAFG----LENIGVprEEMVERVDQALRQVGMED---FLNREPHRLSG---GQKQRVAIAGVLALQPDIIILDEAT 168
|
170 180 190
....*....|....*....|....*....|.
gi 808355238 207 SGLDAFMASEVVRALLDL-ANKGKTIIVVLH 236
Cdd:PRK13635 169 SMLDPRGRREVLETVRQLkEQKGITVLSITH 199
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
56-211 |
1.18e-10 |
|
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: 63.58 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQKMRQM-------CAYV-QQVDLFcG 125
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIA-----GLERPdsGRIRLGGEVLQDSARGIFlpphrrrIGYVfQEARLF-P 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTahmrMKNATVQQKMERVENVLRdmnltdcqntLIGI-------PNRMKGisiGEKKRLAFACEILTDPK 198
Cdd:COG4148 91 HLSVRGNLLYG----RKRAPRAERRISFDEVVE----------LLGIghlldrrPATLSG---GERQRVAIGRALLSSPR 153
|
170
....*....|...
gi 808355238 199 ILFCDEPTSGLDA 211
Cdd:COG4148 154 LLLMDEPLAALDL 166
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
65-237 |
1.50e-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: 64.65 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 65 EVLALMGGSGAGKTTLMNILAHL--DTNGVeylgdVTVNGKKITKQ--KMRQMCAYVQQVDLFCGTLTVREQLTYTAhmR 140
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLlpPTSGT-----VLVGGKDIETNldAVRQSLGMCPQHNILFHHLTVAEHILFYA--Q 1029
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 141 MKNATVQQKMERVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMAsevvRA 220
Cdd:TIGR01257 1030 LKGRSWEEAQLEMEAMLEDTGLHHKRN------EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RS 1099
|
170 180
....*....|....*....|
gi 808355238 221 LLDLANK---GKTIIVVLHQ 237
Cdd:TIGR01257 1100 IWDLLLKyrsGRTIIMSTHH 1119
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
57-210 |
1.50e-10 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 61.93 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 57 VSGVA---EPGEVLALMGGSGAGKTTLMNILA--HLDTNgveylGDVTVNGKKI---TKQKMRQM--CAYVQQVDLFcGT 126
Cdd:PRK11300 21 VNNVNlevREQEIVSLIGPNGAGKTTVFNCLTgfYKPTG-----GTILLRGQHIeglPGHQIARMgvVRTFQHVRLF-RE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMRMKNATV-------------QQKMERVENVLRDMNLTDCQntligipNRMKG-ISIGEKKRLAFACE 192
Cdd:PRK11300 95 MTVIENLLVAQHQQLKTGLFsgllktpafrraeSEALDRAATWLERVGLLEHA-------NRQAGnLAYGQQRRLEIARC 167
|
170
....*....|....*...
gi 808355238 193 ILTDPKILFCDEPTSGLD 210
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLN 185
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
62-210 |
2.08e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.02 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 62 EPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLTVREQLTYTAHMRM 141
Cdd:PRK13543 35 DAGEALLVQGDNGAGKTTLLRVLAGLLHVES---GQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 142 KNAtvqQKMErvENVLRDMNLTDCQNTLIgipnrmKGISIGEKKRLAFACEILTDPKILFCDEPTSGLD 210
Cdd:PRK13543 112 RRA---KQMP--GSALAIVGLAGYEDTLV------RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
178-261 |
2.75e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 62.18 E-value: 2.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 178 GISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKT 257
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHT-MEHVLEVADEVIVMDKGKI 254
|
....
gi 808355238 258 VYHG 261
Cdd:PRK13631 255 LKTG 258
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
45-263 |
4.11e-10 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtNGVEY--LGDVTVNGKKITKQKMRQMCAYVQQVdl 122
Cdd:PRK11153 12 PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCI-----NLLERptSGRVLVDGQDLTALSEKELRKARRQI-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 fcGTL----------TVREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACE 192
Cdd:PRK11153 85 --GMIfqhfnllssrTVFDNVALP--LELAGTPKAEIKARVTELLELVGLSDKADRY---PAQLSG---GQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 193 ILTDPKILFCDEPTSGLDafmaSEVVRALLDLANK-----GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAV 263
Cdd:PRK11153 155 LASNPKVLLCDEATSALD----PATTRSILELLKDinrelGLTIVLITHE-MDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
51-243 |
5.39e-10 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 5.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEY-LGDVTVNGKKITKQKMRQmcAYVQQVDlfcGTLTV 129
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGF----VPYqHGSITLDGKPVEGPGAER--GVVFQNE---GLLPW 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 REQLTYTAhMRMKNATVqQKMERVENVLRDMNLTDcqntLIGIPNR-MKGISIGEKKRLAFACEILTDPKILFCDEPTSG 208
Cdd:PRK11248 85 RNVQDNVA-FGLQLAGV-EKMQRLEIAHQMLKKVG----LEGAEKRyIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 209 LDAFMASEVVRALLDL-ANKGKTIIVVLHQPSSTVF 243
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVF 194
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
54-287 |
7.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 7.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKM----RQMCAYVQQVD-LFCGTlT 128
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFE---EFEGKVKIDGELLTAENVwnlrRKIGMVFQNPDnQFVGA-T 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLTYTahMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSG 208
Cdd:PRK13642 99 VEDDVAFG--MENQGIPREEMIKRVDEALLAVNMLDFKTRE---PARLSG---GQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 209 LDAFMASEVVRALLDLANKGK-TIIVVLHQPSSTVFRmfHKVCFMATGKTVYHGAVDRL-------------CPFFDKLG 274
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAASS--DRILVMKAGEIIKEAAPSELfatsedmveigldVPFSSNLM 248
|
250
....*....|....*...
gi 808355238 275 PDFR-----VPESYNPAD 287
Cdd:PRK13642 249 KDLRkngfdLPEKYLSED 266
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
51-261 |
8.76e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 60.06 E-value: 8.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNilaHLD-----TNGVEYLGDVTVNGKKITKQKMRQMCAYVQQV---DL 122
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQ---HLNgllkpTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYpeyQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FcgTLTVREQLTYTAhmrmKNATVQQkmERVEN-VLRDMNLtdcqntlIGIP-NRMKG-----ISIGEKKRLAFACEILT 195
Cdd:PRK13637 97 F--EETIEKDIAFGP----INLGLSE--EEIENrVKRAMNI-------VGLDyEDYKDkspfeLSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKGK-TIIVVLHQpSSTVFRMFHKVCFMATGKTVYHG 261
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHS-MEDVAKLADRIIVMNKGKCELQG 227
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
60-236 |
9.20e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 61.72 E-value: 9.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 60 VAEPGEVLALMGGSGAGKTTLMNILA------------HLDTNGV----------EYLGDVtVNGKKITKQKmrqmcayV 117
Cdd:COG1245 95 VPKKGKVTGILGPNGIGKSTALKILSgelkpnlgdydeEPSWDEVlkrfrgtelqDYFKKL-ANGEIKVAHK-------P 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 118 QQVDL----FCGTltVREQLTyTAHMRMKNATVQQKMErVENVL-RDMNltdcqnTLIGipnrmkgisiGEKKRLAFACE 192
Cdd:COG1245 167 QYVDLipkvFKGT--VRELLE-KVDERGKLDELAEKLG-LENILdRDIS------ELSG----------GELQRVAIAAA 226
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 808355238 193 ILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:COG1245 227 LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEH 270
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
51-236 |
9.97e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 9.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVTVNGKkiTKQK----MRQMCAYVQQV---D 121
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALlkPTTGTVTVDDITITHK--TKDKyirpVRKRIGMVFQFpesQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTLTvREQLTYTAHMRMKnatVQQKMERVENVLrdMNLTDCQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILF 201
Cdd:PRK13646 98 LFEDTVE-REIIFGPKNFKMN---LDEVKNYAHRLL--MDLGFSRDVMSQSPFQMSG---GQMRKIAIVSILAMNPDIIV 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLH 236
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSH 204
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
45-264 |
1.27e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILA-HLDTNGVEylGDVTVNGKKITKQKMRQMcayvQQVDLF 123
Cdd:CHL00131 14 HASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAgHPAYKILE--GDILFKGESILDLEPEER----AHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 CGTLTVRE----------QLTYTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLIGiPNRMKGISIGEKKRLAFACEI 193
Cdd:CHL00131 88 LAFQYPIEipgvsnadflRLAYNSKRKFQGLPELDPLEFLEIINEKLKLVGMDPSFLS-RNVNEGFSGGEKKRNEILQMA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 194 LTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVD 264
Cdd:CHL00131 167 LLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKPDYVHVMQNGKIIKTGDAE 237
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
47-266 |
1.71e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 59.34 E-value: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKITKQK-----MRQMCAYVQQ 119
Cdd:PRK14271 30 GFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkVSGYRYSGDVLLGGRSIFNYRdvlefRRRVGMLFQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDLFcgTLTVREQLTytAHMRMKNATVQQKMERVENV-LRDMNLTDC-QNTLIGIPNRMKGisiGEKKRLAFACEILTDP 197
Cdd:PRK14271 110 PNPF--PMSIMDNVL--AGVRAHKLVPRKEFRGVAQArLTEVGLWDAvKDRLSDSPFRLSG---GQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 198 KILFCDEPTSGLDAFMASEVVRALLDLANKgKTIIVVLHQPSSTVfRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAA-RISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
54-263 |
1.80e-09 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.57 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNIL--AHLDTNGVeylgdVTVNGK---KITKQKMRQMCAYV--QQVDLFcGT 126
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLsgIHEPTKGT-----ITINNInynKLDHKLAAQLGIGIiyQELSVI-DE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMRMK----NATVQQKM-ERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILF 201
Cdd:PRK09700 95 LTVLENLYIGRHLTKKvcgvNIIDWREMrVRAAMMLLRVGLKVDLDEKVA------NLSISHKQMLEIAKTLMLDAKVII 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 202 CDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAV 263
Cdd:PRK09700 169 MDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAE-IRRICDRYTVMKDGSSVCSGMV 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
63-236 |
2.79e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 58.26 E-value: 2.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PGEVLALMGGSGAGKTTLMNILA-HLDTNGveylGDVTVNGKKI----TKQKMRQMCAYVQQVDLFCGtLTVREQLT--- 134
Cdd:PRK10575 36 AGKVTGLIGHNGSGKSTLLKMLGrHQPPSE----GEILLDAQPLeswsSKAFARKVAYLPQQLPAAEG-MTVRELVAigr 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 135 YTAHMRMKNATVQQKmERVENVLRDMNLTDCQNTLIgipnrmKGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMA 214
Cdd:PRK10575 111 YPWHGALGRFGAADR-EKVEEAISLVGLKPLAHRLV------DSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183
|
170 180
....*....|....*....|...
gi 808355238 215 SEVVRALLDLAN-KGKTIIVVLH 236
Cdd:PRK10575 184 VDVLALVHRLSQeRGLTVIAVLH 206
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
47-236 |
4.60e-09 |
|
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: 57.06 E-value: 4.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLM------------NILAHLDTNGVeylgDVTvngkKITKQKM---- 110
Cdd:COG4778 20 GGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygnylpdsgSILVRHDGGWV----DLA----QASPREIlalr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 111 RQMCAYVQQ----------VDLfcgtltVREQLtytahmRMKNATVQQKMERVENVLRDMNltdcqntligIPNRMKGI- 179
Cdd:COG4778 92 RRTIGYVSQflrviprvsaLDV------VAEPL------LERGVDREEARARARELLARLN----------LPERLWDLp 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 180 ----SIGEKKRLAFACEILTDPKILFCDEPTSGLDAfMASEVVRALL-DLANKGKTIIVVLH 236
Cdd:COG4778 150 patfSGGEQQRVNIARGFIADPPLLLLDEPTASLDA-ANRAVVVELIeEAKARGTAIIGIFH 210
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
51-236 |
6.44e-09 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 54.76 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGK-KItkqkmrqmcAYVQQvdlfcgtltv 129
Cdd:cd03221 13 KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELE---PDEGIVTWGSTvKI---------GYFEQ---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 reqltytahmrmknatvqqkmervenvlrdmnltdcqntLIGipnrmkgisiGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:cd03221 71 ---------------------------------------LSG----------GEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180
....*....|....*....|....*...
gi 808355238 210 DAFMasevVRALLD-LANKGKTIIVVLH 236
Cdd:cd03221 102 DLES----IEALEEaLKEYPGTVILVSH 125
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
48-266 |
7.89e-09 |
|
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: 58.54 E-value: 7.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVA---EPGEVLALMGGSGAGKTTL-MNILAHLDTNGveylgDVTVNGKKITK---QKMRQMCAYVQQV 120
Cdd:COG4172 293 RRTVGHVKAVDGVSltlRRGETLGLVGESGSGKSTLgLALLRLIPSEG-----EIRFDGQDLDGlsrRALRPLRRRMQVV 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 --DLFcGTL--------TVREQLTytAHMRMKNAtvQQKMERVENVLRDMNLTDcqNTLIGIPNRMKGisiGEKKRLAFA 190
Cdd:COG4172 368 fqDPF-GSLsprmtvgqIIAEGLR--VHGPGLSA--AERRARVAEALEEVGLDP--AARHRYPHEFSG---GQRQRIAIA 437
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 191 CEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSstVFR-MFHKVCFMATGKTVYHGAVDRL 266
Cdd:COG4172 438 RALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLA--VVRaLAHRVMVMKDGKVVEQGPTEQV 513
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-261 |
9.10e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.33 E-value: 9.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 38 GLVATVPQAGGGRKEVIRNVSGVAE------PGEVLALMGGSGAGKTTLMNILAHL-DTNGveylGDVTVNGKKITK--- 107
Cdd:PRK10261 318 NLVTRFPLRSGLLNRVTREVHAVEKvsfdlwPGETLSLVGESGSGKSTTGRALLRLvESQG----GEIIFNGQRIDTlsp 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 108 ---QKMRQMCAYVQQvDLFcGTLTVREQLTYT------AHMRMKNATVQQK----MERV----ENVLRdmnltdcqntli 170
Cdd:PRK10261 394 gklQALRRDIQFIFQ-DPY-ASLDPRQTVGDSimeplrVHGLLPGKAAAARvawlLERVgllpEHAWR------------ 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 171 gIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVC 250
Cdd:PRK10261 460 -YPHEFSG---GQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVA 535
|
250
....*....|.
gi 808355238 251 FMATGKTVYHG 261
Cdd:PRK10261 536 VMYLGQIVEIG 546
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
53-237 |
1.35e-08 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 56.40 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEYLGDVTVNG---KKITKQKMRQMCAYV-QQVDLFCGTLT 128
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL----LNTEGDIQIDGvswNSVPLQKWRKAFGVIpQKVFIFSGTFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VR---------EQLTYTAHMRMKNATVQQKMERVENVLRDMNLTdcqntligipnrmkgISIGEKKRLAFACEILTDPKI 199
Cdd:cd03289 95 KNldpygkwsdEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCV---------------LSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 808355238 200 LFCDEPTSGLDAfMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:cd03289 160 LLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHR 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
54-240 |
1.49e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 56.43 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEYL--GDVTVNGKKITKQKMRQMCAYVQQVDLFCGTLTVRE 131
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALM-----GFVRLasGKISILGQPTRQALQKNLVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 132 Q----LTYTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:PRK15056 98 EdvvmMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIG------ELSGGQKKRVFLARAIAQQGQVILLDEPFT 171
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 208 GLDAFMASEVVRALLDLANKGKTIIVVLHQPSS 240
Cdd:PRK15056 172 GVDVKTEARIISLLRELRDEGKTMLVSTHNLGS 204
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
56-258 |
1.59e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGvEYLGDVTVNGKKITKQKMR-----------QMCAYVQQvdlfc 124
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG-TYEGEIIFEGEELQASNIRdteragiaiihQELALVKE----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 gtLTVREQL----TYTAHMRMKNATVQQkmeRVENVLRDMNLTdcqntlIGIPNRMKGISIGEKKRLAFACEILTDPKIL 200
Cdd:PRK13549 97 --LSVLENIflgnEITPGGIMDYDAMYL---RAQKLLAQLKLD------INPATPVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 201 FCDEPTSGLdafMASEvVRALL----DLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTV 258
Cdd:PRK13549 166 ILDEPTASL---TESE-TAVLLdiirDLKAHGIACIYISHKLNE-VKAISDTICVIRDGRHI 222
|
|
| ABC2_membrane_7 |
pfam19055 |
ABC-2 type transporter; |
236-290 |
1.62e-08 |
|
ABC-2 type transporter;
Pssm-ID: 465963 [Multi-domain] Cd Length: 409 Bit Score: 57.22 E-value: 1.62e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 236 HQPSSTVFRMFHKVCFMAT-GKTVYHGAVDRLCPFFDKLGpdFRVPESYNPADFVM 290
Cdd:pfam19055 1 HQPSYTLFKMFDDLILLAKgGLTVYHGPVKKVEEYFAGLG--INVPERVNPPDHFI 54
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
56-236 |
1.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 56.38 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNilaHLDTNGVEYLGDVTVNGKKITKQ-------KMRQMCAYVQQ---VDLFcg 125
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQ---HFNALLKPSSGTITIAGYHITPEtgnknlkKLRKKVSLVFQfpeAQLF-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAhmrmKN--ATVQQKMERVENVLRDMNLTDcqNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCD 203
Cdd:PRK13641 100 ENTVLKDVEFGP----KNfgFSEDEAKEKALKWLKKVGLSE--DLISKSPFELSG---GQMRRVAIAGVMAYEPEILCLD 170
|
170 180 190
....*....|....*....|....*....|...
gi 808355238 204 EPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
43-236 |
1.74e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 55.27 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 43 VPQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGVEY--LGDVTVNGKKITKQKMRQMCAYVQQV 120
Cdd:PRK10908 7 VSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIC-----GIERpsAGKIWFSGHDITRLKNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DL-FCGTLTVREQLTY---TAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTD 196
Cdd:PRK10908 82 GMiFQDHHLLMDRTVYdnvAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNF---PIQLSG---GEQQRVGIARAVVNK 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATH 195
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
50-236 |
1.94e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 55.96 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVAEPGEVLALMGGSGAGKTT---LMN--ILAHLDTNGVeylgdVTVNGKKITKQKM---RQMCAYVQQV- 120
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTiskLINglLLPDDNPNSK-----ITVDGITLTAKTVwdiREKVGIVFQNp 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 -DLFCGTlTVREQLTYTAHMRmknATVQQKMER-VENVLRDMNLTDCQNTLigiPNRMKGisiGEKKRLAFACEILTDPK 198
Cdd:PRK13640 94 dNQFVGA-TVGDDVAFGLENR---AVPRPEMIKiVRDVLADVGMLDYIDSE---PANLSG---GQKQRVAIAGILAVEPK 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 199 ILFCDEPTSGLDAFMASEVVRALLDLAN-KGKTIIVVLH 236
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITH 202
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
65-334 |
1.96e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 56.17 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 65 EVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGD--VTVNGKKITKQK-MRQMCAYVQQV---DLFcgTLTVREQLTY- 135
Cdd:PRK13645 38 KVTCVIGTTGSGKSTMIQLTNGLiiSETGQTIVGDyaIPANLKKIKEVKrLRKEIGLVFQFpeyQLF--QETIEKDIAFg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 136 TAHMrmkNATVQQKMERVENVLRDMNLTdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGLDAFMAS 215
Cdd:PRK13645 116 PVNL---GENKQEAYKKVPELLKLVQLP--EDYVKRSPFELSG---GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 216 EVVRALLDL-ANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAvdrlcPFfdklgpdfrvpESYNPADfVMSEIS 294
Cdd:PRK13645 188 DFINLFERLnKEYKKRIIMVTHN-MDQVLRIADEVIVMHEGKVISIGS-----PF-----------EIFSNQE-LLTKIE 249
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 808355238 295 ISPeteqedvTRIEYLIHEYQNSdiGTQMLKKTRTAVDEF 334
Cdd:PRK13645 250 IDP-------PKLYQLMYKLKNK--GIDLLNKNIRTIEEF 280
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
64-237 |
2.43e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNI----LAHLDTNGVEYLGDVtvngkkitkqkmrqmcAYVQQVDLFCGTlTVREQLTYTA-- 137
Cdd:PLN03232 643 GSLVAIVGGTGEGKTSLISAmlgeLSHAETSSVVIRGSV----------------AYVPQVSWIFNA-TVRENILFGSdf 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 138 ----HMRMKNATVQQkmervenvlRDMNLTDCQNtLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFM 213
Cdd:PLN03232 706 eserYWRAIDVTALQ---------HDLDLLPGRD-LTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHV 775
|
170 180
....*....|....*....|....
gi 808355238 214 ASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVTNQ 799
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
51-261 |
2.65e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 55.38 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngveyL----GDVTVNGKKITKQKMRQMCAYV----QQVD- 121
Cdd:PRK13632 22 NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGL-------LkpqsGEIKIDGITISKENLKEIRKKIgiifQNPDn 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGtLTVREQLTYTAHMRMKNatvQQKMER-VENVLRDMNLTDcqnTLIGIPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:PRK13632 95 QFIG-ATVEDDIAFGLENKKVP---PKKMKDiIDDLAKKVGMED---YLDKEPQNLSG---GQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKG-KTIIVVLHQPSSTVfrMFHKVCFMATGKTVYHG 261
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAI--LADKVIVFSEGKLIAQG 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
48-238 |
3.52e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 54.04 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKeVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtnGVEYLGDVTVNGKKITKQkmRQmcAYVQQVdLFCG-- 125
Cdd:PRK13538 12 DERI-LFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGL---ARPDAGEVLWQGEPIRRQ--RD--EYHQDL-LYLGhq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 -----TLTVREQLTYTAHMRMknatvQQKMERVENVLRDMNLTDCQNTLIGIpnrmkgISIGEKKRLAFACEILTDPKIL 200
Cdd:PRK13538 83 pgiktELTALENLRFYQRLHG-----PGDDEALWEALAQVGLAGFEDVPVRQ------LSAGQQRRVALARLWLTRAPLW 151
|
170 180 190
....*....|....*....|....*....|....*...
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQP 238
Cdd:PRK13538 152 ILDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTHQD 189
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
49-236 |
3.83e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.00 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQKMR---QMCAYVQQVDLFCG 125
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALSARaasRRVASVPQDTSLSF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVRE--QLTYTAHM-RMKNAT------VQQKMERVE-NVLRDMNLTDcqntligipnrmkgISIGEKKRLAFACEILT 195
Cdd:PRK09536 91 EFDVRQvvEMGRTPHRsRFDTWTetdraaVERAMERTGvAQFADRPVTS--------------LSGGERQRVLLARALAQ 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 808355238 196 DPKILFCDEPTSGLD---AFMASEVVRallDLANKGKTIIVVLH 236
Cdd:PRK09536 157 ATPVLLLDEPTASLDinhQVRTLELVR---RLVDDGKTAVAAIH 197
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
45-210 |
4.54e-08 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 54.33 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 45 QAGGgrKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITK---QKMRQMCAYVQQVD 121
Cdd:PRK10247 16 LAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTS---GTLLFEGEDISTlkpEIYRQQVSYCAQTP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTlTVREQLTYTAHMRMKnatvQQKMERVENVLRDMNLTDcqNTLigiPNRMKGISIGEKKRLAFACEILTDPKILF 201
Cdd:PRK10247 91 TLFGD-TVYDNLIFPWQIRNQ----QPDPAIFLDDLERFALPD--TIL---TKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
....*....
gi 808355238 202 CDEPTSGLD 210
Cdd:PRK10247 161 LDEITSALD 169
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
51-294 |
4.57e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.66 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDtngvEYLGDVTVNGK-----------KITKQKMRQMCAYVQ- 118
Cdd:PRK14258 20 QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMN----ELESEVRVEGRveffnqniyerRVNLNRLRRQVSMVHp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 119 QVDLFcgTLTVREQLTYTahmrMKNATVQQKMER---VENVLRDMNLTDcqntliGIPNRMKG----ISIGEKKRLAFAC 191
Cdd:PRK14258 96 KPNLF--PMSVYDNVAYG----VKIVGWRPKLEIddiVESALKDADLWD------EIKHKIHKsaldLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 192 EILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGK-TIIVVLHQpsstvfrmFHKVCFMATGKTVYHGAVDRLCPF- 269
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN--------LHQVSRLSDFTAFFKGNENRIGQLv 235
|
250 260
....*....|....*....|....*.
gi 808355238 270 -FDKLGPDFRVPESYNPADFVMSEIS 294
Cdd:PRK14258 236 eFGLTKKIFNSPHDSRTREYVLSRLG 261
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
50-234 |
4.85e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 55.95 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEViRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK----MRQMCAYV---QQVDL 122
Cdd:PRK09700 276 RKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAG---GEIRLNGKDISPRSpldaVKKGMAYItesRRDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTYTAHM---RMKNA--TVQQKMER--VENVLRDMNLTdCQNtligIPNRMKGISIGEKKRLAFACEILT 195
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLkdgGYKGAmgLFHEVDEQrtAENQRELLALK-CHS----VNQNITELSGGNQQKVLISKWLCC 426
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMV 465
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
54-234 |
5.86e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.78 E-value: 5.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNIL--AHLDTNGveylgDVTVNGKKIT----KQKMRQMCAYVQQvD-----L 122
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLygALPRTSG-----YVTLDGHEVVtrspQDGLANGIVYISE-DrkrdgL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGtLTVREQLTYTA--HMRMKNATVQQKMER--VENVLRDMNltdcqntlIGIPNRMKGI---SIGEKKRLAFACEILT 195
Cdd:PRK10762 342 VLG-MSVKENMSLTAlrYFSRAGGSLKHADEQqaVSDFIRLFN--------IKTPSMEQAIgllSGGNQQKVAIARGLMT 412
|
170 180 190
....*....|....*....|....*....|....*....
gi 808355238 196 DPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILV 451
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
56-262 |
7.46e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.75 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKT-TLMNILAHLDTNGVEYLGDVTVNGKKITK--QKMRQMCAYVQQVDLFCGTLTVREQ 132
Cdd:PRK11022 25 RISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMAEKLEFNGQDLQRisEKERRNLVGAEVAMIFQDPMTSLNP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 133 LTYTAHMRMKNATVQQKMERVENVLRDMNLTdcqnTLIGIPN---RMK----GISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK11022 105 CYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL----NQVGIPDpasRLDvyphQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGA 262
Cdd:PRK11022 181 TTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
49-227 |
8.44e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 53.58 E-value: 8.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtngveyLGDVTVNGKKITKQ-KMRqmCAYVQQVDLFCGTL 127
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVV----------LGLVAPDEGVIKRNgKLR--IGYVPQKLYLDTTL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 TvreqLTYTAHMRM----KNATVQQKMERVEnvlrdmnltdcQNTLIGIPnrMKGISIGEKKRLAFACEILTDPKILFCD 203
Cdd:PRK09544 83 P----LTVNRFLRLrpgtKKEDILPALKRVQ-----------AGHLIDAP--MQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180
....*....|....*....|....
gi 808355238 204 EPTSGLDafMASEVvrALLDLANK 227
Cdd:PRK09544 146 EPTQGVD--VNGQV--ALYDLIDQ 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
50-234 |
8.57e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.94 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGV---EYLGDVTVNGKKIT----KQKMRQMCAYVQQ--- 119
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLF-----GAypgRWEGEIFIDGKPVKirnpQQAIAQGIAMVPEdrk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 -----VDLFCG---TLTVREQltYTAHMRMKNA----TVQQKMERVEnvlrdmnltdcqntlIGIPNRMKGI---SIGEK 184
Cdd:PRK13549 349 rdgivPVMGVGkniTLAALDR--FTGGSRIDDAaelkTILESIQRLK---------------VKTASPELAIarlSGGNQ 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 808355238 185 KRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:PRK13549 412 QKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
56-236 |
8.87e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 53.98 E-value: 8.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGKKITKQK----MRQMCAYVQQVDLFCGTLTVRE 131
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQ---GSVRVDDTLITSTSknkdIKQIRKKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 132 QLTYTAHMRMKNATVQQkmERVENVLRDmnltdcQNTLIGIPNRMKG-----ISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQ--EEAEALARE------KLALVGISESLFEknpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190
....*....|....*....|....*....|
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
55-236 |
9.87e-08 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 54.65 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 55 RNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKITKqkmRQMCAYVQQVDLFcGTLTVREQ 132
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEdiTSGDLFIGEKRMNDVPPAE---RGVGMVFQSYALY-PHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 133 LTYTAHM-RMKNATVQQKMERVENVLRDMNLTDcqntligipNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLDA 211
Cdd:PRK11000 96 MSFGLKLaGAKKEEINQRVNQVAEVLQLAHLLD---------RKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDA 166
|
170 180
....*....|....*....|....*....
gi 808355238 212 F----MASEVVRALLDLankGKTIIVVLH 236
Cdd:PRK11000 167 AlrvqMRIEISRLHKRL---GRTMIYVTH 192
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
63-209 |
1.20e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.62 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PGEVLALMGGSGAGKTTLMNILA---HLDTNGVEYLG-DVTVNGKKITKQkmrqmcAYV----QQVDLFcGTLTVREQLT 134
Cdd:PRK10762 29 PGRVMALVGENGAGKSTMMKVLTgiyTRDAGSILYLGkEVTFNGPKSSQE------AGIgiihQELNLI-PQLTIAENIF 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 808355238 135 YTAHMRMKNATVQ-QKM-ERVENVLRDMNLTDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK10762 102 LGREFVNRFGRIDwKKMyAEADKLLARLNLRFSSDKLVG------ELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
54-237 |
1.83e-07 |
|
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: 54.06 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGvEYLGDVTVNGKKITKQKMRQM----CAYVQQVDLFCGTLTV 129
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLKASNIRDTeragIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 RE------QLTYTAHMRMKNATVQqkmeRVENVLRDMNLTDCQNTLigipnRMKGISIGEKKRLAFACEILTDPKILFCD 203
Cdd:TIGR02633 96 AEniflgnEITLPGGRMAYNAMYL----RAKNLLRELQLDADNVTR-----PVGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190
....*....|....*....|....*....|....
gi 808355238 204 EPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHK 200
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
51-242 |
1.84e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 51 KEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtngVEYL----GDVTVNGKKI---TKQKMRQMCAYVQQ---- 119
Cdd:PRK10790 354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLL-------MGYYplteGEIRLDGRPLsslSHSVLRQGVAMVQQdpvv 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 -VDLFCGTLTVREQLTytahmrmkNATVQQKMERVE--NVLRDMnlTDCQNTLIGipNRMKGISIGEKKRLAFACEILTD 196
Cdd:PRK10790 427 lADTFLANVTLGRDIS--------EEQVWQALETVQlaELARSL--PDGLYTPLG--EQGNNLSVGQKQLLALARVLVQT 494
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRAlLDLANKGKTIIVVLHQPSSTV 242
Cdd:PRK10790 495 PQILILDEATANIDSGTEQAIQQA-LAAVREHTTLVVIAHRLSTIV 539
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
56-244 |
1.86e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILahldtnGVEYL---GDVTVNGKKI----TKQKMRQMCAYVQQVDLFCGTLT 128
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKIL------SGNYQpdaGSILIDGQEMrfasTTAALAAGVAIIYQELHLVPEMT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLtYTAHMRMKNATVQQK--MERVENVLRDMNLTDCQNTligipnRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:PRK11288 96 VAENL-YLGQLPHKGGIVNRRllNYEAREQLEHLGVDIDPDT------PLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLHQ--------PSSTVFR 244
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRmeeifalcDAITVFK 214
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
48-261 |
2.26e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 52.78 E-value: 2.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTL---MNILAhLDTNGVEYLGDV-TVNGKKItkQKMRQMCAYV-QQVDL 122
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIakhMNALL-IPSEGKVYVDGLdTSDEENL--WDIRNKAGMVfQNPDN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTYTAhmrmKNATVQQK--MERVENVLRDMNLTDCQNTligIPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:PRK13633 97 QIVATIVEEDVAFGP----ENLGIPPEeiRERVDESLKKVGMYEYRRH---APHLLSG---GQKQRVAIAGILAMRPECI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANK-GKTIIVVLHQPSSTVfrMFHKVCFMATGKTVYHG 261
Cdd:PRK13633 167 IFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAV--EADRIIVMDSGKVVMEG 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
56-236 |
2.34e-07 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngveyL----GDVTVNGKKITKQKM--RQMCAYVQQV-DLFcGTLT 128
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGL-------LpaseGEAWLFGQPVDAGDIatRRRVGYMSQAfSLY-GELT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 VREQLTYTAHM-RMKNATVQqkmERVENVLRDMNLTDCQNTLigiPNRMkgiSIGEKKRLAFACEILTDPKILFCDEPTS 207
Cdd:NF033858 356 VRQNLELHARLfHLPAAEIA---ARVAEMLERFDLADVADAL---PDSL---PLGIRQRLSLAVAVIHKPELLILDEPTS 426
|
170 180 190
....*....|....*....|....*....|....*
gi 808355238 208 GLD-----AFMasevvRALLDLA-NKGKTIIVVLH 236
Cdd:NF033858 427 GVDpvardMFW-----RLLIELSrEDGVTIFISTH 456
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
49-266 |
2.82e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.56 E-value: 2.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEYLGDVTVNGKKITKQKMRQMCAYVQQVDL------ 122
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRL----INSQGEIWFDGQPLHNLNRRQLLPVRHRIQVvfqdpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 --FCGTLTVREQLTYTAHMRMKNATVQQKMERVENVLRDMNLTdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKIL 200
Cdd:PRK15134 373 ssLNPRLNVLQIIEEGLRVHQPTLSAAQREQQVIAVMEEVGLD--PETRHRYPAEFSG---GQRQRIAIARALILKPSLI 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
42-237 |
3.08e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 53.76 E-value: 3.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 42 TVPQAGGGRKeVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGveylGDVTVNG---KKITKQKMRQMCAYV- 117
Cdd:TIGR01271 1224 TAKYTEAGRA-VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE----GEIQIDGvswNSVTLQTWRKAFGVIp 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 118 QQVDLFCGTLTVR---------EQLTYTAHMRMKNATVQQKMERVENVLRDMNLTdcqntligipnrmkgISIGEKKRLA 188
Cdd:TIGR01271 1299 QKVFIFSGTFRKNldpyeqwsdEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYV---------------LSNGHKQLMC 1363
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 808355238 189 FACEILTDPKILFCDEPTSGLDAfMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:TIGR01271 1364 LARSILSKAKILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHR 1411
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
64-310 |
3.20e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.79 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLdtngVEYL-GDVTVNGKKITKQKMRQMCAYVQQVDLF----CGTLTVR-------- 130
Cdd:PRK15079 47 GETLGVVGESGCGKSTFARAIIGL----VKATdGEVAWLGKDLLGMKDDEWRAVRSDIQMIfqdpLASLNPRmtigeiia 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 131 EQL-TYTAHMrmknaTVQQKMERVENVLRDMNLTdcQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK15079 123 EPLrTYHPKL-----SRQEVKDRVKAMMLKVGLL--PNLINRYPHEFSG---GQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 210 DAFMASEVVRALLDLANK-GKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGAVDRLcpFFDKLGPdfrvpesYNPAdf 288
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREmGLSLIFIAHD-LAVVKHISDRVLVMYLGHAVELGTYDEV--YHNPLHP-------YTKA-- 260
|
250 260
....*....|....*....|..
gi 808355238 289 VMSEISIsPETEQEDVTRIEYL 310
Cdd:PRK15079 261 LMSAVPI-PDPDLERNKTIQLL 281
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
63-262 |
4.09e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 51.93 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PGEVLALMGGSGAGKTTL-MNILAHLDTNGveylGDVTVNGKKITKQKmRQMCAYVQQVdlfcgtLTV----REQLTYT- 136
Cdd:PRK13638 26 LSPVTGLVGANGCGKSTLfMNLSGLLRPQK----GAVLWQGKPLDYSK-RGLLALRQQV------ATVfqdpEQQIFYTd 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 137 ----AHMRMKNATVQQK--MERVENVLrdmNLTDCQNTLigiPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLD 210
Cdd:PRK13638 95 idsdIAFSLRNLGVPEAeiTRRVDEAL---TLVDAQHFR---HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 808355238 211 AFMASEVVRALLDLANKGKTIIVVLHQpSSTVFRMFHKVCFMATGKTVYHGA 262
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHVIISSHD-IDLIYEISDAVYVLRQGQILTHGA 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
50-234 |
4.67e-07 |
|
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: 52.90 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 50 RKEViRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVEylGDVTVNGKKIT----KQKMRQMCAYV---QQVDL 122
Cdd:TIGR02633 273 RKRV-DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFE--GNVFINGKPVDirnpAQAIRAGIAMVpedRKRHG 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 FCGTLTVREQLTYTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLIGIPnrMKGISIGEKKRLAFACEILTDPKILFC 202
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLP--IGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVV 459
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-240 |
7.21e-07 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 52.41 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 25 DGSE---KGRKTIAWSGLVATVPQAgggRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMN-ILAHLDTNGveylGDVTV 100
Cdd:PRK10789 302 DGSEpvpEGRGELDVNIRQFTYPQT---DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSlIQRHFDVSE----GDIRF 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 101 NGKKITKQKM---RQMCAYVQQVD-LFCGTLTVREQLTytahmrMKNATvQQKME---RVENVLRD-MNLTDCQNTLIGI 172
Cdd:PRK10789 375 HDIPLTKLQLdswRSRLAVVSQTPfLFSDTVANNIALG------RPDAT-QQEIEhvaRLASVHDDiLRLPQGYDTEVGE 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 173 PNRMkgISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLHQPSS 240
Cdd:PRK10789 448 RGVM--LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLSA 512
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
60-236 |
7.49e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.12 E-value: 7.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 60 VAEPGEVLALMGGSGAGKTTLMNILA-HLDTNgveyLGDVTVNG------------------KKITKQKMRqmCAY-VQQ 119
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSgELIPN----LGDYEEEPswdevlkrfrgtelqnyfKKLYNGEIK--VVHkPQY 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 120 VDL----FCGTltVREQLTyTAHMRMKNATVQQKMErVENVL-RDMNltdcqnTLIGipnrmkgisiGEKKRLAFACEIL 194
Cdd:PRK13409 169 VDLipkvFKGK--VRELLK-KVDERGKLDEVVERLG-LENILdRDIS------ELSG----------GELQRVAIAAALL 228
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 808355238 195 TDPKILFCDEPTSGLDAFMASEVVRALLDLAnKGKTIIVVLH 236
Cdd:PRK13409 229 RDADFYFFDEPTSYLDIRQRLNVARLIRELA-EGKYVLVVEH 269
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
60-236 |
8.48e-07 |
|
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: 50.83 E-value: 8.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 60 VAEPGEVLALMGGSGAGKTTLMNILA-HLDTNgveyLGDVTVNG---------------KKITKQKMRQMCAYV--QQVD 121
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAgKLKPN----LGKFDDPPdwdeildefrgselqNYFTKLLEGDVKVIVkpQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 LFCGTL--TVREQLTYTAHMRMKNATVQQkMErVENVLrDMNLTDcqntligipnrmkgISIGEKKRLAFACEILTDPKI 199
Cdd:cd03236 98 LIPKAVkgKVGELLKKKDERGKLDELVDQ-LE-LRHVL-DRNIDQ--------------LSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 808355238 200 LFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
57-266 |
8.74e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 51.12 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 57 VSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNG-VEYLGDVTVNGKKITKQKMRQMcayVQQVdlF---CGTLTVR 130
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIEtpTGGeLYYQGQDLLKADPEAQKLLRQK---IQIV--FqnpYGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 131 EQLTYTAHMRMKNATVQQKMERVENVLRDMnltdcqnTLIGI--------PNRMKGisiGEKKRLAFACEILTDPKILFC 202
Cdd:PRK11308 109 KKVGQILEEPLLINTSLSAAERREKALAMM-------AKVGLrpehydryPHMFSG---GQRQRIAIARALMLDPDVVVA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 808355238 203 DEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK11308 179 DEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
177-240 |
8.78e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 8.78e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 177 KGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKG-KTIIVVLHQPSS 240
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIAS 1421
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
47-262 |
9.30e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 9.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKI----TKQKMRQMCAYVQQVDL 122
Cdd:PRK10253 16 GYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMT---PAHGHVWLDGEHIqhyaSKEVARRIGLLAQNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 123 fCGTLTVREQLTYT--AHMRMKNATVQQKMERVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDPKIL 200
Cdd:PRK10253 93 -PGDITVQELVARGryPHQPLFTRWRKEDEEAVTKAMQATGITHLAD------QSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPSSTVFRMFHKVCfMATGKTVYHGA 262
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIA-LREGKIVAQGA 227
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
64-236 |
9.93e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 50.89 E-value: 9.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHL--DTNGVEYLGDVTVNgkKITKQK----MRQMCAYVQQvdlFCGTLTVREQLTYTA 137
Cdd:PRK13643 32 GSYTALIGHTGSGKSTLLQHLNGLlqPTEGKVTVGDIVVS--STSKQKeikpVRKKVGVVFQ---FPESQLFEETVLKDV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 138 HMRMKNATVQQkmERVENVLRDmnltdcQNTLIGI--------PNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK13643 107 AFGPQNFGIPK--EKAEKIAAE------KLEMVGLadefweksPFELSG---GQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180
....*....|....*....|....*..
gi 808355238 210 DAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
48-236 |
1.36e-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: 51.47 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVN-GKKItkqkmrqmcAYVQQVDLFCGT 126
Cdd:TIGR03719 15 PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK---DFNGEARPQpGIKV---------GYLPQEPQLDPT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQ-----------LTYTAHMRMKNATVQ-------QKMERVENVLRDMNLTDCQNTL------IGIPN---RMKGI 179
Cdd:TIGR03719 83 KTVRENveegvaeikdaLDRFNEISAKYAEPDadfdklaAEQAELQEIIDAADAWDLDSQLeiamdaLRCPPwdaDVTKL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 808355238 180 SIGEKKRLAFACEILTDPKILFCDEPTSGLDAfmasEVVrALLD--LANKGKTIIVVLH 236
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESV-AWLErhLQEYPGTVVAVTH 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
64-264 |
1.52e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKT----TLMNILAhldTNGVeYLGDVTVNGKKI----TKQ--KMRqmcayVQQVDL-FCGTLT---- 128
Cdd:PRK09473 42 GETLGIVGESGSGKSqtafALMGLLA---ANGR-IGGSATFNGREIlnlpEKElnKLR-----AEQISMiFQDPMTslnp 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 129 ---VREQLtytahmrMKNATVQQKMERVENVLRDMNLTDCqntlIGIP---NRMK----GISIGEKKRLAFACEILTDPK 198
Cdd:PRK09473 113 ymrVGEQL-------MEVLMLHKGMSKAEAFEESVRMLDA----VKMPearKRMKmyphEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 199 ILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVD 264
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
49-236 |
1.59e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.15 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNIL-AHLDTNGveylGDVTVNGKKI---TKQKM----RQMCAYVQQV 120
Cdd:PRK11831 18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIgGQIAPDH----GEILFDGENIpamSRSRLytvrKRMSMLFQSG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFCgTLTVREQLTYT--AHMRMKNA----TVQQKMERVenvlrdmnltdcqnTLIGIPNRMKG-ISIGEKKRLAFACEI 193
Cdd:PRK11831 94 ALFT-DMNVFDNVAYPlrEHTQLPAPllhsTVMMKLEAV--------------GLRGAAKLMPSeLSGGMARRAALARAI 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 808355238 194 LTDPKILFCDEPTSGLDAFMASEVVRaLLDLANK--GKTIIVVLH 236
Cdd:PRK11831 159 ALEPDLIMFDEPFVGQDPITMGVLVK-LISELNSalGVTCVVVSH 202
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
66-236 |
3.32e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 49.49 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 66 VLALMGGSGAGKTTLMNILAHLDT--NGVEYLGDVTVN--GKKIT----KQKMrqmcAYV-QQVDLFcGTLTVREQLTYT 136
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRpqKGRIVLNGRVLFdaEKGIClppeKRRI----GYVfQDARLF-PHYKVRGNLRYG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 137 ahmrMKNATVQQKMERVEnvlrdmnltdcqntLIGI-------PNRMKGisiGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK11144 101 ----MAKSMVAQFDKIVA--------------LLGIeplldryPGSLSG---GEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180
....*....|....*....|....*...
gi 808355238 210 DAFMASEVVRALLDLANKGKT-IIVVLH 236
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIpILYVSH 187
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
448-560 |
4.27e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 47.89 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 448 AYFLAKSLAelpqYTILPMIYGTIIYWMAGLVASVT----SFLVFVFVCITLTWVAVSIAYVGACIFGDEGLVVTFMPMF 523
Cdd:COG0842 47 EILLGKVLA----YLLRGLLQALLVLLVALLFFGVPlrglSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLV 122
|
90 100 110
....*....|....*....|....*....|....*..
gi 808355238 524 VLPMLVFGGFYVNANSIPVYYQYVSFVSWFKHGFEAL 560
Cdd:COG0842 123 ILPLTFLSGAFFPIESLPGWLQAIAYLNPLTYFVEAL 159
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
53-237 |
7.57e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 47.25 E-value: 7.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKqkmrQMCAYVQQVdLFCG------- 125
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLN---PEKGEILFERQSIKK----DLCTYQKQL-CFVGhrsginp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TLTVREQLTYTAHMRMKNatvqqkMErVENVLRDMNLtdcqNTLIGIPNRMkgISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGA------VG-ITELCRLFSL----EHLIDYPCGL--LSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:PRK13540 155 LVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
49-237 |
7.87e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 49 GRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILahldtngveyLGDV-TVNGKKITkqkMRQMCAYVQQVD-LFcgT 126
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM----------LGELpPRSDASVV---IRGTVAYVPQVSwIF--N 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQLTYTAHMrmkNATVQQKMERVENVLRDMNLTDCQNtLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPT 206
Cdd:PLN03130 693 ATVRDNILFGSPF---DPERYERAIDVTALQHDLDLLPGGD-LTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190
....*....|....*....|....*....|.
gi 808355238 207 SGLDAFMASEVVRALLDLANKGKTIIVVLHQ 237
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKDELRGKTRVLVTNQ 799
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
53-237 |
1.05e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 53 VIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVEY-LGDVTVNGKKITK---QKMRQMCAYVQQVD-LFCGTl 127
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRI----VELeKGRIMIDDCDVAKfglTDLRRVLSIIPQSPvLFSGT- 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 128 tVREQLT-YTAHmrmKNATVQQKMERVEnvLRDMnltdCQNTLIGIPNRM----KGISIGEKKRLAFACEILTDPKILFC 202
Cdd:PLN03232 1326 -VRFNIDpFSEH---NDADLWEALERAH--IKDV----IDRNPFGLDAEVseggENFSVGQRQLLSLARALLRRSKILVL 1395
|
170 180 190
....*....|....*....|....*....|....*
gi 808355238 203 DEPTSGLDAFMASEVVRALLDlANKGKTIIVVLHQ 237
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHR 1429
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
54-261 |
1.11e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 47.67 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTTLMnilahLDTNGV--EYLGDVTVNGKKITK----QKMRQMCAYVQQ--VDLFCG 125
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLA-----LHLNGLlrPQKGKVLVSGIDTGDfsklQGIRKLVGIVFQnpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TlTVREQLTYTAHMRMKNATVQQKmeRVENVLRDMNLTDCQNtligipNRMKGISIGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK13644 93 R-TVEEDLAFGPENLCLPPIEIRK--RVDRALAEIGLEKYRH------RSPKTLSGGQGQCVALAGILTMEPECLIFDEV 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 206 TSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStvFRMFHKVCFMATGKTVYHG 261
Cdd:PRK13644 164 TSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE--LHDADRIIVMDRGKIVLEG 217
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
54-236 |
1.25e-05 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 47.42 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 54 IRNVSGVAEPGEVLALMGGSGAGKTT---LMNILAHLDTngveylGDVTVNGKKITKQ----KMRQMCAYVQQVD-LFCG 125
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAES------GQIIIDGDLLTEEnvwdIRHKIGMVFQNPDnQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 126 TlTVREQLTYTahMRMKNATVQQKMERVENVLrdmNLTDCQNTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFCDEP 205
Cdd:PRK13650 97 A-TVEDDVAFG--LENKGIPHEEMKERVNEAL---ELVGMQDFKEREPARLSG---GQKQRVAIAGAVAMRPKIIILDEA 167
|
170 180 190
....*....|....*....|....*....|..
gi 808355238 206 TSGLDAFMASEVVRALLDLANK-GKTIIVVLH 236
Cdd:PRK13650 168 TSMLDPEGRLELIKTIKGIRDDyQMTVISITH 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
48-266 |
1.37e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 48.31 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKT-TLMNILAHLDTNGveylGDVTvNGKKITKQKMRQMCAYVQQVD----- 121
Cdd:PRK10261 26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQAG----GLVQ-CDKMLLRRRSRQVIELSEQSAaqmrh 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 122 --------LFCGTLT-------VREQLTYTAHMRmKNATVQQKMERVENVLRDMNLTDCQNTLIGIPNRMKGisiGEKKR 186
Cdd:PRK10261 101 vrgadmamIFQEPMTslnpvftVGEQIAESIRLH-QGASREEAMVEAKRMLDQVRIPEAQTILSRYPHQLSG---GMRQR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 187 LAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSSTVFRMFHKVCFMATGKTVYHGAVDRL 266
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
47-236 |
1.95e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.58 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 47 GGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtngveylGDVTVNGkkitkqkmrqmcayvqqvdlfcGT 126
Cdd:PRK15064 328 GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLV----------GELEPDS----------------------GT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREqltytahmrmkNATV----QQKMERVENvlrDMNLTD--CQ--------NTLIGIPNRM-----------KGISI 181
Cdd:PRK15064 376 VKWSE-----------NANIgyyaQDHAYDFEN---DLTLFDwmSQwrqegddeQAVRGTLGRLlfsqddikksvKVLSG 441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 182 GEKKRLAFACEILTDPKILFCDEPTSGLDafMasEVVRAL-LDLANKGKTIIVVLH 236
Cdd:PRK15064 442 GEKGRMLFGKLMMQKPNVLVMDEPTNHMD--M--ESIESLnMALEKYEGTLIFVSH 493
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
62-210 |
2.73e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 62 EPGEVLALMGGSGAGKTTLMNILA---HLDTNGVEYLGDVTVNgkkitkqKMRQ---------MCAYVQQvdlfcGTLTV 129
Cdd:PRK11147 27 EDNERVCLVGRNGAGKSTLMKILNgevLLDDGRIIYEQDLIVA-------RLQQdpprnvegtVYDFVAE-----GIEEQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 130 REQLTYTAHMRMKNATVQQ-----KMERVENVLRDMNLTDCQN------TLIGIPNRMK--GISIGEKKRLAFACEILTD 196
Cdd:PRK11147 95 AEYLKRYHDISHLVETDPSeknlnELAKLQEQLDHHNLWQLENrinevlAQLGLDPDAAlsSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 808355238 197 PKILFCDEPTSGLD 210
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
156-234 |
3.35e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 3.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 156 VLRDMNL-TDCQNTLIGipnrmkGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVV 234
Cdd:PRK10982 374 VIDSMRVkTPGHRTQIG------SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIII 447
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
180-266 |
3.36e-05 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 46.65 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 180 SIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLhQPSSTVFRMFHKVCFMATGKTVY 259
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTT-QYMEEAEQLAHELTVIDRGRVIA 224
|
....*..
gi 808355238 260 HGAVDRL 266
Cdd:NF000106 225 DGKVDEL 231
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
41-278 |
3.57e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.96 E-value: 3.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 41 ATVPQAGGGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTNGVeylGDVTVNGkkitkqkmrqmcayvqQV 120
Cdd:PRK13546 27 ALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTV---GKVDRNG----------------EV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 121 DLFCGTLTVREQLTYTAHMRMKNATVQQKMERVENVLRDMNLTDCQNTLIGIPnrMKGISIGEKKRLAFACEILTDPKIL 200
Cdd:PRK13546 88 SVIAISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQP--VKKYSSGMRAKLGFSINITVNPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 808355238 201 FCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPSStVFRMFHKVCFMATGKTVYHGAVDRLCPFFDKLGPDFR 278
Cdd:PRK13546 166 VIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQ-VRQFCTKIAWIEGGKLKDYGELDDVLPKYEAFLNDFK 242
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
48-236 |
6.73e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.88 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTV-NGKKItkqkmrqmcAYVQQVDLFCGT 126
Cdd:PRK11819 17 PPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK---EFEGEARPaPGIKV---------GYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 127 LTVREQL-------------------TYTAHMRMKNATVqQKMERVENVLRDMNLTDCQNTL------IGIP---NRMKG 178
Cdd:PRK11819 85 KTVRENVeegvaevkaaldrfneiyaAYAEPDADFDALA-AEQGELQEIIDAADAWDLDSQLeiamdaLRCPpwdAKVTK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 179 ISIGEKKRLAFACEILTDPKILFCDEPTSGLDAfmasEVVrALLD--LANKGKTIIVVLH 236
Cdd:PRK11819 164 LSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA----ESV-AWLEqfLHDYPGTVVAVTH 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
42-234 |
1.12e-04 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 45.02 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 42 TVPQAGGGrkEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLDTngVEyLGDVTVNGKKITKQ---KMRQM-CAYV 117
Cdd:COG3845 264 SVRDDRGV--PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRP--PA-SGSIRLDGEDITGLsprERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 118 ----QQVDLfCGTLTVREQLTYTAH----------MRMKNATvqqkmERVENVLRDMNltdcqntlIGIPN---RMKGIS 180
Cdd:COG3845 339 pedrLGRGL-VPDMSVAENLILGRYrrppfsrggfLDRKAIR-----AFAEELIEEFD--------VRTPGpdtPARSLS 404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 808355238 181 IGEKKRLAFACEILTDPKILFCDEPTSGLDaFMASEVVR-ALLDLANKGKTIIVV 234
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLD-VGAIEFIHqRLLELRDAGAAVLLI 458
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
52-227 |
1.20e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 44.40 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 52 EVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLdtngVE-YLGDVTVNGKKIT-------KQKMRQmcayvqqvdLF 123
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGM----IEpTSGELLIDDHPLHfgdysyrSQRIRM---------IF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 124 ---CGTLTVREQLTYT--AHMRMKNA-TVQQKMERVENVLRDMNL-TDCQNTLigiPNRMkgiSIGEKKRLAFACEILTD 196
Cdd:PRK15112 94 qdpSTSLNPRQRISQIldFPLRLNTDlEPEQREKQIIETLRQVGLlPDHASYY---PHML---APGQKQRLGLARALILR 167
|
170 180 190
....*....|....*....|....*....|.
gi 808355238 197 PKILFCDEPTSGLDAFMASEVVRALLDLANK 227
Cdd:PRK15112 168 PKVIIADEALASLDMSMRSQLINLMLELQEK 198
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
64-236 |
2.49e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.19 E-value: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLDTngvEYLGDVTVNGKKITKQKMRqmcAYVQQ-------VDLFCGTLT-----VRE 131
Cdd:PRK10522 349 GELLFLIGGNGSGKSTLAMLLTGLYQ---PQSGEILLDGKPVTAEQPE---DYRKLfsavftdFHLFDQLLGpegkpANP 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 132 QL--TYTAHMRMKNatvqqKMERVENVLRDMNLtdcqntligipnrmkgiSIGEKKRLAFACEILTDPKILFCDEPTSGL 209
Cdd:PRK10522 423 ALveKWLERLKMAH-----KLELEDGRISNLKL-----------------SKGQKKRLALLLALAEERDILLLDEWAADQ 480
|
170 180
....*....|....*....|....*...
gi 808355238 210 DAFMASEVVRALLD-LANKGKTIIVVLH 236
Cdd:PRK10522 481 DPHFRREFYQVLLPlLQEMGKTIFAISH 508
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
162-240 |
3.25e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.86 E-value: 3.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 162 LTDCQNTLIGiPNRMKgISIGEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVRALLDL-ANKGKTIIVVLHQPSS 240
Cdd:PTZ00265 565 LPDKYETLVG-SNASK-LSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIIIAHRLST 642
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
63-245 |
5.66e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 5.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 63 PGEVLALMGGSGAGKTTLMNILAHLdtNGVEYLGDVTVNGKKITKQkmrqmcayvqqvdlfcgtltvreqltytahmrmk 142
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARE--LGPPGGGVIYIDGEDILEE---------------------------------- 44
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 143 natvqqkmervenvlrdmnlTDCQNTLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLDAF-----MASEV 217
Cdd:smart00382 45 --------------------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEE 104
|
170 180
....*....|....*....|....*...
gi 808355238 218 VRALLDLANKGKTIIVVLHQPSSTVFRM 245
Cdd:smart00382 105 LRLLLLLKSEKNLTVILTTNDEKDLGPA 132
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
416-548 |
7.03e-04 |
|
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.
Pssm-ID: 463674 [Multi-domain] Cd Length: 345 Bit Score: 42.38 E-value: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 416 MTFLFYFPSVNVITSELPVFLREHKSNIY--------SVEAYFLAKSLAELPQYTILPMIYGTIIYwmaGLVASVTSFLV 487
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKerllvsgvSPLQYWLGKILGDFLVGLLQLLIILLLLF---GIGIPFGNLGL 240
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 488 FVFVCITLTWVAVSIAYVGACIFGDEGLVVTFMPMFVLPMLVFGGFYVNANSIPVYYQYVS 548
Cdd:pfam12698 241 LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIF 301
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
64-239 |
1.17e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMN-ILAHLDTngVEylGDVTVNGKkitkqkmrqmCAYVQQvDLFCGTLTVREQLTYTAHMRMK 142
Cdd:TIGR00957 664 GALVAVVGQVGCGKSSLLSaLLAEMDK--VE--GHVHMKGS----------VAYVPQ-QAWIQNDSLRENILFGKALNEK 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 143 NatVQQKMERVEnVLRDMN-LTDCQNTLIGipnrMKGISI--GEKKRLAFACEILTDPKILFCDEPTSGLDAFMASEVVR 219
Cdd:TIGR00957 729 Y--YQQVLEACA-LLPDLEiLPSGDRTEIG----EKGVNLsgGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
|
170 180
....*....|....*....|..
gi 808355238 220 ALLDLAN--KGKTIIVVLHQPS 239
Cdd:TIGR00957 802 HVIGPEGvlKNKTRILVTHGIS 823
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
56-103 |
1.47e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 808355238 56 NVSGVAEPGEVLALMGGSGAGKTTLMNILAhldtnGV----EYLGDVTVNGK 103
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLS-----GVyphgSYEGEILFDGE 65
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
179-236 |
1.92e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 1.92e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 808355238 179 ISIGEKKRLAFACEILT---DPKILFCDEPTSGLDAFMASEVVRALLDLANKGKTIIVVLH 236
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEH 870
|
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| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
48-211 |
1.94e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 40.98 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 48 GGRKEVIRNVSGVAEPGEVLALMGGSGAGKTTLMNILAHLD--TNGVEYLGDVTVNGKKitkQKMRQmCAYV-QQVDLFc 124
Cdd:PRK11650 14 DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLEriTSGEIWIGGRVVNELE---PADRD-IAMVfQNYALY- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 125 GTLTVREQLTYTahmrMKNATV--QQKMERVENVLRDMNLTDcqnTLIGIPNRMKGisiGEKKRLAFACEILTDPKILFC 202
Cdd:PRK11650 89 PHMSVRENMAYG----LKIRGMpkAEIEERVAEAARILELEP---LLDRKPRELSG---GQRQRVAMGRAIVREPAVFLF 158
|
....*....
gi 808355238 203 DEPTSGLDA 211
Cdd:PRK11650 159 DEPLSNLDA 167
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
148-239 |
4.04e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 39.68 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 148 QKMERVENVLRDMNLTDCQNTLiGIPNRMKGISIGEKK--RLAFAC-EILTDPKILFCDEPTSGLDAFMASEVVRALLDL 224
Cdd:pfam13304 207 EKSLLVDDRLRERGLILLENGG-GGELPAFELSDGTKRllALLAALlSALPKGGLLLIDEPESGLHPKLLRRLLELLKEL 285
|
90
....*....|....*
gi 808355238 225 ANKGKTIIVVLHQPS 239
Cdd:pfam13304 286 SRNGAQLILTTHSPL 300
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
64-239 |
7.15e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 39.35 E-value: 7.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 64 GEVLALMGGSGAGKTTLMNILAHLdtngveylgdVTVNGKKITKQKmRQMCAYVQQVDLFcGTLTVREQLTY---TAHMR 140
Cdd:TIGR00954 478 GNNLLICGPNGCGKSSLFRILGEL----------WPVYGGRLTKPA-KGKLFYVPQRPYM-TLGTLRDQIIYpdsSEDMK 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 808355238 141 MKNATVQQKMERVENVLRDmNLTDCQNTLIGIPNRMKGISIGEKKRLAFACEILTDPKILFCDEPTSGLdafmASEVVRA 220
Cdd:TIGR00954 546 RRGLSDKDLEQILDNVQLT-HILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAV----SVDVEGY 620
|
170 180
....*....|....*....|
gi 808355238 221 LLDLA-NKGKTIIVVLHQPS 239
Cdd:TIGR00954 621 MYRLCrEFGITLFSVSHRKS 640
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
176-239 |
7.26e-03 |
|
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: 38.07 E-value: 7.26e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 808355238 176 MKGISIGEKKRLAFACEI-LTDPKILFC-DEPTSGLDAFMASEVVRALLDLANKGKTIIVVLHQPS 239
Cdd:cd03238 85 LSTLSGGELQRVKLASELfSEPPGTLFIlDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
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