|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
128-1600 |
1.69e-120 |
|
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: 421.34 E-value: 1.69e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 128 VIFKDTFSY------HLKFSWGQRI---PKTKEHKDHSAPCEPLNNKMicENSAFWEKGFVAFQAAINAGIiemiTNHSV 198
Cdd:TIGR01257 551 VVFPDMYPWtsslppHVKYKIRMDIdvvEKTNKIKDRYWDSGPRADPV--EDFRYIWGGFAYLQDMVEQGI----TRSQM 624
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 199 MEEL-MSVIGSNMKMPPFiaqggVATDFFIFF--CVISFSSLIYYLSVNIT------QERQYMTTLMAMMGLRESAFWLS 269
Cdd:TIGR01257 625 QAEPpVGIYLQQMPYPCF-----VDDSFMIILnrCFPIFMVLAWIYSVSMTvksivlEKELRLKETLKNQGVSNAVIWCT 699
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 270 WSLMYAGFILVVAVLMSLIVKSAQVVVLTGFMVVFLLFLFYGLSLITLSFLMSVLIKKPFLTGL--AIFILTVFWGSLGF 347
Cdd:TIGR01257 700 WFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAAcsGVIYFTLYLPHILC 779
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 348 TALYKHLPAFVEWTLCFLSPFAFTTGMAQLIHLDYD----VNSNVNlNSP--NNSYLIMATLFMLVLDALLYLVLALYFD 421
Cdd:TIGR01257 780 FAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQglglQWSNIG-NSPleGDEFSFLLSMKMMLLDAALYGLLAWYLD 858
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 422 KITLSKYGHQRSPLFFLKSSYWFKRRGASHVVLENEIDSDPSLNDSLEPVSPE-----FQGKE------AIRIKNLKK-- 488
Cdd:TIGR01257 859 QVFPGDYGTPLPWYFLLQESYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEgindsFFERElpglvpGVCVKNLVKif 938
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 489 EYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTITGVCPQSN 568
Cdd:TIGR01257 939 EPSGR----PAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAVRQSLGMCPQHN 1012
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 569 VQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:TIGR01257 1013 ILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 649 DPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWGIGYHLSL------------- 715
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrkmkniqsqrgg 1172
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 716 ------------------HLNEAC-------DPEGITSLVKKHISDARLTTQSEERLVYILPLE--RTNKFPDLYRDLDR 768
Cdd:TIGR01257 1173 cegtcsctskgfstrcpaRVDEITpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKnfKQRAYASLFRELEE 1252
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 769 C-SNQGIEDYGVSMTTLNEVFLKLegksmADESDvgiCGRLQSDGARDMESLVELEQVLSLDSSGSSVSGMA-------- 839
Cdd:TIGR01257 1253 TlADLGLSSFGISDTPLEEIFLKV-----TEDAD---SGSLFAGGAQQKRENANLRHPCSGPTEKAGQTPQAshtcspgq 1324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 840 -------------------------LWRQQLCAVAKVRFFKLKNERKSLMTVLLLFGISFVPQLLEHLVYKVYHKSYSWG 894
Cdd:TIGR01257 1325 paahpegqpppepedpgvplntgarLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALT 1404
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 895 LSPSMY-----FLSPGQPPQDPLTHL--LVINRTG-------------------------SSIDNFVHALRQQGIALDLD 942
Cdd:TIGR01257 1405 LHPWMYgqqytFFSMDEPNSEHLEVLadVLLNKPGfgnrclkeewlpeypcgnstpwktpSVSPNITHLFQKQKWTAAHP 1484
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 943 ALGTRNGTEEALY-----------------------------------------------------------NGAITVLG 963
Cdd:TIGR01257 1485 SPSCRCSTREKLTmlpecpegagglpppqrtqrsteilqdltdrnisdflvktypalirsslkskfwvneqrYGGISIGG 1564
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 964 EEKALRFSVACNAKRLNCFPVLMDiISNGLLGIFNSSE------RIQTD---------------------------RSTV 1010
Cdd:TIGR01257 1565 KLPAIPITGEALVGFLSDLGQMMN-VSGGPVTREASKEmpdflkHLETEdnikvwfnnkgwhalvsflnvahnailRASL 1643
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1011 FEEHMLYEYGFM----------------------SNAFFWIPV--AASLTP-YIAMGSISDHKKKVLSQLWTSGLYPSAY 1065
Cdd:TIGR01257 1644 PKDRDPEEYGITvisqplnltkeqlseitvlttsVDAVVAICVifAMSFVPaSFVLYLIQERVNKAKHLQFISGVSPTTY 1723
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1066 WCGQALVDIPIY-----FLILFLMQIMDSVFSSEEFISVMESLLIQipcsigYASSLIFMTYVISFIFRNGRKNSGIWSF 1140
Cdd:TIGR01257 1724 WLTNFLWDIMNYavsagLVVGIFIGFQKKAYTSPENLPALVALLML------YGWAVIPMMYPASFLFDVPSTAYVALSC 1797
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1141 FFLIV-----TIFFIIATDINEYGFLE---LLICTFLVPPFTLIGSLLI---FSEVSYDSVDYLGTSESQLVFLALLIpy 1209
Cdd:TIGR01257 1798 ANLFIginssAITFVLELFENNRTLLRfnaMLRKLLIVFPHFCLGRGLIdlaLSQAVTDVYAQFGEEHSANPFQWDLI-- 1875
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1210 lHFLLFFFILRCLERYLRkkSLRVDPVFRISprSCPAVPNPEEPGEEDEDVQMERVRT-TGAMAT--LQTDEkpviiasc 1286
Cdd:TIGR01257 1876 -GKNLVAMAVEGVVYFLL--TLLIQHHFFLS--RWIAEPAKEPIFDEDDDVAEERQRIiSGGNKTdiLRLNE-------- 1942
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1287 LRKEYIGRTKRcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGF 1362
Cdd:TIGR01257 1943 LTKVYSGTSSP---------AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVHQN 2013
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1363 LGYCPQENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVL 1442
Cdd:TIGR01257 2014 MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVL 2093
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1443 LDEPSTGMDPEGQQQMWQAIrATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLLEMKVK 1522
Cdd:TIGR01257 2094 LDEPTTGMDPQARRMLWNTI-VSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIK 2172
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1523 TPS-----QVEPLNTEIMRLFPQAARQERYSSLMVYKLPVEDvrpLSEAFFKLERLKENFDLEEYSLSQSTLEQVFLELS 1597
Cdd:TIGR01257 2173 SPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS---LARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFA 2249
|
...
gi 153792543 1598 KEQ 1600
Cdd:TIGR01257 2250 KQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
481-704 |
8.29e-83 |
|
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: 270.92 E-value: 8.29e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:cd03263 1 LQIRNLTKTYKK--GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLK 704
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1287-1508 |
4.23e-81 |
|
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: 265.91 E-value: 4.23e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1287 LRKEYIGRTKrcfskmkkkIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGF 1362
Cdd:cd03263 6 LTKTYKKGTK---------PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGysirTDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1363 LGYCPQENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVL 1442
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1443 LDEPSTGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1508
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
481-699 |
1.99e-76 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 253.45 E-value: 1.99e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1303-1511 |
1.43e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.72 E-value: 1.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTV 1378
Cdd:COG1131 11 GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRrrigYVPQEPALYPDLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:COG1131 91 RENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSGLDPEARREL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1459 WQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKF 1511
Cdd:COG1131 171 WELLREL---AAEGKtvLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
481-699 |
9.71e-61 |
|
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: 208.56 E-value: 9.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK--EPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
481-694 |
3.29e-57 |
|
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: 195.69 E-value: 3.29e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLfakikgilpheveqevqqvlqdlemeniqdilaqnlSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1303-1514 |
5.53e-54 |
|
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: 189.30 E-value: 5.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTV 1378
Cdd:COG4555 12 GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrqigVLPDERGLYDRLTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:COG4555 92 RENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1459 WQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKD 1514
Cdd:COG4555 172 REILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEE 226
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1307-1596 |
9.82e-53 |
|
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: 187.60 E-value: 9.82e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGFLGYCPQENVLWPNLTVKEHL 1382
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvREPRKVRRSIGIVPQYASVDEDLTGRENL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:TIGR01188 88 EMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYI 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1463 RAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYlLEMKVKTPSQVEPLNTE-IMRLFP-Q 1540
Cdd:TIGR01188 168 RA-LKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMlIAELGEtG 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1541 AARQERYSSLMVYKLPVED-VRPLSEAffkLERLKEN-FDLEEYSLSQSTLEQVFLEL 1596
Cdd:TIGR01188 246 LGLLAVTVDSDRIKILVPDgDETVPEI---VEAAIRNgIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1303-1498 |
1.01e-51 |
|
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: 179.90 E-value: 1.01e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTV 1378
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrrigYLPEEPSLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLElyaavkglkkkdavvtitrlvnalklqdhlkalvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:cd03230 91 RENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREF 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153792543 1459 WQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03230 135 WELLR-ELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
481-695 |
1.16e-50 |
|
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: 178.54 E-value: 1.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveALRGLGFDIYEGqITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMddSDAVLTI 560
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ--PQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQsnvQFGF---LTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQ 637
Cdd:cd03264 74 IGYLPQ---EFGVypnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 638 VLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLK 695
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
493-793 |
4.09e-50 |
|
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: 180.28 E-value: 4.09e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 493 KHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVseMDDSDAVLTITGVCPQSNVQFG 572
Cdd:TIGR01188 2 VYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQYASVDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 573 FLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLS 652
Cdd:TIGR01188 80 DLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 653 RHRIWNLL-KERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWG-----IGYHLSLHLNEACDpEGI 726
Cdd:TIGR01188 160 RRAIWDYIrALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGkdtleSRPRDIQSLKVEVS-MLI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 727 TSLVKKHISDARLTTQSEERLVYILPLERTnkFPDLYRDLDRcsnQGIEDYGVSMT--TLNEVFLKLEG 793
Cdd:TIGR01188 239 AELGETGLGLLAVTVDSDRIKILVPDGDET--VPEIVEAAIR---NGIRIRSISTErpSLDDVFLKLTG 302
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1304-1601 |
5.78e-50 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 179.53 E-value: 5.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-YCPQENVLWPNLTVKEHL 1382
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIgYLPEERGLYPKMKVGEQL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:COG4152 93 VYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1463 RATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemKVKTPSQVEPLNTeimrlFPQ 1540
Cdd:COG4152 173 REL---AAKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL---RLEADGDAGWLRA-----LPG 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1541 AARQERYSSLMVYKLP-VEDVRPLseaffkLERLKENFDLEEYSLSQSTLEQVFLELSKEQE 1601
Cdd:COG4152 242 VTVVEEDGDGAELKLEdGADAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
481-704 |
6.94e-49 |
|
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: 173.71 E-value: 6.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:cd03265 1 IEVENLVKKY----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLK 704
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
481-699 |
5.27e-48 |
|
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: 171.36 E-value: 5.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQ-SNVQFGFLTVRENLrLFA-KIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLtlgiAILG---- 634
Cdd:COG1122 78 -GLVFQnPDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
481-694 |
1.79e-47 |
|
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: 169.59 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVL-- 558
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 --TItGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDP 636
Cdd:cd03255 81 rrHI-GFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 637 QVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADiLADRKVFISNGRL 694
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1307-1508 |
1.12e-46 |
|
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: 167.16 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGFLGYCPQENVLWPNLTVKEHL 1382
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREVRRRIGIVFQDLSVDDELTGWENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:cd03265 95 YIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYI 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 1463 RATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1508
Cdd:cd03265 175 EKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
482-693 |
1.64e-46 |
|
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: 166.49 E-value: 1.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYsgKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTIt 561
Cdd:cd03225 1 ELKNLSFSY--PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCPQ-SNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03225 78 GLVFQnPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
481-698 |
2.38e-46 |
|
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: 166.39 E-value: 2.38e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVLTI 560
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1290-1502 |
1.72e-45 |
|
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: 163.61 E-value: 1.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1290 EYIGRTKRcfskMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-YCPQ 1368
Cdd:cd03269 2 EVENVTKR----FGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIgYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1369 ENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1449 GMDPEGQQQMWQAIRATFTNtERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03269 158 GLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
478-694 |
5.59e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 162.52 E-value: 5.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD-A 556
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERElA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 557 VLtitgvcpqSNVQFGF----------LTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKL 626
Cdd:COG1136 82 RL--------RRRHIGFvfqffnllpeLTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADIlADRKVFISNGRL 694
Cdd:COG1136 154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
481-693 |
2.96e-44 |
|
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: 159.95 E-value: 2.96e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemDDSDAVLTI 560
Cdd:COG4133 3 LEAENLSCRR----GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIR--DAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEveQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQfmDEADILADRKVFISNGR 693
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLArGGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
481-694 |
1.45e-43 |
|
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: 157.76 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQtvsEMDDSDAVLTI 560
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGK---SYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILphevEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 641 LDEPTAGLDPLSRHRIWNLL-KERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1281-1599 |
1.02e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 159.48 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1281 VIIASCLRKEY---------IGRTKRCFSKMKKKI-ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF 1350
Cdd:COG4586 1 IIEVENLSKTYrvyekepglKGALKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1351 LKGsgggaalgflgYCPQEN----------V------LWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLK 1414
Cdd:COG4586 81 VLG-----------YVPFKRrkefarrigvVfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1415 ALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAVCDRVAI 1492
Cdd:COG4586 150 TPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKE--YNRERGTtiLLTSHDMDDIEALCDRVIV 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1493 MVSGRLRCIGSIQHLKSKFGKDYLLEMKVKTPsqVEPLNteimrlFPQAARQERYSSLMVyKLPVEDVRPLSEAffkLER 1572
Cdd:COG4586 228 IDHGRIIYDGSLEELKERFGPYKTIVLELAEP--VPPLE------LPRGGEVIEREGNRV-RLEVDPRESLAEV---LAR 295
|
330 340
....*....|....*....|....*..
gi 153792543 1573 LKENFDLEEYSLSQSTLEQVFLELSKE 1599
Cdd:COG4586 296 LLARYPVRDLTIEEPPIEEVIRRIYKE 322
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
481-695 |
1.87e-42 |
|
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: 155.32 E-value: 1.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSdavlti 560
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISN--GRLK 695
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1297-1499 |
8.36e-42 |
|
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: 152.76 E-value: 8.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1297 RCFSKM-KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGflgycPQENV---- 1371
Cdd:cd03268 4 NDLTKTyGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----ALRRIgali 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 ----LWPNLTVKEHLELYAAVKGLKKKDavvtITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPS 1447
Cdd:cd03268 79 eapgFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1448 TGMDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1499
Cdd:cd03268 155 NGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
480-695 |
1.96e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.71 E-value: 1.96e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSdavlt 559
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 iTGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:COG1116 82 -RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISN--GRLK 695
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
481-693 |
4.72e-41 |
|
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: 151.05 E-value: 4.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV-LT 559
Cdd:cd03224 1 LEVENLNAGY----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERArAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ItGVCPQSNVQFGFLTVRENLRLFAKIKGilPHEVEQEVQQVlqdLEM----ENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:cd03224 77 I-GYVPEGRRIFPELTVEENLLLGAYARR--RAKRKARLERV---YELfprlKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-798 |
7.21e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 154.60 E-value: 7.21e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemDDSDAVLT 559
Cdd:PRK13536 41 AIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQ-SNVQFGFlTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:PRK13536 115 RIGVVPQfDNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLkkkwgIGYHLSLHL 717
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL-----IDEHIGCQV 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 718 NE--ACDPEGITSLVKKHISdaRLTTQSEERLVYILPLERTNKFPDLY---RDLDRCSNqgiedygvsmttLNEVFLKLE 792
Cdd:PRK13536 269 IEiyGGDPHELSSLVKPYAR--RIEVSGETLFCYAPDPEQVRVQLRGRaglRLLQRPPN------------LEDVFLRLT 334
|
....*.
gi 153792543 793 GKSMAD 798
Cdd:PRK13536 335 GREMEK 340
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
480-693 |
1.85e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 152.27 E-value: 1.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMddSDAVLT 559
Cdd:PRK13537 7 PIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR--ARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQ-SNVQFGFlTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:PRK13537 81 RVGVVPQfDNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLArGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
481-698 |
5.28e-40 |
|
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: 147.81 E-value: 5.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDavlti 560
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR----- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
480-699 |
2.34e-39 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 2.34e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD---- 555
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRElarr 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 -AVLtitgvcPQSNVQFGFLTVRENLRLfakikGILPH---------EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRK 625
Cdd:COG1120 77 iAYV------PQEPPAPFGLTVRELVAL-----GRYPHlglfgrpsaEDREAVEEALERTGLEHLADRPVDELSGGERQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
500-646 |
3.29e-39 |
|
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: 143.17 E-value: 3.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSeMDDSDAVLTITGVCPQSNVQFGFLTVREN 579
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLT-DDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 580 LRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQN----LSGGQKRKLTLGIAILGDPQVLLLDEPTA 646
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
481-694 |
6.50e-39 |
|
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: 145.34 E-value: 6.50e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AVL 558
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQSNVQFGFLTVRENLRLFAKIKGILP-HEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQ 637
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSeEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 638 VLLLDEPTAGLDPLSRHRIWNL---LKERRAGRVIVFSTQfMDEADILADRKVFISNGRL 694
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLirsLKKELGLTSIMVTHD-LDTAFAIADRIAVLYDGKI 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-797 |
6.64e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.56 E-value: 6.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmDDSDavlt 559
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-EDRR---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itgvcpqsnvQFGFL----------TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:COG4152 72 ----------RIGYLpeerglypkmKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWG 708
Cdd:COG4152 142 AALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 709 iGYHLSLHLNEacDPEGITSLvkkhisdARLTTQSEERLVYILPLERTNKFPDLYRDLdrCSNQGIEDYGVSMTTLNEVF 788
Cdd:COG4152 222 -RNTLRLEADG--DAGWLRAL-------PGVTVVEEDGDGAELKLEDGADAQELLRAL--LARGPVREFEEVRPSLNEIF 289
|
....*....
gi 153792543 789 LKLEGKSMA 797
Cdd:COG4152 290 IEVVGEKAE 298
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
481-694 |
6.66e-39 |
|
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: 145.02 E-value: 6.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSP-----PTTGSVTIYNQTVSEMDDSD 555
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 AVL--TITGVCPQSNVqfgF-LTVRENLRLFAKIKGILPHEV-EQEVQQVLQDLEM-ENIQDIL-AQNLSGGQKRKLTLG 629
Cdd:cd03260 77 LELrrRVGMVFQKPNP---FpGSIYDNVAYGLRLHGIKLKEElDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1299-1603 |
9.33e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 147.64 E-value: 9.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1299 FSKMKK----KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGFLGYCPQEN 1370
Cdd:PRK13537 10 FRNVEKrygdKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGepvpSRARHARQRVGVVPQFD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1371 VLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:PRK13537 90 NLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1451 DPEGQQQMWQAIRATFTnteRGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL-KSKFGKDyLLEMKVKTPsqv 1527
Cdd:PRK13537 170 DPQARHLMWERLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDP--- 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1528 EPLNTEimrLFPQAARQE-RYSSLMVYklpVEDVRPLseaffkLERLKENFDLeEYSLSQSTLEQVFLELSKEQELD 1603
Cdd:PRK13537 243 VALRDE---LAPLAERTEiSGETLFCY---VRDPEPL------HARLKGRAGL-RYLHRPANLEDVFLRLTGREMQD 306
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
480-699 |
1.34e-38 |
|
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: 144.74 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AV 557
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKElyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTITGVCPQSNVQFGFLTVREN----LRLFAKIKgilPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENvafpLREHTDLS---EAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR----VIVfsTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELIRELRDELgltsVVV--THDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
458-713 |
1.62e-38 |
|
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: 153.38 E-value: 1.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 458 IDSDPSLNDSLEPVSPEFQGkeAIRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT 537
Cdd:COG4987 313 LDAPPAVTEPAEPAPAPGGP--SLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 538 TGSVTIYNQTVSEMDDsDAVLTITGVCPQSNVQF-GflTVRENLRLfAKikgilPHEVEQEVQQVLQDLEmenIQDILAQ 616
Cdd:COG4987 389 SGSITLGGVDLRDLDE-DDLRRRIAVVPQRPHLFdT--TLRENLRL-AR-----PDATDEELWAALERVG---LGDWLAA 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 617 --------------NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADiL 682
Cdd:COG4987 457 lpdgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-R 535
|
250 260 270
....*....|....*....|....*....|.
gi 153792543 683 ADRKVFISNGRLKCAGSSLFLKKKWGIGYHL 713
Cdd:COG4987 536 MDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1303-1499 |
5.08e-38 |
|
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: 141.95 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGeVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTV 1378
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRrrigYLPQEFGVYPNFTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEgqqqm 1458
Cdd:cd03264 90 REFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE----- 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1459 wQAIRatFTN------TERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1499
Cdd:cd03264 165 -ERIR--FRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
481-694 |
1.44e-37 |
|
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: 140.73 E-value: 1.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMddsDAVLTI 560
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV---PPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03259 154 LDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
495-700 |
1.69e-37 |
|
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: 141.27 E-value: 1.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 495 GKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV-LTItGVCPQSNVQFGF 573
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIArLGI-GYVPEGRRIFPS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 574 LTVRENLRLFAKIKGIlPHEVEQEVQQVLqDL-----EMeniQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:COG0410 93 LTVEENLLLGAYARRD-RAEVRADLERVY-ELfprlkER---RRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 649 DPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSS 700
Cdd:COG0410 168 APLIVEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
482-693 |
1.76e-36 |
|
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: 135.45 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavltit 561
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 gvcpqsnvqfgfltvrenlrlfakikgilPHEVEQEVQQVLQdlemeniqdilaqnLSGGQKRKLTLGIAILGDPQVLLL 641
Cdd:cd00267 68 -----------------------------LEELRRRIGYVPQ--------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 642 DEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
481-693 |
1.76e-36 |
|
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: 135.97 E-value: 1.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQSNVQFGFlTVRENLrlfakikgilpheveqevqqvlqdlemeniqdilaqnLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03228 79 -AYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADiLADRKVFISNGR 693
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
481-694 |
2.86e-36 |
|
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: 137.71 E-value: 2.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTi 560
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpQSNV-----QFGFL---TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAI 632
Cdd:cd03258 81 -----RRRIgmifqHFNLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
480-699 |
6.17e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 137.14 E-value: 6.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmddsdAVLT 559
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVcPQ-SNVQFGF-LTVRE--------NLRLFakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:COG1121 77 IGYV-PQrAEVDWDFpITVRDvvlmgrygRRGLF----RRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFIsNGRLKCAGS 699
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
481-699 |
6.36e-36 |
|
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: 136.80 E-value: 6.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvsEMDDSDavltI 560
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV--------LFDGED----I 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGF------------LTVRENLRL---FAKIKGILP-------HEVEQEVQQVLQDLEMENIQDILAQNL 618
Cdd:cd03219 65 TGLPPHEIARLGIgrtfqiprlfpeLTVLENVMVaaqARTGSGLLLararreeREARERAEELLERVGLADLADRPAGEL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 619 SGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVfstqfMDEADI-----LADRKVFISNG 692
Cdd:cd03219 145 SYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRElRERGITVL-----LVEHDMdvvmsLADRVTVLDQG 219
|
....*..
gi 153792543 693 RLKCAGS 699
Cdd:cd03219 220 RVIAEGT 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
448-700 |
6.59e-36 |
|
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: 144.28 E-value: 6.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 448 GASHVVLEN--EIDSDPSLNDSLEPVSPEFQGKE-AIRIKNLKKEY-SGKHGKVEALRGLGFDIYEGQITALLGHSGAGK 523
Cdd:COG1123 225 GPPEEILAApqALAAVPRLGAARGRAAPAAAAAEpLLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGK 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 524 TTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD-AVLtitgvcpQSNVQFGF----------LTVRENLRLFAKIKGILP- 591
Cdd:COG1123 305 STLARLLLGLLRPTSGSILFDGKDLTKLSRRSlREL-------RRRVQMVFqdpysslnprMTVGDIIAEPLRLHGLLSr 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 592 HEVEQEVQQVLQDLEM-ENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRV 668
Cdd:COG1123 378 AERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLT 457
|
250 260 270
....*....|....*....|....*....|..
gi 153792543 669 IVFSTQFMDEADILADRKVFISNGRLKCAGSS 700
Cdd:COG1123 458 YLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
478-694 |
1.23e-35 |
|
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: 136.31 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIyNQTVSEMDDSDAV 557
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV-AGLVPWKRRKKFL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQ 637
Cdd:cd03267 94 RRIGVVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 638 VLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
481-693 |
1.98e-35 |
|
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: 133.47 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVL-T 559
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLrR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFLTVRENLRLfakikgilpheveqevqqvlqdlemeniqdilaqNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1295-1502 |
2.01e-35 |
|
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: 134.80 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1295 TKRcFSKMKKKI-ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGFLGYCPQE 1369
Cdd:cd03266 8 TKR-FRDVKKTVqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvKEPAEARRRLGFVSDS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1370 NVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:cd03266 87 TGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1450 MDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03266 167 LDVMATRALREFIRQ-LRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
482-694 |
2.40e-35 |
|
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: 135.94 E-value: 2.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTiynqtvseMDDSDavltIT 561
Cdd:COG0411 6 EVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRIL--------FDGRD----IT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCP------------QsNVQ-FGFLTVRENLRL---------FAKIKGILP------HEVEQEVQQVLQDLEMENIQDI 613
Cdd:COG0411 70 GLPPhriarlgiartfQ-NPRlFPELTVLENVLVaaharlgrgLLAALLRLPrarreeREARERAEELLERVGLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 614 LAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIvfsTQFMDEADI-----LADRKVF 688
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGI---TILLIEHDMdlvmgLADRIVV 225
|
....*.
gi 153792543 689 ISNGRL 694
Cdd:COG0411 226 LDFGRV 231
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
480-694 |
3.91e-35 |
|
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: 134.93 E-value: 3.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAvlt 559
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAF--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itgvcpQSNVQFGF----------LTVRENLRLFAKIKGILphEVEQEVQQVLQDLEM-ENIQDILAQNLSGGQKRKLTL 628
Cdd:COG1124 78 ------RRRVQMVFqdpyaslhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA--GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
481-748 |
4.24e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 135.64 E-value: 4.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemdDSDAVLTI 560
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL---DEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpQSNV---------QFGFLTVR-------ENLrlfakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKR 624
Cdd:TIGR04520 76 -----RKKVgmvfqnpdnQFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 625 KltlgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEAdILADRKVFISNGRLKCAG 698
Cdd:TIGR04520 144 R----VAIAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKlnKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEG 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 699 S--SLFLK----KKWGIG----YHLSLHLNEacdpEGITslVKKHIsdarlttQSEERLV 748
Cdd:TIGR04520 219 TprEIFSQvellKEIGLDvpfiTELAKALKK----RGIP--LPPDI-------LTEEELV 265
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
482-698 |
5.80e-35 |
|
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: 133.43 E-value: 5.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLtit 561
Cdd:cd03235 1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 gvcPQS-NVQFGF-LTVRE--NLRLFAKIK--GILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:cd03235 74 ---PQRrSIDRDFpISVRDvvLMGLYGHKGlfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFIsNGRLKCAG 698
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
481-694 |
7.66e-35 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 133.25 E-value: 7.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD-AVL- 558
Cdd:COG2884 2 IRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREiPYLr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 -TItGVCPQSnvqFGFL---TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGG-QKRkltLGI--A 631
Cdd:COG2884 79 rRI-GVVFQD---FRLLpdrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIarA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFST---QFMDEadiLADRKVFISNGRL 694
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIAThdlELVDR---MPKRVLELEDGRL 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
480-699 |
7.91e-35 |
|
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: 141.19 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT---TGSVTIYNQTVSEMDDSDA 556
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 557 VLTItGVCPQS-NVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:COG1123 82 GRRI-GMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
471-699 |
9.30e-35 |
|
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: 141.82 E-value: 9.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 471 VSPEFQGKEAIRIKNLKKEYsgkHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSE 550
Cdd:COG4988 327 APLPAAGPPSIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 551 MDDSDAVLTITGVcPQSNVQFGfLTVRENLRLFAkikgilPHEVEQEVQQVLQDLemeNIQDILAQ-------------- 616
Cdd:COG4988 404 LDPASWRRQIAWV-PQNPYLFA-GTIRENLRLGR------PDASDEELEAALEAA---GLDEFVAAlpdgldtplgeggr 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 617 NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQfmDEADI-LADRKVFISNGRLK 695
Cdd:COG4988 473 GLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIV 550
|
....
gi 153792543 696 CAGS 699
Cdd:COG4988 551 EQGT 554
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
481-694 |
1.13e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 132.25 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGkveaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdSDAVLTI 560
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP-PPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGfLTVRENLRLFAKIKGILPHEveQEVQQVLQDLEMEniQDIL---AQNLSGGQKRKLTLGIAILGDPQ 637
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLP--PDILdkpVERLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 638 VLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
480-694 |
1.22e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.77 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEM-----Dds 554
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLppekrN-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 davltiTGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILG 634
Cdd:COG3842 79 ------VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFST--QfmDEADILADRKVFISNGRL 694
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
482-698 |
1.88e-34 |
|
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: 130.63 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavltit 561
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 gvcpqsnvqfgfltvrenLRLFAKIKGILPheveqevqQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLL 641
Cdd:cd03214 68 ------------------PKELARKIAYVP--------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 642 DEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
480-694 |
2.99e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 135.59 E-value: 2.99e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvsemDDSDavlt 559
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILI--------GGRD---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCP---------QSNVQFGFLTVRENLrLFA-KIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:COG3839 67 VTDLPPkdrniamvfQSYALYPHMTVYENI-AFPlKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG3839 146 RALVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
482-699 |
5.37e-34 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 131.11 E-value: 5.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTIT 561
Cdd:TIGR03410 2 EVSNLNVYYGQSH----ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQ---VLQDLemeniQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:TIGR03410 78 AYVPQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPKL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 639 LLLDEPTAGLDP---LSRHRIWNLLKERRaGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:TIGR03410 153 LLLDEPTEGIQPsiiKDIGRVIRRLRAEG-GMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1301-1498 |
8.30e-34 |
|
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: 130.92 E-value: 8.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgYCP------------- 1367
Cdd:cd03267 30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-----------LVPwkrrkkflrrigv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1368 ---QENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLD 1444
Cdd:cd03267 99 vfgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1445 EPSTGMDPEGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03267 179 EPTIGLDVVAQENIRNFLKE--YNRERGTtvLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
481-694 |
8.73e-34 |
|
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: 130.88 E-value: 8.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQ--DLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:cd03295 78 -GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLK--ERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1309-1448 |
1.28e-33 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 126.99 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTVKEHLE 1383
Cdd:pfam00005 2 KNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLrkeigYVFQDPQLFPRLTVRENLR 81
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1384 LYAAVKGLKKKDAVVTITRLVNALKLQD----HLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:pfam00005 82 LGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1309-1478 |
1.33e-33 |
|
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: 129.14 E-value: 1.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTVKEHLEL 1384
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRrrlaYLGHADGLKPELTVRENLRF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 YAAVKGLKKKDAvvTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:COG4133 99 WAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAA 176
|
170
....*....|....*.
gi 153792543 1465 tftNTERG--ALLTTH 1478
Cdd:COG4133 177 ---HLARGgaVLLTTH 189
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
480-694 |
1.52e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 130.56 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AV 557
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTITGVCPQsnvQFGF---LTVREN--------LRLFAKIKGILPhevEQEVQQVLQDLEMENIQDILAQ---NLSGGQK 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFP---PEDRERALEALERVGLADKAYQradQLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 624 RKLtlGIA--ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG3638 153 QRV--AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiaREDGITVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
482-695 |
1.53e-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: 128.91 E-value: 1.53e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLkkEYSGKHGKvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVltit 561
Cdd:cd03226 1 RIENI--SFSYKKGT-EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSI---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCPQ-SNVQFGFLTVRENLRLFAKikgiLPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLK----ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLK 695
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1305-1497 |
2.58e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 132.65 E-value: 2.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG----SGGGAALGFLGYCPQENVLWPNLTVKE 1380
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGvpvpARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQ 1460
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180 190
....*....|....*....|....*....|....*....
gi 153792543 1461 AIRATFTnteRGA--LLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:PRK13536 214 RLRSLLA---RGKtiLLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
481-690 |
2.93e-33 |
|
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: 129.20 E-value: 2.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMD-DSDAVLT 559
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ItGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:cd03218 77 I-GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 640 LLDEPTAGLDPLSRHRIWNL---LKERRAGRVI----VFST-QFMDEADILADRKVFIS 690
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIikiLKDRGIGVLItdhnVRETlSITDRAYIIYEGKVLAE 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
481-694 |
3.67e-33 |
|
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: 128.78 E-value: 3.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDavLTI 560
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRL--RKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGvcpqSNVQFGF----------LTVRENLRLFAKIKGILpHEVEQEVQQVLQDLEM----ENIQDILAQNLSGGQKRKL 626
Cdd:cd03257 80 RR----KEIQMVFqdpmsslnprMTIGEQIAEPLRIHGKL-SKKEARKEAVLLLLVGvglpEEVLNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
453-713 |
4.51e-33 |
|
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: 138.43 E-value: 4.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 453 VLENEIDSDPslnDSLEPVSPEFQGkeAIRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSG 532
Cdd:COG2274 451 ILDLPPEREE---GRSKLSLPRLKG--DIELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 533 LSPPTTGSVTIYNQTVSEMDdSDAVLTITGVCPQSNVQF-GflTVRENLRLFAkikgilPHEVEQEVQQVLQDLEMEniQ 611
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQID-PASLRRQIGVVLQDVFLFsG--TIRENITLGD------PDATDEEIIEAARLAGLH--D 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 612 DILA-------------QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQfmDE 678
Cdd:COG2274 593 FIEAlpmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RL 670
|
250 260 270
....*....|....*....|....*....|....*.
gi 153792543 679 ADI-LADRKVFISNGRLKCAGSSLFLKKKWGIGYHL 713
Cdd:COG2274 671 STIrLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
481-694 |
1.15e-32 |
|
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: 126.60 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLti 560
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDI-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03301 75 -AMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
480-699 |
3.87e-32 |
|
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: 126.30 E-value: 3.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLt 559
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itGVCPQSNVQFGFLTVRENLRLFAKIKGILPH----EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:cd03296 77 --GFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
481-694 |
6.39e-32 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 128.66 E-value: 6.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD---AV 557
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElraAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTItGVCPQsnvQFGFL---TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKltLGIA--I 632
Cdd:COG1135 82 RKI-GMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIAraL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
481-732 |
5.76e-31 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 124.10 E-value: 5.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYS-GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVsemdDSDAVLT 559
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDI----TAKKKKK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGF-------LTVRE-------NLrlfakikGILPHEVEQEVQQVLQDLEMEniQDILAQN---LSGGQ 622
Cdd:TIGR04521 77 LKDLRKKVGLVFQFpehqlfeETVYKdiafgpkNL-------GLSEEEAEERVKEALELVGLD--EEYLERSpfeLSGGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 623 KRKltlgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKC 696
Cdd:TIGR04521 148 MRR----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVL 223
|
250 260 270
....*....|....*....|....*....|....*...
gi 153792543 697 AGSS--LFLKKKWGIGYHLSLhlneacdPEgITSLVKK 732
Cdd:TIGR04521 224 DGTPreVFSDVDELEKIGLDV-------PE-ITELARK 253
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
480-731 |
7.97e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.81 E-value: 7.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEY-----------------SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVT 542
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 543 iynqtvsemddsdaVLtitGVCPQ----SNV-QFGF-----------LTVRENLRLFAKIKGIlPhevEQEVQQVLQDL- 605
Cdd:COG4586 81 --------------VL---GYVPFkrrkEFArRIGVvfgqrsqlwwdLPAIDSFRLLKAIYRI-P---DAEYKKRLDELv 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 606 EMENIQDILAQ---NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDeaD 680
Cdd:COG4586 140 ELLDLGELLDTpvrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMD--D 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 681 I--LADRKVFISNGRLKCAGSSLFLKKKWGIGYHLSLHLNEACDPEGITSLVK 731
Cdd:COG4586 218 IeaLCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE 270
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
484-694 |
2.24e-30 |
|
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: 119.58 E-value: 2.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYSGKHGKVEA--LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGL--SPPTTGSVTIYNQTVSEmddsDAVLT 559
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLDK----RSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFLTVRENLRLFAKIKGIlpheveqevqqvlqdlemeniqdilaqnlSGGQKRKLTLGIAILGDPQVL 639
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFST-QFMDEADILADRKVFISNGRL 694
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
495-679 |
2.71e-30 |
|
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: 119.06 E-value: 2.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 495 GKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI--------------YNQTVSE-MDDSDAVLT 559
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIdgepldysrkglleRRQRVGLvFQDPDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVcpQSNVQFGFLtvreNLrlfakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:TIGR01166 83 AADV--DQDVAFGPL----NL-------GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEA 679
Cdd:TIGR01166 150 LLDEPTAGLDPAGREQMLAILRRlRAEGMTVVISTHDVDLA 190
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1303-1497 |
3.21e-30 |
|
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: 119.49 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYC--------PQENVLwp 1374
Cdd:cd03225 12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRkvglvfqnPDDQFF-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCfVLSIL-GNPPVVLLDEPSTGMDPE 1453
Cdd:cd03225 90 GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILLLDEPTAGLDPA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153792543 1454 GQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:cd03225 169 GRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
481-690 |
4.96e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 120.13 E-value: 4.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvsemDDSDavltI 560
Cdd:COG1137 4 LEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL--------DGED----I 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 T------------GVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTL 628
Cdd:COG1137 68 ThlpmhkrarlgiGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNL---LKERRAGRVI----VFST-QFMDEADILADRKVFIS 690
Cdd:COG1137 148 ARALATNPKFILLDEPFAGVDPIAVADIQKIirhLKERGIGVLItdhnVRETlGICDRAYIISEGKVLAE 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
481-699 |
9.57e-30 |
|
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: 118.88 E-value: 9.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTvsemddsdavltI 560
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD------------I 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCP---------QSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIA 631
Cdd:cd03300 65 TNLPPhkrpvntvfQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
481-694 |
9.79e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 119.33 E-value: 9.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AVL 558
Cdd:TIGR02315 2 LEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQSNVQFGFLTVRENL---RLFAK--IKGILPHEVEQEVQQVLQDLEMENIQD---ILAQNLSGGQKRKLTLGI 630
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVlhgRLGYKptWRSLLGRFSEEDKERALSALERVGLADkayQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
479-690 |
1.40e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.58 E-value: 1.40e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVsEMDDSDavl 558
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGAD--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 tiTGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:COG4525 78 --RGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFIS 690
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
479-694 |
1.46e-29 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 119.67 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSdAVL 558
Cdd:cd03294 19 KLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRK-ELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TI----TGVCPQSnvqFGFL---TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIA 631
Cdd:cd03294 98 ELrrkkISMVFQS---FALLphrTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03294 175 LAVDPDILLMDEAFSALDPLIRREMQDELLRlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
481-694 |
1.65e-29 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 117.63 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemDDSDAVLTI 560
Cdd:cd03262 1 IEIKNLHKSFGDFH----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT--DDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 ---TGVCPQSNVQFGFLTVRENLRL-FAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDP 636
Cdd:cd03262 75 rqkVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 637 QVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
481-694 |
2.03e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 121.45 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDavLTI 560
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE--LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 T----GVCPQsnvQFGFL---TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK11153 80 ArrqiGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1304-1502 |
3.69e-29 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 116.46 E-value: 3.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---SGGGAALGFLGYCPQENVLWPNLTVKE 1380
Cdd:cd03259 12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRNIGMVFQDYALFPHLTVAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQ 1460
Cdd:cd03259 92 NIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLREELRE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 1461 AIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03259 172 ELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1303-1497 |
3.81e-29 |
|
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: 114.65 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAalgflgycpqenvlWPNLTVKEHL 1382
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--------------LPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 elyaavkglkkkdavvtitrlvnalklqdhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:cd00267 76 --------------------------------GYVPQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELL 123
|
170 180 190
....*....|....*....|....*....|....*
gi 153792543 1463 RAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:cd00267 124 RE-LAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
481-694 |
3.90e-29 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 120.64 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvsemDDSDAVLTI 560
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL--------NGRDLFTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 ------TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILG 634
Cdd:COG1118 71 pprerrVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG1118 151 EPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
481-694 |
1.11e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 115.20 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVL-- 558
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
481-693 |
1.12e-28 |
|
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: 116.13 E-value: 1.12e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AVL 558
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQS-----------NVQFGFLTVRENLRLFAkikGILPhevEQEVQQVLQDLEMENIQD---ILAQNLSGGQKR 624
Cdd:cd03256 78 RQIGMIFQQfnlierlsvleNVLSGRLGRRSTWRSLF---GLFP---KEEKQRALAALERVGLLDkayQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 625 KLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
492-694 |
1.25e-28 |
|
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: 115.45 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 492 GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPP---TTGSVTIYNQTVSemddSDAVLTITGVCPQSN 568
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRK----PDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 569 VQFGFLTVRENLRLFAKIKG--ILPHEVEQEV--QQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEP 644
Cdd:cd03234 91 ILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 645 TAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADI--LADRKVFISNGRL 694
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
481-694 |
1.27e-28 |
|
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: 113.29 E-value: 1.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemddsdavlti 560
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpqsnvqfgFLTVRENLRLfakikGIlpheveQEVQQvlqdlemeniqdilaqnLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03216 66 ------------FASPRDARRA-----GI------AMVYQ-----------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
481-695 |
1.67e-28 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 115.19 E-value: 1.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavLTI 560
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKD-----LHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGiLPhevEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:TIGR03740 72 IGSLIESPPLYENLTARENLKVHTTLLG-LP---DSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLK 695
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSfPEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
479-699 |
1.73e-28 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 116.02 E-value: 1.73e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--- 555
Cdd:PRK13548 1 AMLEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElar 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 --AVLtitgvcPQ-SNVQFGFlTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQK------RKL 626
Cdd:PRK13548 77 rrAVL------PQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE---RRAGRVIVfstqfmdeadIL---------ADRKVFISNGRL 694
Cdd:PRK13548 150 AQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQlahERGLAVIV----------VLhdlnlaaryADRIVLLHQGRL 219
|
....*
gi 153792543 695 KCAGS 699
Cdd:PRK13548 220 VADGT 224
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
510-698 |
1.82e-28 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 114.51 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGvcpQSNVQFGFLTVRENLRLfAKIKGI 589
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF---QENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 590 LPHEVEQE-VQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAG 666
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDlhAETK 179
|
170 180 190
....*....|....*....|....*....|..
gi 153792543 667 RVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03298 180 MTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
481-694 |
3.36e-28 |
|
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: 114.17 E-value: 3.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEY------------------SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVT 542
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 543 IYNQTVSemddsdaVLTITGvcpqsnvqfGF---LTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLS 619
Cdd:cd03220 81 VRGRVSS-------LLGLGG---------GFnpeLTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 620 GGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:cd03220 145 SGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
458-694 |
6.54e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 121.04 E-value: 6.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 458 IDSDPSLNDSLEPVSPEfQGKEAIRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT 537
Cdd:COG1132 318 LDEPPEIPDPPGAVPLP-PVRGEIEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 538 TGSVTIYNQTVSEMdDSDAVLTITGVCPQSNVQFGfLTVRENLRLFAkikgilPHEVEQEVQQVLQDLE-MENIQDiLAQ 616
Cdd:COG1132 394 SGRILIDGVDIRDL-TLESLRRQIGVVPQDTFLFS-GTIRENIRYGR------PDATDEEVEEAAKAAQaHEFIEA-LPD 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 617 -----------NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR-VIV----FSTqfmdead 680
Cdd:COG1132 465 gydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRtTIViahrLST------- 537
|
250
....*....|....*
gi 153792543 681 IL-ADRKVFISNGRL 694
Cdd:COG1132 538 IRnADRILVLDDGRI 552
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1301-1503 |
2.99e-27 |
|
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: 111.87 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL------GYCPQENVLWP 1374
Cdd:cd03218 9 RYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKrarlgiGYLPQEASIFR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEG 1454
Cdd:cd03218 89 KLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1455 QQQMwQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:cd03218 169 VQDI-QKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
480-699 |
3.49e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.78 E-value: 3.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT 559
Cdd:PRK13632 7 MIKVENVSFSYPN--SENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK13632 85 IGIIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFS-TQFMDEAdILADRKVFISNGRLKCAGS 699
Cdd:PRK13632 165 IFDESTSMLDPKGKREIKKIMVDlRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1307-1498 |
5.40e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 111.67 E-value: 5.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqENV--------------- 1371
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---------------RDItglpphriarlgiar 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 ------LWPNLTVKEHLEL----------YAAVKGLKK-----KDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCF 1430
Cdd:COG0411 84 tfqnprLFPELTVLENVLVaaharlgrglLAALLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1431 VLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRR--LRDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
499-670 |
7.59e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 110.98 E-value: 7.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDavltIT--GVC-----PqsNVqF 571
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHE----IArlGIGrkfqkP--TV-F 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 572 GFLTVRENLRL--------FAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDE 643
Cdd:COG4674 98 EELTVFENLELalkgdrgvFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDE 177
|
170 180
....*....|....*....|....*...
gi 153792543 644 PTAGLDPLSRHRIWNLLKERRAGR-VIV 670
Cdd:COG4674 178 PVAGMTDAETERTAELLKSLAGKHsVVV 205
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1307-1497 |
7.80e-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: 110.22 E-value: 7.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------SGGGAALGFLGYCPQENVLWPNLTVKE 1380
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGrditglPPHERARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLKKKDAvvTITRLVNAL-KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMW 1459
Cdd:cd03224 95 NLLLGAYARRRAKRKA--RLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 153792543 1460 QAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:cd03224 173 EAIR-ELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
481-694 |
8.48e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.71 E-value: 8.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKkeYSGKHGkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEmdDSDAVL-- 558
Cdd:PRK13639 2 LETRDLK--YSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY--DKKSLLev 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 --TITGVCPQSNVQFGFLTVRENLRlFAKIKGILPH-EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKltlgIAILG- 634
Cdd:PRK13639 77 rkTVGIVFQNPDDQLFAPTVEEDVA-FGPLNLGLSKeEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGi 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 635 ---DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK13639 152 lamKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
491-673 |
1.21e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 109.19 E-value: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 491 SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQtvsEMDDSDAVLTITGVCPQSNVQ 570
Cdd:PRK13539 9 ACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG---DIDDPDVAEACHYLGHRNAMK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 571 fGFLTVRENLRLFAKIKGILPHEVEqevqQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK13539 86 -PALTVAENLEFWAAFLGGEELDIA----AALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDA 160
|
170 180
....*....|....*....|....
gi 153792543 651 LSRHRIWNLLKERRA-GRVIVFST 673
Cdd:PRK13539 161 AAVALFAELIRAHLAqGGIVIAAT 184
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1298-1518 |
1.24e-26 |
|
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: 109.73 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1298 CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgYCPQENVLW---- 1373
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDG-----------KDITKKNLRelrr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 --------P-----NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCF--VLSIlgNP 1438
Cdd:COG1122 76 kvglvfqnPddqlfAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIagVLAM--EP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1439 PVVLLDEPSTGMDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLLE 1518
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV---FSDYELLE 229
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
480-698 |
1.79e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 110.98 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgKHGkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSE--------- 550
Cdd:PRK13647 4 IIEVEDLHFRY--KDG-TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAenekwvrsk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 551 -----MDDSDAVLTITgvcPQSNVQFGFLtvreNLRLFAKikgilphEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRK 625
Cdd:PRK13647 81 vglvfQDPDDQVFSST---VWDDVAFGPV----NMGLDKD-------EVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 626 ltlgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:PRK13647 147 ----VAIAGvlamDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
505-699 |
1.87e-26 |
|
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: 112.89 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemdDSDAVLTI------TGVCPQSNVQFGFLTVRE 578
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ---DSARGIFLpphrrrIGYVFQEARLFPHLSVRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 579 NLRlFAkIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN 658
Cdd:COG4148 97 NLL-YG-RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153792543 659 LLkERRAGRV---IVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:COG4148 175 YL-ERLRDELdipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
505-679 |
2.38e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 117.53 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVsemDDSD-AVLTITGVCPQSNVQFGFLTVRENLRLF 583
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPV---DAGDiATRRRVGYMSQAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 584 AKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE- 662
Cdd:NF033858 364 ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIEl 443
|
170
....*....|....*...
gi 153792543 663 -RRAGRVIVFSTQFMDEA 679
Cdd:NF033858 444 sREDGVTIFISTHFMNEA 461
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
505-698 |
2.50e-26 |
|
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: 108.54 E-value: 2.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIyEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIyNQTVseMDDSDAVLTIT------GVCPQSNVQFGFLTVRE 578
Cdd:cd03297 19 FDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTV--LFDSRKKINLPpqqrkiGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 579 NLrLFAkIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN 658
Cdd:cd03297 95 NL-AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 659 LLKERRA--GRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03297 173 ELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1307-1498 |
2.66e-26 |
|
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: 109.06 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycPQE------------NVLWP 1374
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP------PHEiarlgigrtfqiPRLFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELyAAVKGLK-----------KKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLL 1443
Cdd:cd03219 89 ELTVLENVMV-AAQARTGsglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1444 DEPSTGMDPEGQQQMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03219 168 DEPAAGLNPEETEELAELIREL---RERGItvLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
488-702 |
3.01e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 109.20 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 488 KEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGVCPQS 567
Cdd:PRK11614 9 DKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 568 NVQFGFLTVRENLRL---FA----------KIKGILPHEVEQEVQQvlqdlemeniqdilAQNLSGGQKRKLTLGIAILG 634
Cdd:PRK11614 89 RRVFSRMTVEENLAMggfFAerdqfqerikWVYELFPRLHERRIQR--------------AGTMSGGEQQMLAIGRALMS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGR--LKCAGSSLF 702
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
480-687 |
4.36e-26 |
|
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: 114.69 E-value: 4.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT 559
Cdd:TIGR02857 321 SLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVcPQSNVQF-GflTVRENLRLFAkiKGILPHEVEQEVQQV-----LQDLEmENIQDILAQN---LSGGQKRKLTLGI 630
Cdd:TIGR02857 398 IAWV-PQHPFLFaG--TIAENIRLAR--PDASDAEIREALERAgldefVAALP-QGLDTPIGEGgagLSGGQAQRLALAR 471
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQfmDEADI-LADRKV 687
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaLADRIV 527
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
500-692 |
5.02e-26 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 108.32 E-value: 5.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTitgvcpQSNVQFGFLTVREN 579
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVF------QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LRLfaKIKGILPHEVEQEVQQVLQD-LEMENI---QDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRH- 654
Cdd:TIGR01184 75 IAL--AVDRVLPDLSKSERRAIVEEhIALVGLteaADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGn 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153792543 655 ------RIWNllkerRAGRVIVFSTQFMDEADILADRKVFISNG 692
Cdd:TIGR01184 153 lqeelmQIWE-----EHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
481-693 |
8.61e-26 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 107.53 E-value: 8.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvealrgLGFD--IYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--- 555
Cdd:COG3840 2 LRLDDLTYRYGDFP--------LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAErpv 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 AVLTitgvcpQSNVQFGFLTVRENLRLfakikGILPH-----EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGI 630
Cdd:COG3840 74 SMLF------QENNLFPHLTVAQNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
481-665 |
8.89e-26 |
|
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: 110.14 E-value: 8.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPP---TTGSVTIYNQTVSEMDDSDaV 557
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE-L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTITGvcpqSNVQFGF----------LTVRENLRLFAKIKGILPH-EVEQEVQQVLQDLEMENIQDILAQ---NLSGGQK 623
Cdd:COG0444 81 RKIRG----REIQMIFqdpmtslnpvMTVGDQIAEPLRIHGGLSKaEARERAIELLERVGLPDPERRLDRyphELSGGMR 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 624 RKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA 665
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQR 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
472-694 |
1.52e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.43 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 472 SPEFQGKEAIRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTL-------SGLSppTTGSVTIY 544
Cdd:COG1117 3 APASTLEPKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmndliPGAR--VEGEILLD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 545 NQTVSEmDDSDAVL---TITGVCPQSNVqfgF-LTVRENLRLFAKIKGILP-HEVEQEVQQVLQDLEM-ENIQDIL---A 615
Cdd:COG1117 77 GEDIYD-PDVDVVElrrRVGMVFQKPNP---FpKSIYDNVAYGLRLHGIKSkSELDEIVEESLRKAALwDEVKDRLkksA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 616 QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNL---LKERRAgrvIVFSTQFMDEADILADRKVFISNG 692
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELileLKKDYT---IVIVTHNMQQAARVSDYTAFFYLG 229
|
..
gi 153792543 693 RL 694
Cdd:COG1117 230 EL 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
477-694 |
1.57e-25 |
|
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: 105.21 E-value: 1.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 477 GKEAIRIKNLkkeySGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDA 556
Cdd:cd03215 1 GEPVLEVRGL----SVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 557 VLTitGVcpqsnvqfGFLTvrENlRlfaKIKGILPhevEQEVqqvlqdleMENIqdILAQNLSGGQKRKLTLGIAILGDP 636
Cdd:cd03215 73 IRA--GI--------AYVP--ED-R---KREGLVL---DLSV--------AENI--ALSSLLSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 637 QVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGR-VIVFSTQfMDEADILADRKVFISNGRL 694
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRElADAGKaVLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
496-694 |
1.74e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 106.13 E-value: 1.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 496 KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTItGVCPQSNVQFgFLT 575
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI-GYVPQDVTLF-YGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 576 VRENLRLFAkikgilPHEVEQEVqqvLQDLEMENIQDILA--------------QNLSGGQKRKLTLGIAILGDPQVLLL 641
Cdd:cd03245 94 LRDNITLGA------PLADDERI---LRAAELAGVTDFVNkhpngldlqigergRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 642 DEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADiLADRKVFISNGRL 694
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
480-694 |
2.58e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 106.64 E-value: 2.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQtvsEMDDSDAVLT 559
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGN---HFDFSKTPSD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGF--------LTVRENL-RLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGI 630
Cdd:PRK11124 75 KAIRELRRNVGMVFqqynlwphLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAG--RVIVfsTQFMDEADILADRKVFISNGRL 694
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGitQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1303-1497 |
3.65e-25 |
|
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: 103.81 E-value: 3.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-------YCPQENVLWPN 1375
Cdd:cd03229 11 GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplrrrigMVFQDFALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 LTVKEHLELyaavkglkkkdavvtitrlvnalklqdhlkalvrTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03229 91 LTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITR 136
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 1456 QQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:cd03229 137 REVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
480-685 |
3.78e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 111.26 E-value: 3.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDA--- 556
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAqaa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 557 -VLTItgvcPQSNVQFGFLTVRENLRL--FAKIKGILPH-EVEQEVQQVLQDLEMeNIQ-DILAQNLSGGQKRKLTLGIA 631
Cdd:COG1129 80 gIAII----HQELNLVPNLSVAENIFLgrEPRRGGLIDWrAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADR 685
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEIADR 209
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
481-650 |
4.20e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.85 E-value: 4.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemDDSDAVLTI 560
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT--DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 ---TGVCPQS-NVqFGFLTVRENLRLfA--KIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQK-RkltlgIAI- 632
Cdd:COG1126 76 rrkVGMVFQQfNL-FPHLTVLENVTL-ApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqR-----VAIa 148
|
170 180
....*....|....*....|.
gi 153792543 633 --LG-DPQVLLLDEPTAGLDP 650
Cdd:COG1126 149 raLAmEPKVMLFDEPTSALDP 169
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
476-699 |
4.61e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 109.27 E-value: 4.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 476 QGKEAIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVS----EM 551
Cdd:PRK09452 10 SLSPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvpaEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 552 DDSDAVLtitgvcpQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIA 631
Cdd:PRK09452 86 RHVNTVF-------QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--ERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1289-1504 |
6.89e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 105.16 E-value: 6.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1289 KEYIGRTKRcfSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgflgycpq 1368
Cdd:COG1134 25 KELLLRRRR--TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-------------- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1369 enVLW---------PNLTVKEHLELYAAVKGLKKKDavvtITRLVNALK----LQDHLKALVRTLSEGVKRKLCFVLSIL 1435
Cdd:COG1134 89 --VSAllelgagfhPELTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVKTYSSGMRARLAFAVATA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1436 GNPPVVLLDEP-STGmDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1504
Cdd:COG1134 163 VDPDILLVDEVlAVG-DAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
473-694 |
1.18e-24 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 111.50 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 473 PEFQGKeaIRIKNLKKEYSGKhgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMD 552
Cdd:TIGR03375 458 PRLQGE--IEFRNVSFAYPGQ--ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 DSDAVLTItGVCPQSNVQFgFLTVRENLRLFAkikgilPHEVEQEVQQVLQDLEMENIQDILAQ-----------NLSGG 621
Cdd:TIGR03375 534 PADLRRNI-GYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGG 605
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 622 QKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFST---QFMDeadiLADRKVFISNGRL 694
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGRI 677
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
510-695 |
1.95e-24 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 103.02 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGvcpQSNVQFGFLTVRENLRLFAKIKGI 589
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLF---QENNLFAHLTVRQNIGLGLHPGLK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 590 LPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGR 667
Cdd:TIGR01277 101 LNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQlcSERQR 180
|
170 180
....*....|....*....|....*...
gi 153792543 668 VIVFSTQFMDEADILADRKVFISNGRLK 695
Cdd:TIGR01277 181 TLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
480-680 |
2.10e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 111.37 E-value: 2.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT 559
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQsnvqfGF-------LTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAI 632
Cdd:NF033858 77 RIAYMPQ-----GLgknlyptLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR----VIVfSTQFMDEAD 680
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmsVLV-ATAYMEEAE 202
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1301-1502 |
2.51e-24 |
|
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: 103.00 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqeNVLW------- 1373
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------------RVSSllglggg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 --PNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP-STGm 1450
Cdd:cd03220 95 fnPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG- 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1451 DPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03220 174 DAAFQEKCQRRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
481-650 |
2.66e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 104.01 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKE-YSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT 559
Cdd:COG1101 2 LELKNLSKTfNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 I--------TGVCPQsnvqfgfLTVRENLRLfAKIKGI-------LPHEVEQEVQQVLQDLEM--ENIQDILAQNLSGGQ 622
Cdd:COG1101 82 IgrvfqdpmMGTAPS-------MTIEENLAL-AYRRGKrrglrrgLTKKRRELFRELLATLGLglENRLDTKVGLLSGGQ 153
|
170 180
....*....|....*....|....*...
gi 153792543 623 KRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1307-1498 |
2.99e-24 |
|
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: 102.97 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG--------YCPQE--NVLWPNL 1376
Cdd:cd03257 20 ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirrkeiqMVFQDpmSSLNPRM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLE--LYAAVKGLKKKDAVVTITRLVNALKL-QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:cd03257 100 TIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALDVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03257 180 VQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
481-698 |
3.08e-24 |
|
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: 103.18 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEM--DDSDavl 558
Cdd:cd03299 1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKRD--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 tiTGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:cd03299 73 --ISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
479-699 |
3.17e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.24 E-value: 3.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEY------------------SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGS 540
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 541 VTIyNQTVSemddsdAVLTITGvcpqsnvqfGF---LTVRENLRLFAKIKGILPHEVEqevqqvlqdlemENIQDILA-- 615
Cdd:COG1134 83 VEV-NGRVS------ALLELGA---------GFhpeLTGRENIYLNGRLLGLSRKEID------------EKFDEIVEfa 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 616 ----------QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILAD 684
Cdd:COG1134 135 elgdfidqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELREsGRTVIFVSHSMGAVRRLCD 214
|
250
....*....|....*
gi 153792543 685 RKVFISNGRLKCAGS 699
Cdd:COG1134 215 RAIWLEKGRLVMDGD 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
481-694 |
3.75e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 3.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGL-----SPPTTGSVTIYNQTVSEMDDSD 555
Cdd:PRK14247 4 IEIRDLKVSF----GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 ------AVLTITGVCPQsnvqfgfLTVRENLRLFAKIKGILPH--EVEQEVQQVLQDLEM-ENIQDIL---AQNLSGGQK 623
Cdd:PRK14247 80 lrrrvqMVFQIPNPIPN-------LSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 624 RKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK14247 153 QRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
498-715 |
3.94e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.48 E-value: 3.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 498 EALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI---TGVC---PQSnvQF 571
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVrkrIGMVfqfPES--QL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 572 GFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMEniQDILAQN---LSGGQKRKLTLgIAILG-DPQVLLLDEPTAG 647
Cdd:PRK13646 99 FEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAI-VSILAmNPDIIVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 648 LDPLSRHRIWNLLKERRA--GRVIVFSTQFMDEADILADRKVFISNGRL--KCAGSSLFLKKKWGIGYHLSL 715
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHIGL 247
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
442-673 |
6.92e-24 |
|
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: 107.83 E-value: 6.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 442 YWFKRRGASHVVLENEIDSDPSLNDSLEPVSPEFQGKEAIRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGA 521
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGS 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 522 GKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTItGVCPQSNVQFGfLTVRENLRLFAkikgilPHEVEQEVQQV 601
Cdd:TIGR02868 373 GKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRV-SVCAQDAHLFD-TTVRENLRLAR------PDATDEELWAA 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 602 LQDLEMENIQDIL-----------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIV 670
Cdd:TIGR02868 445 LERVGLADWLRALpdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVV 524
|
...
gi 153792543 671 FST 673
Cdd:TIGR02868 525 LIT 527
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1280-1503 |
7.04e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.03 E-value: 7.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1280 PVIIASCLRKEYigrtkrcfskmKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------ 1353
Cdd:COG1137 2 MTLEAENLVKSY-----------GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGedithl 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1354 ----------SgggaalgflgYCPQENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEG 1423
Cdd:COG1137 71 pmhkrarlgiG----------YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1424 VKRKLCFVLSILGNPPVVLLDEPSTGMDP---EGQQQMWQAIRatftntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG1137 141 ERRRVEIARALATNPKFILLDEPFAGVDPiavADIQKIIRHLK------ERGIgvLITDHNVRETLGICDRAYIISEGKV 214
|
....*
gi 153792543 1499 RCIGS 1503
Cdd:COG1137 215 LAEGT 219
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
480-694 |
7.26e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQtvsEMDDSDAVLT 559
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGH---QFDFSQKPSE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGF--------LTVRENLrLFAKIK--GILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:COG4161 75 KAIRLLRQKVGMVFqqynlwphLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA---GRVIVfsTQFMDEADILADRKVFISNGRL 694
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtgiTQVIV--THEVEFARKVASQVVYMEKGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1295-1497 |
8.32e-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: 101.39 E-value: 8.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1295 TKRCFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENVLWP 1374
Cdd:cd03293 7 SKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGYVFQQDALLP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEG 1454
Cdd:cd03293 87 WLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPFSALDALT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 1455 QQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMvSGR 1497
Cdd:cd03293 167 REQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL-SAR 208
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
481-705 |
1.07e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 101.53 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSdAVLTI 560
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQF-GflTVRENLRLFakiKGILPHEVEQEVQQVLQ-DLEMENIQDIL-------AQNLSGGQKRKLTLGIA 631
Cdd:cd03254 79 IGVVLQDTFLFsG--TIMENIRLG---RPNATDEEVIEAAKEAGaHDFIMKLPNGYdtvlgenGGNLSQGERQLLAIARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR-VIV----FSTqfmdeadIL-ADRKVFISNGRLKCAGS--SLFL 703
Cdd:cd03254 154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRtSIIiahrLST-------IKnADKILVLDDGKIIEEGThdELLA 226
|
..
gi 153792543 704 KK 705
Cdd:cd03254 227 KK 228
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1308-1502 |
1.75e-23 |
|
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: 100.45 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1308 TRNISFCVKkGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCP---------QENVLWPNLTV 1378
Cdd:cd03297 14 TLKIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPqqrkiglvfQQYALFPHLNV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELyaavkGLKKK-DAVVTI--TRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03297 93 RENLAF-----GLKRKrNREDRIsvDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1456 QQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03297 168 LQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
484-699 |
1.80e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 101.12 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGV 563
Cdd:PRK10895 7 KNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 564 CPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQE-VQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLD 642
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 643 EPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1309-1503 |
1.93e-23 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 101.27 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTVKE--- 1380
Cdd:COG1120 18 DDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELarriaYVPQEPPAPFGLTVRElva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 -----HLELYAavkGLKKKD--AVVTITRLVNALKLQDHlkaLVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:COG1120 98 lgrypHLGLFG---RPSAEDreAVEEALERTGLEHLADR---PVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:COG1120 172 HQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
477-699 |
3.49e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.32 E-value: 3.49e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 477 GKEAIRIKNLKKEYSGKHGKVE--ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMD-- 552
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 --------------DSDAVLTITgvcpQSNVQFGfltvRENLrlfakikGILPHEVEQEVQQVLQDLEMENIQDILAQNL 618
Cdd:PRK13633 81 wdirnkagmvfqnpDNQIVATIV----EEDVAFG----PENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 619 SGGQKRKltlgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEAdILADRKVFISNG 692
Cdd:PRK13633 146 SGGQKQR----VAIAGilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSG 220
|
....*..
gi 153792543 693 RLKCAGS 699
Cdd:PRK13633 221 KVVMEGT 227
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
480-699 |
3.56e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 103.24 E-value: 3.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLt 559
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKV- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itGVCPQSNVQFGFLTVREN----LRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:PRK10851 77 --GFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 636 PQVLLLDEPTAGLDPLSRhriwnllKE-RRAGRVI--------VFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK10851 155 PQILLLDEPFGALDAQVR-------KElRRWLRQLheelkftsVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1279-1507 |
3.62e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 105.37 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1279 KPVIIASCLRKEYIGRTKRcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTA---GQVFLKGSG 1355
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVP---------AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1356 GGAALGFLG-----YCPQE--NVLWPnLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKL 1428
Cdd:COG1123 73 LLELSEALRgrrigMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1429 CFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
478-694 |
3.68e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.62 E-value: 3.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTL---INTLSGLSP--PTTGSVT-----IYNQT 547
Cdd:PRK14239 3 EPILQVSDLSVYY----NKKKALNSVSLDFYPNEITALIGPSGSGKSTLlrsINRMNDLNPevTITGSIVynghnIYSPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 548 VsemDDSDAVLTITGVCPQSNvQFGFlTVRENLRLFAKIKGILPHEV-EQEVQQVLQDLEM-ENIQDIL---AQNLSGGQ 622
Cdd:PRK14239 79 T---DTVDLRKEIGMVFQQPN-PFPM-SIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwDEVKDRLhdsALGLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 623 KRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
479-698 |
4.85e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.16 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTG-SVTIYNQT---------- 547
Cdd:COG1119 2 PLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggedvwelr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 548 -----VS-EMDDS--------DAVLTitgvcpqsnvqfGFltvrenlrlFAKIkGILPH---EVEQEVQQVLQDLEMENI 610
Cdd:COG1119 78 kriglVSpALQLRfprdetvlDVVLS------------GF---------FDSI-GLYREptdEQRERARELLELLGLAHL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 611 QDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEadILA--DRK 686
Cdd:COG1119 136 ADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHV 213
|
250
....*....|..
gi 153792543 687 VFISNGRLKCAG 698
Cdd:COG1119 214 LLLKDGRVVAAG 225
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
505-699 |
4.96e-23 |
|
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: 102.50 E-value: 4.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTvseMDDSDAVLTIT------GVCPQSNVQFGFLTVRE 578
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRT---LFDSRKGIFLPpekrriGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 579 NLRLfaKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN 658
Cdd:TIGR02142 95 NLRY--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 659 LLKERRA--GRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:TIGR02142 173 YLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
478-698 |
5.20e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 100.86 E-value: 5.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYsgKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV 557
Cdd:PRK13635 3 EEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTITGVCPQSNVQFGFLTVRENLRLFAKIKGIlPHEVEQE-VQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDP 636
Cdd:PRK13635 81 RQVGMVFQNPDNQFVGATVQDDVAFGLENIGV-PREEMVErVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 637 QVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFS-TQFMDEAdILADRKVFISNGRLKCAG 698
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQlKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEG 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1304-1506 |
6.31e-23 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 99.78 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQ-ENVLW--PnLTVKE 1380
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRRIGYVPQrAEVDWdfP-ITVRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 --HLELYAAV---KGLKKKD--AVVTITRLVNALKLQDHlkaLVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:COG1121 97 vvLMGRYGRRglfRRPSRADreAVDEALERVGLEDLADR---PIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1454 GQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIGSIQH 1506
Cdd:COG1121 174 TEEALYELLRE-LRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1305-1502 |
6.75e-23 |
|
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: 98.76 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQ-ENVLW--PnLTVKE- 1380
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRIGYVPQrRSIDRdfP-ISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 -------HLELYaavKGLKKKD-AVVTitrlvNALK---LQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:cd03235 91 vlmglygHKGLF---RRLSKADkAKVD-----EALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1450 MDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVaIMVSGRLRCIG 1502
Cdd:cd03235 163 VDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1303-1498 |
7.57e-23 |
|
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: 98.72 E-value: 7.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG---------YCPQENVLW 1373
Cdd:cd03255 15 EKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafrrrhigFVFQSFNLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:cd03255 95 PDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1454 GQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAvCDRVAIMVSGRL 1498
Cdd:cd03255 175 TGKEVMELLRE--LNKEAGTtiVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
480-714 |
7.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 7.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYS-GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVL 558
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TI---TGVCPQ-SNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEM-ENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK13641 82 KLrkkVSLVFQfPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL--KCAGSSLFLKKKWGIG 710
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEWLKK 241
|
....
gi 153792543 711 YHLS 714
Cdd:PRK13641 242 HYLD 245
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
507-715 |
8.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 100.48 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 507 IYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI---TGVC---PQSnvQFGFLTVRENL 580
Cdd:PRK13634 30 IPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLrkkVGIVfqfPEH--QLFEETVEKDI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 581 RLFAKIKGILPHEVEQEVQQVLQDLEMEniQDILAQN---LSGGQKRKltlgIAILG----DPQVLLLDEPTAGLDPLSR 653
Cdd:PRK13634 108 CFGPMNFGVSEEDAKQKAREMIELVGLP--EELLARSpfeLSGGQMRR----VAIAGvlamEPEVLVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 654 HRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS--SLFLKKKWGIGYHLSL 715
Cdd:PRK13634 182 KEMMEMFYKlhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEAIGLDL 247
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
477-695 |
9.30e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 104.38 E-value: 9.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 477 GKEAIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIyNQTVSemddsda 556
Cdd:COG0488 312 GKKVLELEGLSKSYGDK----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 557 vltiTGVCPQSNVQFgfltvRENLRLFAKIKGILPHEVEQEVQQVLQDL----EMeniQDILAQNLSGGQKRKLTLGIAI 632
Cdd:COG0488 380 ----IGYFDQHQEEL-----DPDKTVLDELRDGAPGGTEQEVRGYLGRFlfsgDD---AFKPVGVLSGGEKARLALAKLL 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKErRAGRVIVFS--TQFMDEadiLADRKVFISNGRLK 695
Cdd:COG0488 448 LSPPNVLLLDEPTNHLDIETLEALEEALDD-FPGTVLLVShdRYFLDR---VATRILEFEDGGVR 508
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
481-758 |
1.68e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 99.74 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEY-SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvSEMDDSDAVLT 559
Cdd:PRK13637 3 IKIENLTHIYmEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII-----DGVDITDKKVK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFL-------TVRENLRLFAKIKGILPHEVEQEVQQVLQ--DLEMENIQDILAQNLSGGQKRKLTLGI 630
Cdd:PRK13637 78 LSDIRKKVGLVFQYPeyqlfeeTIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG--SSLFLK-- 704
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKElhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGtpREVFKEve 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 705 --KKWGIGYhlslhlneacdPEgITSLVKK------HISDARLTTqsEERLVYILPLERTNK 758
Cdd:PRK13637 238 tlESIGLAV-----------PQ-VTYLVRKlrkkgfNIPDDIFTI--EEAKEEILKYLRGEK 285
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
481-719 |
1.97e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 99.15 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYS-GKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSE-----MDDS 554
Cdd:PRK13636 6 LKVEELNYNYSdGTH----ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkglMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 DAVltitGVCPQS-NVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK13636 82 ESV----GMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG--SSLFLKKKWGI 709
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLR 237
|
250
....*....|....
gi 153792543 710 GYHLSL----HLNE 719
Cdd:PRK13636 238 KVNLRLprigHLME 251
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
515-700 |
2.02e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 100.26 E-value: 2.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 515 LLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdAVLTITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEV 594
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP---PHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 595 EQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--ERRAGRVIVFS 672
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 153792543 673 TQFMDEADILADRKVFISNGRLKCAGSS 700
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
481-699 |
2.03e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.11 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK13652 4 IETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDlpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
480-694 |
4.64e-22 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.13 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVsemDDSDAVLT 559
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI---DTARSLSQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFltVRENLRLFAK-------------IKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKL 626
Cdd:PRK11264 76 QKGLIRQLRQHVGF--VFQNFNLFPHrtvleniiegpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDP------LSRHRiwNLLKERRAgRVIVfsTQFMDEADILADRKVFISNGRL 694
Cdd:PRK11264 154 AIARALAMRPEVILFDEPTSALDPelvgevLNTIR--QLAQEKRT-MVIV--THEMSFARDVADRAIFMDQGRI 222
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
480-692 |
6.07e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMD-DSDAVL 558
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGaERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQSNVQfgfltvrENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:PRK11248 77 QNEGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNG 692
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1309-1497 |
6.23e-22 |
|
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: 96.59 E-value: 6.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG------YCPQENVLWPNLTVKEHL 1382
Cdd:COG0410 20 HGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIarlgigYVPEGRRIFPSLTVEENL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELyaAVKGLKKKDAVVTITRLVNAL--KLQDHLKALVRTLSEGVKRklcfVLSI----LGNPPVVLLDEPSTGMDPEGQQ 1456
Cdd:COG0410 100 LL--GAYARRDRAEVRADLERVYELfpRLKERRRQRAGTLSGGEQQ----MLAIgralMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 1457 QMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:COG0410 174 EIFEIIRRL---NREGVtiLLVEQNARFALEIADRAYVLERGR 213
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
481-670 |
6.48e-22 |
|
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: 94.59 E-value: 6.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavlti 560
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpqsnvqfgfltvRENLRlfaKIKGILPHEVEqevqqVLQDLEMENIqdilaqnLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03246 71 ----------------PNELG---DHVGYLPQDDE-----LFSGSIAENI-------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190
....*....|....*....|....*....|...
gi 153792543 641 LDEPTAGLDPLSRHRIWNL---LKERRAGRVIV 670
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAiaaLKAAGATRIVI 152
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
481-699 |
8.24e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 96.62 E-value: 8.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK11231 3 LRTENLTVGY----GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TgVCPQSNVQFGFLTVRE--------NLRLFakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAI 632
Cdd:PRK11231 79 A-LLPQHHLTPEGITVRElvaygrspWLSLW----GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 633 LGDPQVLLLDEPTAGLDpLSRH-RIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1307-1498 |
9.29e-22 |
|
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: 93.65 E-value: 9.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgflgycpqenvlwpnltvkehlelya 1386
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 AVKGLKKKDAvvtitrlvnalklQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATf 1466
Cdd:cd03216 63 EVSFASPRDA-------------RRAGIAMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL- 128
|
170 180 190
....*....|....*....|....*....|....
gi 153792543 1467 tnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03216 129 --RAQGVavIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1307-1503 |
1.15e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.63 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAAlgflgycP----------QENVLWPNL 1376
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-------PpekrnvgmvfQDYALFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEG-----------VKRklcfvlsilgnPPVVLLDE 1445
Cdd:COG3842 93 TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvalaralAPE-----------PRVLLLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1446 PSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
480-688 |
1.31e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSP-----PTTGSVTIYNQTVSE--MD 552
Cdd:PRK14258 7 AIKVNNLSFYYDTQ----KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYErrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 DSDAVLTITGVCPQSNVqfgF-LTVRENLRLFAKIKGILPH-EVEQEVQQVLQDLEM-ENIQDIL---AQNLSGGQKRKL 626
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNL---FpMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwDEIKHKIhksALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKER--RAGRVIVFSTQFMDEADILADRKVF 688
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAF 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
481-693 |
1.40e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 98.75 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkveALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK11607 20 LEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGvcpQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK11607 96 MF---QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 641 LDEPTAGLDPLSRHR----IWNLLKerRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK11607 173 LDEPMGALDKKLRDRmqleVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
499-699 |
1.49e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 96.74 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTV---SEMDDSDAVLTITGVC---PQSnvQFG 572
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVfqfPES--QLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 573 FLTVRENLRLFAKIKGILPHEVEqevQQVLQDLEMENI-QDILAQN---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:PRK13649 100 EETVLKDVAFGPQNFGVSQEEAE---ALAREKLALVGIsESLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 649 DPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK13649 177 DPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
484-670 |
1.57e-21 |
|
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: 93.85 E-value: 1.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSppTTGSVTiYNQTVSEMDDSDAVLTITGV 563
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRK--TAGVIT-GEILINGRPLDKNFQRSTGY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 564 CPQSNVQFGFLTVRENLRLFAKIKGilpheveqevqqvlqdlemeniqdilaqnLSGGQKRKLTLGIAILGDPQVLLLDE 643
Cdd:cd03232 84 VEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDE 134
|
170 180
....*....|....*....|....*...
gi 153792543 644 PTAGLDPLSRHRIWNLLKE-RRAGRVIV 670
Cdd:cd03232 135 PTSGLDSQAAYNIVRFLKKlADSGQAIL 162
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
488-673 |
1.69e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 94.10 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 488 KEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVlTITGVCPQS 567
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIAR-GLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 568 NVQfGFLTVRENLRLFAKIkgilpHEVEQeVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 647
Cdd:cd03231 83 GIK-TTLSVLENLRFWHAD-----HSDEQ-VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*..
gi 153792543 648 LDPLSRHRIWNLLKER-RAGRVIVFST 673
Cdd:cd03231 156 LDKAGVARFAEAMAGHcARGGMVVLTT 182
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1303-1502 |
2.01e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 94.24 E-value: 2.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP---------QENVLW 1373
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP------PkdrdiamvfQNYALY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:cd03301 85 PHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAK 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03301 165 LRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
481-698 |
2.43e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.86 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK09700 6 ISMAGIGKSFGP----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENL---RLFAK----IKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1303-1507 |
2.57e-21 |
|
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: 94.57 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF--------LKGSGGGAALGFLGYCPQE-NVLW 1373
Cdd:cd03258 16 GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLvdgtdltlLSGKELRKARRRIGMIFQHfNLLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 pNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:cd03258 96 -SRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1454 GQQQMWQAIRAtfTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:cd03258 175 TTQSILALLRD--INRELGltIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
507-693 |
2.79e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.51 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 507 IYEGQITALLGHSGAGKTTLINTLSGLSPPTT---GSVTIYNQTVsemdDSDAVLTITGVCPQSNVQFGFLTVRENLRLF 583
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 584 A--KIKGILPHEVEQE-VQQVLQDLEMENIQDILAQ------NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRH 654
Cdd:TIGR00955 124 AhlRMPRRVTKKEKRErVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153792543 655 RIWNLLKERRAGRVIVFSTQFMDEADI--LADRKVFISNGR 693
Cdd:TIGR00955 204 SVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGR 244
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
480-694 |
4.29e-21 |
|
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: 94.04 E-value: 4.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDsDAVLT 559
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE-DARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGvcpqSNVQFGF--------LTVRENLRLFAKIKGIlpHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIA 631
Cdd:COG4181 87 LRA----RHVGFVFqsfqllptLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 632 ILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQfmDEAdiLA---DRKVFISNGRL 694
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTH--DPA--LAarcDRVLRLRAGRL 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
495-650 |
4.77e-21 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.81 E-value: 4.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 495 GKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDS--DAVLTI---TGVCPQsnv 569
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEphENILYLghlPGLKPE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 570 qfgfLTVRENLRLFAKIKGILPHEVEQEVQQV-LQDLEmeniqDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:TIGR01189 88 ----LSALENLHFWAAIHGGAQRTIEDALAAVgLTGFE-----DLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTAL 158
|
..
gi 153792543 649 DP 650
Cdd:TIGR01189 159 DK 160
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1309-1516 |
4.81e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 93.94 E-value: 4.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---SGGGAALGFLGYCPQENVLWPNLTVKEHLELY 1385
Cdd:cd03299 16 KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGkdiTNLPPEKRDISYVPQNYALFPHMTVYKNIAYG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1386 AAVKGLKKKD---AVVTITRLVNAlklqDH-LKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQA 1461
Cdd:cd03299 96 LKKRKVDKKEierKVLEIAEMLGI----DHlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1462 IRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ----HLKSKFGKDYL 1516
Cdd:cd03299 172 LKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
476-694 |
6.30e-21 |
|
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: 98.72 E-value: 6.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 476 QGKEAIRIKNLKKEY-SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI------YNQTV 548
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewVDMTK 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 549 SEMDDSDAVLTITGVCPQSNVQFGFLTVRENL---------RLFAKIKGILPHEVEQevqqvLQDLEMENIQDILAQNLS 619
Cdd:TIGR03269 355 PGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLteaiglelpDELARMKAVITLKMVG-----FDEEKAEEILDKYPDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 620 GGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN-LLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
499-687 |
7.04e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 7.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI-------YNQTVSEMDDSdavltitgvCPqsnvqf 571
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRaggarvaYVPQRSEVPDS---------LP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 572 gfLTVRE--NLRLFAKIKGILPH------EVEQEVQQV-LQDLEMENIQDilaqnLSGGQKRKLTLGIAILGDPQVLLLD 642
Cdd:NF040873 72 --LTVRDlvAMGRWARRGLWRRLtrddraAVDDALERVgLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 643 EPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEAdILADRKV 687
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELV-RRADPCV 189
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
499-739 |
1.07e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.42 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI---TGVC---PQSnvQFG 572
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVrkkVGVVfqfPES--QLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 573 FLTVRENLRLFAKIKGILPHEVEQEVQQvlqDLEMENIQDILAQN----LSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:PRK13643 99 EETVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 649 DPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG--SSLFLK----KKWGIGYHLSLHLNEAC 721
Cdd:PRK13643 176 DPKARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVFQEvdflKAHELGVPKATHFADQL 255
|
250
....*....|....*...
gi 153792543 722 DPEGITSLVKKHISDARL 739
Cdd:PRK13643 256 QKTGAVTFEKLPITRAEL 273
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
481-713 |
1.48e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 92.29 E-value: 1.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQSNVQFGFlTVRENLRlFAKiKGILPHEVEQEVQQV-LQDLEM---ENIQDILAQN---LSGGQKRKLTLGIAIL 633
Cdd:cd03251 79 -GLVSQDVFLFND-TVAENIA-YGR-PGATREEVEEAARAAnAHEFIMelpEGYDTVIGERgvkLSGGQRQRIAIARALL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR-VIV----FSTqFMDeadilADRKVFISNGRLKCAGSSLFLKKKWG 708
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERLMKNRtTFViahrLST-IEN-----ADRIVVLEDGKIVERGTHEELLAQGG 228
|
....*
gi 153792543 709 IGYHL 713
Cdd:cd03251 229 VYAKL 233
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
505-694 |
1.60e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 92.34 E-value: 1.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGvcpQSNVQFGFLTVRENLRLfa 584
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLF---QENNLFSHLTVAQNIGL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 585 kikGILP-----HEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNL 659
Cdd:PRK10771 95 ---GLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 153792543 660 LKE---RRAGRVIVFSTQFMDEADIlADRKVFISNGRL 694
Cdd:PRK10771 172 VSQvcqERQLTLLMVSHSLEDAARI-APRSLVVADGRI 208
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
480-699 |
1.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 93.71 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPP--------TTGSVTIYNQTVSEM 551
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnpnskiTVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 552 DDSdavltiTGVCPQS-NVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTL-G 629
Cdd:PRK13640 83 REK------VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaG 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 630 IAILGdPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFS-TQFMDEADiLADRKVFISNGRLKCAGS 699
Cdd:PRK13640 157 ILAVE-PKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
481-698 |
1.71e-20 |
|
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: 90.45 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDD--SDAVl 558
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKalSSLI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 titGVCPQSNVQFGfLTVRENLrlfakikgilpheveqevqqvlqdlemeniqdilAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:cd03247 78 ---SVLNQRPYLFD-TTLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPI 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADiLADRKVFISNGRLKCAG 698
Cdd:cd03247 120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
481-712 |
1.79e-20 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 1.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLti 560
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK11000 78 -GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 641 LDEPTAGLDPLSR--HRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLkkkwgigYH 712
Cdd:PRK11000 157 LDEPLSNLDAALRvqMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
456-692 |
1.87e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 99.03 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 456 NEIDSDPSLNDSLEpvSPEFQGKEAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSp 535
Cdd:TIGR00956 737 DLTDESDDVNDEKD--MEKESGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV- 813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 536 pTTGSVTIYNQTVS--EMDDSDAvlTITGVCPQSNVQFGFLTVRENLRLFAKIKgiLPHEVEQE-----VQQVLQDLEME 608
Cdd:TIGR00956 814 -TTGVITGGDRLVNgrPLDSSFQ--RSIGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEME 888
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 609 NIQDIL----AQNLSGGQKRKLTLGIAILGDPQVLL-LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVfSTQFMDEADIL 682
Cdd:TIGR00956 889 SYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAIL-CTIHQPSAILF 967
|
250
....*....|..
gi 153792543 683 A--DRKVFISNG 692
Cdd:TIGR00956 968 EefDRLLLLQKG 979
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
481-699 |
2.32e-20 |
|
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: 91.40 E-value: 2.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:cd03244 3 IEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TgVCPQSNVQF-GflTVRENLRLFAKikgilpHEvEQEVQQVLQDLEMENIQDILA-----------QNLSGGQKRKLTL 628
Cdd:cd03244 81 S-IIPQDPVLFsG--TIRSNLDPFGE------YS-DEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQ----FMDeadilADRKVFISNGRLKCAGS 699
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1307-1516 |
2.36e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 98.27 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG----YCPQENVLWPNLTVKEHL 1382
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRrrvgYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1463 -------RAT-FtntergalLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1516
Cdd:NF033858 441 ielsredGVTiF--------ISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARGAATL 493
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1309-1502 |
2.60e-20 |
|
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: 90.19 E-value: 2.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqenvlwpnltvkEHLELYAAv 1388
Cdd:cd03214 16 DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG--------------------------KDLASLSP- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 KGLKKKDAVV-TITRLVNALKLQDhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFT 1467
Cdd:cd03214 69 KELARKIAYVpQALELLGLAHLAD---RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRLAR 145
|
170 180 190
....*....|....*....|....*....|....*
gi 153792543 1468 NTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03214 146 ERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1305-1503 |
3.85e-20 |
|
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: 91.14 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAAlgflgycP----------QENVLWP 1374
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-------PphkrpvntvfQNYALFP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEG 1454
Cdd:cd03300 86 HLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1455 QQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:cd03300 166 RKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-695 |
4.09e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 91.03 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 485 NLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDS-DAVLtitgv 563
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAaKAEL----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 564 cpqSNVQFGFL----------TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK11629 85 ---RNQKLGFIyqfhhllpdfTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILaDRKVFISNGRLK 695
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1309-1497 |
4.65e-20 |
|
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: 91.30 E-value: 4.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQ-VFL----KGsgggaalgflgycpQENVlWPnltVKEHL- 1382
Cdd:COG1119 20 DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerRG--------------GEDV-WE---LRKRIg 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ----ELYAAV-KGLKKKDAVVT-------------------ITRLVNALKLQDHLKALVRTLSEGVKRKlcfVL---SIL 1435
Cdd:COG1119 82 lvspALQLRFpRDETVLDVVLSgffdsiglyreptdeqrerARELLELLGLAHLADRPFGTLSQGEQRR---VLiarALV 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1436 GNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
480-693 |
5.65e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.37 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAvlT 559
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR--D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCpQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK11650 78 IAMVF-QNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK11650 157 LFDEPLSNLDAKLRVQMRLEIQRlhRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
482-694 |
5.91e-20 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 95.36 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTIT 561
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCPQSNVQFGFLTVRENLRLfakikGILPH--------EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAIL 633
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYL-----GQLPHkggivnrrLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK11288 157 RNARVIAFDEPTSSLSAREIEQLFRVIRELRAeGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1269-1507 |
7.12e-20 |
|
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: 95.36 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1269 GAMATLQTDEKPVIIASCLRKEYIGRTKRcfskmkKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQ 1348
Cdd:COG1123 248 GRAAPAAAAAEPLLEVRNLSKRYPVRGKG------GVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1349 VFLKGSGGGAALGFLGYCPQENV----------LWPNLTVKEHLELYAAVKGLKKKDAvvtITRLVNALkLQ------DH 1412
Cdd:COG1123 322 ILFDGKDLTKLSRRSLRELRRRVqmvfqdpyssLNPRMTVGDIIAEPLRLHGLLSRAE---RRERVAEL-LErvglppDL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1413 LKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAI 1492
Cdd:COG1123 398 ADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAV 477
|
250
....*....|....*
gi 153792543 1493 MVSGRLRCIGSIQHL 1507
Cdd:COG1123 478 MYDGRIVEDGPTEEV 492
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1309-1498 |
7.61e-20 |
|
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: 89.15 E-value: 7.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTA--GQVFLKG--SGGGAALGFLGYCPQENVLWPNLTVKEHLEL 1384
Cdd:cd03213 26 KNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGrpLDKRSFRKIIGYVPQDDILHPTLTVRETLMF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 YAAVKGlkkkdavvtitrlvnalklqdhlkalvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:cd03213 106 AAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRR 156
|
170 180 190
....*....|....*....|....*....|....*
gi 153792543 1465 tFTNTERGALLTTHYM-AEAEAVCDRVAIMVSGRL 1498
Cdd:cd03213 157 -LADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
481-685 |
7.69e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 95.12 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDA-VLT 559
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAhQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVcPQSNVQFGFLTVRENLrLFAKIKgilPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK15439 88 IYLV-PQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKERRAGRV-IVFSTQFMDEADILADR 685
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADR 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
512-708 |
7.99e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 93.02 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 512 ITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavltiTGVC-PQSNVQFGFltVRENLRLFA--KIKG 588
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAE--------KGIClPPEKRRIGY--VFQDARLFPhyKVRG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 589 IL----PHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDpLSRHRiwNLLK--E 662
Cdd:PRK11144 96 NLrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-LPRKR--ELLPylE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 663 RRAGRV---IVFSTQFMDEADILADRKVFISNGRLKCAGSslfLKKKWG 708
Cdd:PRK11144 173 RLAREInipILYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
478-694 |
1.04e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 90.67 E-value: 1.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGL-----SPPTTGSVTIYNQTVSEMD 552
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 -DSDAVLTITGVCPQSNVQFGFLTVRENLRLFAKIKGILP--HEVEQEVQQVLQDLEM-ENIQDIL---AQNLSGGQKRK 625
Cdd:PRK14267 78 vDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwDEVKDRLndyPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
481-694 |
1.77e-19 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 90.25 E-value: 1.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYS-----GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD 555
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 AVL-----------TITGVCPQSNVQFgflTVRENLRLFAKIKgilphEVEQE--VQQVLQDLEME-NIQDILAQNLSGG 621
Cdd:TIGR02769 83 RRAfrrdvqlvfqdSPSAVNPRMTVRQ---IIGEPLRHLTSLD-----ESEQKarIAELLDMVGLRsEDADKLPRQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 622 QKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA--GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
481-713 |
2.11e-19 |
|
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: 89.14 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdSDAVLTI 560
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFgFLTVRENLRLfakikGILPHEVEQEVQQVLQdlemENIQDILAQ--------------NLSGGQKRKL 626
Cdd:cd03249 79 IGLVSQEPVLF-DGTIAENIRY-----GKPDATDEEVEEAAKK----ANIHDFIMSlpdgydtlvgergsQLSGGQKQRI 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIV-----FSTqfmdeadIL-ADRKVFISNGRLKCAGSS 700
Cdd:cd03249 149 AIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 153792543 701 LFLKKKWGIGYHL 713
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
483-694 |
2.64e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.41 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMdDSDAVLTItg 562
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQL-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 563 vcpqSNVQFGF----------LTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAI 632
Cdd:PRK10535 84 ----RREHFGFifqryhllshLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADiLADRKVFISNGRL 694
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1306-1498 |
3.00e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 93.17 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP------------QENVLW 1373
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRS------PrdaialgigmvhQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHLELYAAVKG---LKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:COG3845 93 PNLTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153792543 1451 DPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG3845 173 TPQEADELFEILRR-LAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
481-690 |
3.95e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 89.07 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLI---NTLSGLSPP--TTGSVTIYNQTVSEMD-DS 554
Cdd:PRK14243 11 LRTENLNVYY----GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLYAPDvDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 DAVLTITGVCPQSNVQFGfLTVRENLRLFAKI---KGILPHEVEQEVQQ-VLQDlemeNIQDILAQN---LSGGQKRKLT 627
Cdd:PRK14243 87 VEVRRRIGMVFQKPNPFP-KSIYDNIAYGARIngyKGDMDELVERSLRQaALWD----EVKDKLKQSglsLSGGQQQRLC 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 628 LGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFIS 690
Cdd:PRK14243 162 IARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
461-694 |
4.88e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.40 E-value: 4.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 461 DPSLNDSLEPVSPefqGKEAIRIKNLkkEYSGKHGkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGS 540
Cdd:COG3845 241 EVLLRVEKAPAEP---GEVVLEVENL--SVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGS 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 541 VTIYNQTVSEMDdsdaVLTI--------------TGVCPQsnvqfgfLTVRENLRL-------FAKiKGIL-PHEVEQEV 598
Cdd:COG3845 315 IRLDGEDITGLS----PRERrrlgvayipedrlgRGLVPD-------MSVAENLILgryrrppFSR-GGFLdRKAIRAFA 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 599 QQVLQDLemeNIQ----DILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN-LLKERRAGR-VIVFS 672
Cdd:COG3845 383 EELIEEF---DVRtpgpDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAaVLLIS 459
|
250 260
....*....|....*....|..
gi 153792543 673 TQfMDEADILADRKVFISNGRL 694
Cdd:COG3845 460 ED-LDEILALSDRIAVMYEGRI 480
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1307-1498 |
4.96e-19 |
|
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: 87.65 E-value: 4.96e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWpNLTVKEH 1381
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLrrnigYVPQDVTLF-YGTLRDN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1382 LELyaavkglkkKDAVVTITRLVNALKL-------QDHLKALV-------RTLSEGVKRKLCFVLSILGNPPVVLLDEPS 1447
Cdd:cd03245 98 ITL---------GAPLADDERILRAAELagvtdfvNKHPNGLDlqigergRGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1448 TGMDPEGQQQMWQAIRATFtnTERGALLTTHYMAeAEAVCDRVAIMVSGRL 1498
Cdd:cd03245 169 SAMDMNSEERLKERLRQLL--GDKTLIIITHRPS-LLDLVDRIIVMDSGRI 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
477-819 |
5.45e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 90.56 E-value: 5.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 477 GKEAIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAG--KTTLINTLSGlspPTTGSVTIYNQTVSEmDDS 554
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCA-NRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 DAVLTITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILG 634
Cdd:NF000106 82 ALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 635 DPQVLLLDEPTAGLDPLSRHRIWNLLKER-RAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSSLFLKKKWGiGYHL 713
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 714 SLHLNEACDPEGITSLVKKHISD--ARLTTQSEERLVYIlPLERTNKFPDLYRDLDRcSNQGIEDYGVSMTTLNEVFLKL 791
Cdd:NF000106 241 QIRPAHAAELDRMVGAIAQAGLDgiAGATADHEDGVVNV-PIVSDEQLSAVVGMLGE-RGFTISGHQHPSAQL*EVFLAI 318
|
330 340
....*....|....*....|....*...
gi 153792543 792 EGKSMADESDVGicgrlQSDGARDMESL 819
Cdd:NF000106 319 TGQKTSEAADGG-----PQDGPQDQQGV 341
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1309-1478 |
6.68e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 6.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG--SGGGAALGFLGYCPQENVLWPNLTVKEHLELYA 1386
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 AVKGLKKKDAVVTITrlvnALKLQD--HLKAlvRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:PRK13539 99 AFLGGEELDIAAALE----AVGLAPlaHLPF--GYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....*.
gi 153792543 1465 tftNTERG--ALLTTH 1478
Cdd:PRK13539 173 ---HLAQGgiVIAATH 185
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
481-694 |
9.33e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 9.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHG-KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIY-----NQTVSEMDDS 554
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdekNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 ---DAVLT---------ITGVCPQSNVQFGFL-------TVRENLRLFAKIKGILPHEVEQEVQQVLQ--DLEMENIQDI 613
Cdd:PRK13651 83 vleKLVIQktrfkkikkIKEIRRRVGVVFQFAeyqlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESYLQRS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 614 lAQNLSGGQKRKLTLGiAILG-DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISN 691
Cdd:PRK13651 163 -PFELSGGQKRRVALA-GILAmEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 153792543 692 GRL 694
Cdd:PRK13651 241 GKI 243
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1309-1498 |
9.36e-19 |
|
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: 86.43 E-value: 9.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQE--------NvLWPNLTVKE 1380
Cdd:cd03262 17 KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKvgmvfqqfN-LFPHLTVLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELyaA---VKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:cd03262 96 NITL--ApikVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPELVGE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 1458 MWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03262 174 VLDVMKDL---AEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1298-1496 |
1.77e-18 |
|
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: 85.39 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1298 CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG--YCPQEnvlwPN 1375
Cdd:cd03226 6 SFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRKSigYVMQD----VD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 L-----TVKEhlELYAAVKGLKKKDAVV-TITRLVNALKLQDhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:cd03226 82 YqlftdSVRE--ELLLGLKELDAGNEQAeTVLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSG 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1450 MDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSG 1496
Cdd:cd03226 157 LDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1309-1498 |
2.15e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP------------QENVLWPNL 1376
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS------PrdaqaagiaiihQELNLVPNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKE--HLELYAAVKGLKKKDAVVTITR-LVNALKLQDHLKALVRTLSEGvKRKLcfVL---SILGNPPVVLLDEPSTGM 1450
Cdd:COG1129 95 SVAEniFLGREPRRGGLIDWRAMRRRAReLLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 1451 DPEGQQQMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG1129 172 TEREVERLFRIIRRL---KAQGVaiIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1271-1503 |
2.17e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.49 E-value: 2.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1271 MATLqtdekpviIASCLRKEYIGRTkrcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF 1350
Cdd:PRK10895 1 MATL--------TAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1351 LKGSGGGAALGFLG------YCPQENVLWPNLTVKEH----LELYAAVKGLKKKDAVVTITRLVNALKLQDHLKalvRTL 1420
Cdd:PRK10895 62 IDDEDISLLPLHARarrgigYLPQEASIFRRLSVYDNlmavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMG---QSL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1421 SEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRC 1500
Cdd:PRK10895 139 SGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
...
gi 153792543 1501 IGS 1503
Cdd:PRK10895 218 HGT 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
481-698 |
2.40e-18 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 89.52 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK09536 4 IDVSDLSVEF----GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFlTVRENLRLfakikGILPHEV---------EQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIA 631
Cdd:PRK09536 80 ASVPQDTSLSFEF-DVRQVVEM-----GRTPHRSrfdtwtetdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 632 ILGDPQVLLLDEPTAGLDplSRHRIWNLLKERR---AGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:PRK09536 154 LAQATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
481-701 |
2.59e-18 |
|
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: 90.63 E-value: 2.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLS--PPTTGSVtIYNQTVSE----MDDS 554
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRI-IYHVALCEkcgyVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 DAVLTITGVCPQS----NVQFGFL--TVRENL---------RLFA------KIKGILP------HEVEQEVQQVLQDLEM 607
Cdd:TIGR03269 76 SKVGEPCPVCGGTlepeEVDFWNLsdKLRRRIrkriaimlqRTFAlygddtVLDNVLEaleeigYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 608 ENIQDI---LAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADIL 682
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDL 235
|
250
....*....|....*....
gi 153792543 683 ADRKVFISNGRLKCAGSSL 701
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPD 254
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
500-687 |
2.72e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.23 E-value: 2.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSG-LSPP--TTGSVTIYNQtvsEMDDSDAVLTITGVCPQSNVQFGFLTV 576
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSPAfsASGEVLLNGR---RLTALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 577 RENLrLFAkikgiLPHEV-----EQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:COG4136 94 GENL-AFA-----LPPTIgraqrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153792543 652 SRHRI----WNLLKERRAGRVIVfsTQfmDEADILADRKV 687
Cdd:COG4136 168 LRAQFrefvFEQIRQRGIPALLV--TH--DEEDAPAAGRV 203
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
466-694 |
2.93e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 466 DSLEPVSPEFQGKEAIRIKNLKKEysgkhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYN 545
Cdd:COG1129 242 EDLFPKRAAAPGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 546 QTVSEMDDSDAV------LT----ITGVCPQsnvqfgfLTVREN-----LRLFAKiKGILPHEVEQE-VQQVLQDLemeN 609
Cdd:COG1129 314 KPVRIRSPRDAIragiayVPedrkGEGLVLD-------LSIRENitlasLDRLSR-GGLLDRRRERAlAEEYIKRL---R 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 610 I----QDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGR-VIVFSTQfMDEADILA 683
Cdd:COG1129 383 IktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKaVIVISSE-LPELLGLS 461
|
250
....*....|.
gi 153792543 684 DRKVFISNGRL 694
Cdd:COG1129 462 DRILVMREGRI 472
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
481-698 |
3.59e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 86.18 E-value: 3.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK10619 6 LNVIDLHKRY-GEH---EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 -------------TGVCPQSNVqFGFLTVREN-LRLFAKIKGILPHEVEQEVQQVLQDLEM-ENIQDILAQNLSGGQKRK 625
Cdd:PRK10619 82 adknqlrllrtrlTMVFQHFNL-WSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPL---SRHRIWNLLKERraGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPElvgEVLRIMQQLAEE--GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
480-699 |
3.98e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT 559
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITgVCPQSnVQFGFLTVRENLRLfAKikgilPHEVEQEVQQVLQDLEMENiqdiLAQN--------------LSGGQKRK 625
Cdd:PRK11160 416 IS-VVSQR-VHLFSATLRDNLLL-AA-----PNASDEALIEVLQQVGLEK----LLEDdkglnawlgeggrqLSGGEQRR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFST-------QFmdeadilaDRKVFISNGRLKCAG 698
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrltgleQF--------DRICVMDNGQIIEQG 555
|
.
gi 153792543 699 S 699
Cdd:PRK11160 556 T 556
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1315-1498 |
5.80e-18 |
|
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: 84.08 E-value: 5.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGycP-----QENVLWPNLTVKEHLELyAAVK 1389
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADR--PvsmlfQENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1390 GLK----KKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAT 1465
Cdd:cd03298 98 GLKltaeDRQAIEVALARVG---LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 153792543 1466 FTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
480-685 |
6.15e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 88.93 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV-L 558
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIaL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TItGVCPQSNVQFGFLTVRENLRLFAKIKGIL---PHEVEQEVQQVLQDLEMEnIQ-DILAQNLSGGQKRKLTlgI--AI 632
Cdd:COG3845 81 GI-GMVHQHFMLVPNLTVAENIVLGLEPTKGGrldRKAARARIRELSERYGLD-VDpDAKVEDLSVGEQQRVE--IlkAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 633 LGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADR 685
Cdd:COG3845 157 YRGARILILDEPTAVLTPQEADELFEILRRlAAEGKSIIFITHKLREVMAIADR 210
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
481-699 |
6.35e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.81 E-value: 6.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK13644 2 IRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQS-NVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 640 LLDEPTAGLDPLSRHRIW-NLLKERRAGRVIVFSTQFMDEADIlADRKVFISNGRLKCAGS 699
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLeRIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
481-660 |
7.42e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 7.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD-AVLT 559
Cdd:PRK10584 7 VEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArAKLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 I--TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQ 637
Cdd:PRK10584 87 AkhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166
|
170 180
....*....|....*....|...
gi 153792543 638 VLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLL 189
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
481-712 |
8.51e-18 |
|
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: 84.59 E-value: 8.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdSDAVLTI 560
Cdd:cd03253 1 IEFENVTFAY---DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGfLTVRENLRlFAKIKGIlPHEVEQEVQQVLQDLEMENIQD----ILAQN---LSGGQKRKLTLGIAIL 633
Cdd:cd03253 77 IGVVPQDTVLFN-DTIGYNIR-YGRPDAT-DEEVIEAAKAAQIHDKIMRFPDgydtIVGERglkLSGGEKQRVAIARAIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 634 GDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVF-----STqFMDeadilADRKVFISNGRLKCAGSSLFLKKKWG 708
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIViahrlST-IVN-----ADKIIVLKDGRIVERGTHEELLAKGG 227
|
....
gi 153792543 709 IgYH 712
Cdd:cd03253 228 L-YA 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
481-679 |
9.23e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 85.19 E-value: 9.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK13648 8 IVFKNVSFQYQSD--ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRlFAKIKGILPHE-VEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK13648 86 GIVFQNPDNQFVGSIVKYDVA-FGLENHAVPYDeMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKERRAGR--VIVFSTQFMDEA 679
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
503-662 |
9.56e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.13 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 503 LGFDIYEGQITALLGHSGAGKTTLINTLSGLSPpTTGSVTIYNQTVSEMDDSDAVLTITGVcpQSNVQFGFLTVRENLRL 582
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPESWRKHLSWV--GQNPQLPHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 583 fAKikgilPHEVEQEVQQVLQDlemENIQDILAQ--------------NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:PRK11174 446 -GN-----PDASDEQLQQALEN---AWVSEFLPLlpqgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170
....*....|....
gi 153792543 649 DPLSRHRIWNLLKE 662
Cdd:PRK11174 517 DAHSEQLVMQALNA 530
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
483-695 |
1.01e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.58 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI-------Y-NQTVSEMDDS 554
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpkglrigYlPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 ---DAVLtiTGVCPQSNVQFGFLTVRENL-----------RLFAKIKGILPHEVEQEVQQVLQDLEM-ENIQDILAQNLS 619
Cdd:COG0488 77 tvlDTVL--DGDAELRALEAELEELEAKLaepdedlerlaELQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSELS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 620 GGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSrhRIW--NLLKERRaGRVIVFS--TQFMDEadiLADRKVFISNGRLK 695
Cdd:COG0488 155 GGWRRRVALARALLSEPDLLLLDEPTNHLDLES--IEWleEFLKNYP-GTVLVVShdRYFLDR---VATRILELDRGKLT 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1304-1498 |
1.24e-17 |
|
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: 83.77 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITG-----DTIPTAGQVFLKGSgggaalgfLGYCPQENVLW----- 1373
Cdd:cd03260 12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGK--------DIYDLDVDVLElrrrv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 ------PNL---TVKEHLELYAAVKGLKKKDAVVTITRlvNALK-------LQDHLKALvrTLSEGVKRKLCFVLSILGN 1437
Cdd:cd03260 84 gmvfqkPNPfpgSIYDNVAYGLRLHGIKLKEELDERVE--EALRkaalwdeVKDRLHAL--GLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1438 PPVVLLDEPSTGMDPEGQQQMWQAIRAtfTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAE--LKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
481-693 |
1.26e-17 |
|
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: 81.34 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYnqtvsemddsdavlti 560
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpqSNVQFGFLtvrenlrlfakikgilphevEQevqqvlqdlemeniqdilaqnLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:cd03221 61 ------STVKIGYF--------------------EQ---------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRaGRVIVFS--TQFMDEadiLADRKVFISNGR 693
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP-GTVILVShdRYFLDQ---VATKIIELEDGK 144
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1309-1497 |
1.37e-17 |
|
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: 82.05 E-value: 1.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWpNLTVKEHLe 1383
Cdd:cd03228 19 KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLrkniaYVPQDPFLF-SGTIRENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 lyaavkglkkkdavvtitrlvnalklqdhlkalvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIR 1463
Cdd:cd03228 97 ------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALR 140
|
170 180 190
....*....|....*....|....*....|....
gi 153792543 1464 ATFtnTERGALLTTHYMAEAEAvCDRVAIMVSGR 1497
Cdd:cd03228 141 ALA--KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1310-1505 |
1.59e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 84.05 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaaLGFLGYCPQE------------NVLWPnLT 1377
Cdd:PRK13548 20 DVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG------RPLADWSPAElarrravlpqhsSLSFP-FT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1378 VKEHLELYAAVKGLKKKDAvvtiTRLV-NALKLQD--HLKA-LVRTLSEGVK------RKLCFVLSILGNPPVVLLDEPS 1447
Cdd:PRK13548 93 VEEVVAMGRAPHGLSRAED----DALVaAALAQVDlaHLAGrDYPQLSGGEQqrvqlaRVLAQLWEPDGPPRWLLLDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1448 TGMDPEGQQQMWQAIRAtFTNTERGAL--------LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1505
Cdd:PRK13548 169 SALDLAHQHHVLRLARQ-LAHERGLAVivvlhdlnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
481-699 |
1.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 84.78 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK13650 84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFS-TQFMDEAdILADRKVFISNGRLKCAGS 699
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGiRDDYQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1301-1498 |
1.83e-17 |
|
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: 83.09 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITG---DTIPTAGQVFLKGSGG--GAALGFLGYCPQENVLWPN 1375
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRkpDQFQKCVAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 LTVKEHLeLYAAVKGL------KKKDAVVTITRLvNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:cd03234 96 LTVRETL-TYTAILRLprkssdAIRKKRVEDVLL-RDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 1450 MDPEGQQQMWQAIRATFTnTERGALLTTHY-MAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03234 174 LDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
481-693 |
2.48e-17 |
|
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: 82.13 E-value: 2.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVE-ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTvsemddsdavlt 559
Cdd:cd03250 1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSI------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itGVCPQSN-VQFGflTVRENLrLFAKikgilPHEvEQEVQQVL------QDLEM--ENIQDILAQ---NLSGGQKRKLT 627
Cdd:cd03250 69 --AYVSQEPwIQNG--TIRENI-LFGK-----PFD-EERYEKVIkacalePDLEIlpDGDLTEIGEkgiNLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 628 LGIAILGDPQVLLLDEPTAGLDPLSRHRIWN--LLKERRAGRVIVFST---QFMDEadilADRKVFISNGR 693
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVThqlQLLPH----ADQIVVLDNGR 204
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
484-699 |
3.08e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 85.86 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYS-GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD---AVLT 559
Cdd:PRK10070 27 QGLSKEQIlEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElreVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 ITGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKERRAG--RVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKhqRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1310-1507 |
3.35e-17 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 82.50 E-value: 3.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP---------QENVLWPNLTVKE 1380
Cdd:COG3840 17 RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP------PaerpvsmlfQENNLFPHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELyaavkGLK--------KKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP 1452
Cdd:COG3840 91 NIGL-----GLRpglkltaeQRAQVEQALERVG---LAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1453 EGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:COG3840 163 ALRQEMLDLVDE--LCRERGLtvLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
501-649 |
3.60e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 501 RGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDS--DAVLTI---TGVCPQsnvqfgfLT 575
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYLghqPGIKTE-------LT 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 576 VRENLRLFAKIKGILPhevEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK13538 91 ALENLRFYQRLHGPGD---DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1292-1502 |
5.24e-17 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 83.08 E-value: 5.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1292 IGRTKR-CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGF-------- 1362
Cdd:cd03294 23 KGKSKEeILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKelrelrrk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1363 -LGYCPQENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVV 1441
Cdd:cd03294 103 kISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDIL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1442 LLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:cd03294 183 LMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1307-1453 |
6.95e-17 |
|
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: 81.30 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF--------LKGSGGGAALGFLGYCPQENVLWPNLTV 1378
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRvngqdvsdLRGRAIPYLRRKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1307-1510 |
7.51e-17 |
|
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: 85.97 E-value: 7.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL-----GYCPQENVLwPNLTVKEH 1381
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASwrrqiAWVPQNPYL-FAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1382 LELYAAvkglkkkDAvvTITRLVNALKlQDHLKALVRTLSEGV---------------KRKLCFVLSILGNPPVVLLDEP 1446
Cdd:COG4988 431 LRLGRP-------DA--SDEELEAALE-AAGLDEFVAALPDGLdtplgeggrglsggqAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1447 STGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSK 1510
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
478-689 |
1.09e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 1.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV 557
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTItgvcPQSN-VQFGFLTVRENLRLFAKI--KGIL----PHEvEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGI 630
Cdd:PRK15056 81 AYV----PQSEeVDWSFPVLVEDVVMMGRYghMGWLrrakKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFI 689
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMV 215
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1307-1503 |
1.14e-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: 81.19 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTVKEH 1381
Cdd:cd03295 16 AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELrrkigYVIQQIGLFPHMTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1382 LELYAAVKGL---KKKDAVVTITRLVNaLKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP----EG 1454
Cdd:cd03295 96 IALVPKLLKWpkeKIRERADELLALVG-LDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPitrdQL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1455 QQQMW---QAIRATFtntergaLLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:cd03295 175 QEEFKrlqQELGKTI-------VFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
451-694 |
1.44e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 84.72 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 451 HVVLENEIDsDPSLNDSLEPVSPEFQGKEAIRIKNLKKEYSGKHG---------KVEALRGLGF-----DIYEGQITALL 516
Cdd:PRK15439 217 TIALSGKTA-DLSTDDIIQAITPAAREKSLSASQKLWLELPGNRRqqaagapvlTVEDLTGEGFrnislEVRAGEILGLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 517 GHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDS---------------------DAVLTITgVCPQSNVQFGFL- 574
Cdd:PRK15439 296 GVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAqrlarglvylpedrqssglylDAPLAWN-VCALTHNRRGFWi 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 575 -TVRENLRL--FAKIKGILPHEVEQEVqqvlqdlemeniqdilaQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:PRK15439 375 kPARENAVLerYRRALNIKFNHAEQAA-----------------RTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 153792543 652 SRHRIWNLLKERRAGRV-IVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
481-687 |
1.55e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 81.66 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEY-----SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD 555
Cdd:PRK10419 4 LNVSGLSHHYahgglSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 A---------VL--TITGVCPQSNVQFgflTVRENLRlfaKIKGILPHEVEQEVQQVLQDLEM-ENIQDILAQNLSGGQK 623
Cdd:PRK10419 84 RkafrrdiqmVFqdSISAVNPRKTVRE---IIREPLR---HLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 624 RKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--------------------ERRAGRVIVfstqfMDEADILA 683
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKklqqqfgtaclfithdlrlvERFCQRVMV-----MDNGQIVE 232
|
....
gi 153792543 684 DRKV 687
Cdd:PRK10419 233 TQPV 236
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1310-1498 |
1.61e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 80.83 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQE---NV--------LWPNLTV 1378
Cdd:COG4161 20 DINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKPSEKAIRLlrqKVgmvfqqynLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:COG4161 100 MENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153792543 1458 MWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG4161 180 VVEIIR-ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1309-1478 |
1.62e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 79.85 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFlgycPQENVLW--------PNLTVKE 1380
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE----YHQDLLYlghqpgikTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLKKKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQ 1460
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALWEALAQVG---LAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170 180
....*....|....*....|
gi 153792543 1461 AIRAtftNTERG--ALLTTH 1478
Cdd:PRK13538 171 LLAQ---HAEQGgmVILTTH 187
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
498-713 |
1.73e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 80.61 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 498 EALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdSDAVLTITGVCPQSNVQFGfLTVR 577
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD-PAWLRRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 578 ENLRLFAKikGILPHEVEQEVQqvLQD-----LEM-ENIQDILAQN---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:cd03252 94 DNIALADP--GMSMERVIEAAK--LAGahdfiSELpEGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 649 DPLSRHRIWNLLKERRAGR-VIVFSTQFmdEADILADRKVFISNGRLKCAGSSLFLKKKWGIGYHL 713
Cdd:cd03252 170 DYESEHAIMRNMHDICAGRtVIIIAHRL--STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
483-694 |
2.16e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 80.88 E-value: 2.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvsemddsdavltITG 562
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------------------LAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 563 VCPQSNVqfgfltvRENLRLFAKIKGILP-HEVEQEV---------QQVLQDLEMENIQDiLAQN----LSGGQKRKLTL 628
Cdd:PRK11247 73 TAPLAEA-------REDTRLMFQDARLLPwKKVIDNVglglkgqwrDAALQALAAVGLAD-RANEwpaaLSGGQKQRVAL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSR-------HRIWnllkeRRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRiemqdliESLW-----QQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1309-1504 |
2.37e-16 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 80.20 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENVLWPNLTVKEHLELY--A 1386
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNYSLLPWLTVRENIALAvdR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 AVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP-------EGQQQMW 1459
Cdd:TIGR01184 82 VLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgnlqEELMQIW 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1460 QAIRATftntergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1504
Cdd:TIGR01184 162 EEHRVT-------VLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
479-693 |
2.52e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.79 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEY-----SGKhgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtIYNQTVSEMDD 553
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGK--RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSI-LVRHDGGWVDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 554 SDA----VL-----TItGVCPQsnvqfgFLTVR----------ENLRLfakiKGILPHEVEQEVQQVLQDLEM-ENIQDI 613
Cdd:COG4778 80 AQAspreILalrrrTI-GYVSQ------FLRVIprvsaldvvaEPLLE----RGVDREEARARARELLARLNLpERLWDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 614 LAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVfsTQFMDEA--DILADRKVFIS 690
Cdd:COG4778 149 PPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEaKARGTAII--GIFHDEEvrEAVADRVVDVT 226
|
...
gi 153792543 691 NGR 693
Cdd:COG4778 227 PFS 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1309-1508 |
3.16e-16 |
|
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: 79.85 E-value: 3.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGY--------CPQENVLWPNLTV-- 1378
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYrlrrrmgmLFQSGALFDSLTVfe 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 ------KEHLELYAAvkglkkkdavvTITRLVnALKLQ-----DHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPS 1447
Cdd:cd03261 97 nvafplREHTRLSEE-----------EIREIV-LEKLEavglrGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1448 TGMDPEGQ---QQMWQAIRATFTNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK 1508
Cdd:cd03261 165 AGLDPIASgviDDLIRSLKKELGLT---SIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
496-694 |
3.59e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 3.59e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 496 KVEALRGLG-----FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTvsemddsdavltITGVCPQSNVQ 570
Cdd:PRK10762 259 KVDNLSGPGvndvsFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHE------------VVTRSPQDGLA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 571 FGF---------------LTVREN-----LRLFAKIKGILPHEVEQevQQVLQDLEMENI----QDILAQNLSGGQKRKL 626
Cdd:PRK10762 327 NGIvyisedrkrdglvlgMSVKENmsltaLRYFSRAGGSLKHADEQ--QAVSDFIRLFNIktpsMEQAIGLLSGGNQQKV 404
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1304-1524 |
4.62e-16 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 80.17 E-value: 4.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAalgflgycpqENVLWpnlTVKEHL- 1382
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD----------EENLW---EIRKKVg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 --------ELYAAV-----------KGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCfVLSILG-NPPVVL 1442
Cdd:TIGR04520 81 mvfqnpdnQFVGATveddvafglenLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPDIII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1443 LDEPsTGM-DPEGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLEM 1519
Cdd:TIGR04520 160 LDEA-TSMlDPKGRKEVLETIRK--LNKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREIFSQ--VELLKEI 233
|
....*
gi 153792543 1520 KVKTP 1524
Cdd:TIGR04520 234 GLDVP 238
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
481-694 |
4.81e-16 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.15 E-value: 4.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAvlti 560
Cdd:PRK10908 2 IRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcPQSNVQFGFL----------TVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGI 630
Cdd:PRK10908 75 ----PFLRRQIGMIfqdhhllmdrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIAR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK10908 151 AVVNKPAVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
495-698 |
5.09e-16 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 83.17 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 495 GKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTItGVCPQsNVQFGFL 574
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHI-GYLPQ-DVELFPG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 575 TVRENLRLF------------AKIKGIlpHEVeqevqqvLQDLEMENIQDILA--QNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:TIGR01842 407 TVAENIARFgenadpekiieaAKLAGV--HEL-------ILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVV 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARFG 535
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
472-694 |
5.21e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.04 E-value: 5.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 472 SPEFQGKEAIRIKNLKKEysgkhgkveALRG-LGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSE 550
Cdd:PRK11288 249 RPRPLGEVRLRLDGLKGP---------GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 551 MDDSDAVLTITGVCPQSNVQFGFL---TVRENL-----RLFAKIKGILPHEVEQE-VQQVLQDLemeNI------QDILa 615
Cdd:PRK11288 320 RSPRDAIRAGIMLCPEDRKAEGIIpvhSVADNInisarRHHLRAGCLINNRWEAEnADRFIRSL---NIktpsreQLIM- 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 616 qNLSGGQKRKltlgiAILG-----DPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFI 689
Cdd:PRK11288 396 -NLSGGNQQK-----AILGrwlseDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVM 469
|
....*
gi 153792543 690 SNGRL 694
Cdd:PRK11288 470 REGRI 474
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
483-649 |
5.94e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 5.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSE--MDDSDAVLTI 560
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsIQQRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tgvcpQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK11432 85 -----QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
....*....
gi 153792543 641 LDEPTAGLD 649
Cdd:PRK11432 160 FDEPLSNLD 168
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
481-670 |
6.21e-16 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 78.22 E-value: 6.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:cd03369 7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TgVCPQSNVQF-GflTVRENLRLFAkikgilpHEVEQEVQQVLQDLEMENiqdilaqNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:cd03369 85 T-IIPQDPTLFsG--TIRSNLDPFD-------EYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVL 147
|
170 180 190
....*....|....*....|....*....|.
gi 153792543 640 LLDEPTAGLDPLSRHRIWNLLKERRAGRVIV 670
Cdd:cd03369 148 VLDEATASIDYATDALIQKTIREEFTNSTIL 178
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1307-1516 |
6.77e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 81.42 E-value: 6.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---SGGGAALGFLGYCPQENVLWPNLTVKEHLE 1383
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGvdlSHVPPYQRPINMMFQSYALFPHMTVEQNIA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIR 1463
Cdd:PRK11607 114 FGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVV 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1464 ATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS----IQHLKSKFGKDYL 1516
Cdd:PRK11607 194 DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFI 250
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1307-1512 |
1.01e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAG--KSTTISMITGdtiPTAGQVFLK-----GSGGGAALGFLGYCPQENVLWPNLTVK 1379
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRf*twcANRRALRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 EHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMW 1459
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1460 QAIRATFTNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:NF000106 185 DEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1309-1453 |
1.24e-15 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 77.79 E-value: 1.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqENV----------------- 1371
Cdd:COG2884 19 SDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG---------------QDLsrlkrreipylrrrigv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 ------LWPNLTVKEHLELYAAVKGLKKKDavvtITRLVNAL----KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVV 1441
Cdd:COG2884 84 vfqdfrLLPDRTVYENVALPLRVTGKSRKE----IRRRVREVldlvGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170
....*....|..
gi 153792543 1442 LLDEPSTGMDPE 1453
Cdd:COG2884 160 LADEPTGNLDPE 171
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
496-649 |
1.34e-15 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 82.97 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 496 KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSpptTGSVTIYNQTVSEM-DDSDAVLTITGVCPQSNVQFGFL 574
Cdd:PLN03140 892 RLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRK---TGGYIEGDIRISGFpKKQETFARISGYCEQNDIHSPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 575 TVRENLRLFAKIKgiLPHEVEQE-----VQQVLQDLEMENIQDILA-----QNLSGGQKRKLTLGIAILGDPQVLLLDEP 644
Cdd:PLN03140 969 TVRESLIYSAFLR--LPKEVSKEekmmfVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEP 1046
|
....*
gi 153792543 645 TAGLD 649
Cdd:PLN03140 1047 TSGLD 1051
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
458-667 |
1.53e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 82.07 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 458 IDSDPSLNDSLEPVsPEFQGKeaIRIKNLKKEYSGKhgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT 537
Cdd:TIGR02203 311 LDSPPEKDTGTRAI-ERARGD--VEFRNVTFRYPGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPD 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 538 TGSVTIynqtvsemdDSDAVLTITGVCPQSNVQFgfltVRENLRLF-----AKIKGILPHEVEQEvqQVLQDLEMENIQD 612
Cdd:TIGR02203 386 SGQILL---------DGHDLADYTLASLRRQVAL----VSQDVVLFndtiaNNIAYGRTEQADRA--EIERALAAAYAQD 450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 613 ILAQ--------------NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR 667
Cdd:TIGR02203 451 FVDKlplgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR 519
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1278-1502 |
1.57e-15 |
|
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: 81.77 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1278 EKPVIIASCLRKEYIGrTKRCFSKmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF------- 1350
Cdd:TIGR03269 276 GEPIIKVRNVSKRYIS-VDRGVVK-----AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrvgdew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1351 ---------LKGSGGGAALGFLgycpQENVLWPNLTVKEHLELYAAV---KGLKKKDAVVTITRL-VNALKLQDHLKALV 1417
Cdd:TIGR03269 350 vdmtkpgpdGRGRAKRYIGILH----QEYDLYPHRTVLDNLTEAIGLelpDELARMKAVITLKMVgFDEEKAEEILDKYP 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1418 RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:TIGR03269 426 DELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
....*
gi 153792543 1498 LRCIG 1502
Cdd:TIGR03269 506 IVKIG 510
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
500-694 |
1.68e-15 |
|
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: 77.51 E-value: 1.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDS--DAVLTITGVCP-------QSNVQ 570
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPvlfarslQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 571 FGfLTVRENLRLFAKIKGILPHEVEQEVQQVLQdlemENIQDILAQnLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:cd03248 110 YG-LQSCSFECVKEAAQKAHAHSFISELASGYD----TEVGEKGSQ-LSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 651 LSRHRIWNLLK---ERRAGRVIVFSTQFMDEadilADRKVFISNGRL 694
Cdd:cd03248 184 ESEQQVQQALYdwpERRTVLVIAHRLSTVER----ADQILVLDGGRI 226
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
468-699 |
1.80e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 79.51 E-value: 1.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 468 LEPVSPeFQGKEAIRIKNLKKEYSGKH-GKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQ 546
Cdd:PRK13631 10 LKVPNP-LSDDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 547 TVSemDDSDAVLTITGVCPQSNVQFGFL------------------TVRENLrLFAKIK-GILPHEVEQEVQQVLQDLEM 607
Cdd:PRK13631 89 YIG--DKKNNHELITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDI-MFGPVAlGVKKSEAKKLAKFYLNKMGL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 608 EniQDILAQN---LSGGQKRKltlgIAILG----DPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEA 679
Cdd:PRK13631 166 D--DSYLERSpfgLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|
gi 153792543 680 DILADRKVFISNGRLKCAGS 699
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGT 259
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
60-390 |
2.22e-15 |
|
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: 79.36 E-value: 2.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 60 MSVVDLGRVDNFNDSNYMMVFAPESEATHEIMNKVASAPFMKgrTIVACPDEKSMNELDLNYSIDAVRVIFKDtFSYHLK 139
Cdd:pfam12698 18 LGLIFSNAVNDPEELPVAVVDEDNSSLSRQLVRALEASPTVN--LVQYVDSEEEAKEALKNGKIDGLLVIPKG-FSKDLL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 140 fswgqripktkehKDHSAPCEPLNNKMICENSAFWEKGFVAFQAAINAGIIEM-----ITNHSVMEELMSVIGSNMKMPP 214
Cdd:pfam12698 95 -------------KGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLllealSTSAPIPVESTPLFNPQSGYAY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 215 FIAqggvatdFFIFFCVISFSSLIyyLSVNITQER-QYMTTLMAMMGLRESAFWLSWSLMYAGFILVVAVLMSLIVKsAQ 293
Cdd:pfam12698 162 YLV-------GLILMIIILIGAAI--IAVSIVEEKeSRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLF-GI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 294 VVVLTGFMVVFLLFLFYGLSLITLSFLMSVLIKKPFLTGLAIFILT-VFWGSLGFTALYKHLPAFVEWTLCFLSPFAFTT 372
Cdd:pfam12698 232 GIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVIlLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPID 311
|
330
....*....|....*...
gi 153792543 373 GMAQLIHLDYDVNSNVNL 390
Cdd:pfam12698 312 GLLRLIYGDSLWEIAPSL 329
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
499-664 |
2.35e-15 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 77.72 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMdDSDAVLTITGVCPQSNVQ-FGFLTVR 577
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQIARMGVVRTFQHVRlFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 578 ENLrLFAK--------IKGILP----HEVEQE-VQQVLQDLEMENIQDIL---AQNLSGGQKRKLTLGIAILGDPQVLLL 641
Cdd:PRK11300 99 ENL-LVAQhqqlktglFSGLLKtpafRRAESEaLDRAATWLERVGLLEHAnrqAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180
....*....|....*....|...
gi 153792543 642 DEPTAGLDPLSRHRIWNLLKERR 664
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELR 200
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
481-694 |
2.64e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 77.44 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSemDDSDAVLTI 560
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 ---TGVCPQSNVQFGFLTVRENLrLFA--KIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGD 635
Cdd:PRK09493 76 rqeAGMVFQQFYLFPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 636 PQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
498-699 |
2.69e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 498 EALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSV---------------TIYNQTVSEMDDSDAVLTITG 562
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwqgkpldyskrgllALRQQVATVFQDPEQQIFYTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 563 VcpQSNVQFGFltvrENLrlfakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLD 642
Cdd:PRK13638 95 I--DSDIAFSL----RNL-------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 643 EPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRRIVAqGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1310-1524 |
2.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.85 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGaalgflgycpQENVlW------------PN-- 1375
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT----------EENV-WdirhkigmvfqnPDnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 ---LTVKEHLELYAAVKGLKKKDAVvtiTRLVNALKL---QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:PRK13650 94 fvgATVEDDVAFGLENKGIPHEEMK---ERVNEALELvgmQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1450 MDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKfGKDyLLEMKVKTP 1524
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR-GND-LLQLGLDIP 242
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
448-713 |
3.73e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 3.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 448 GASHVVLEnEIDSDPSLNDSLEPVSPEFQGKeaIRIKNLKKEYSgKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLI 527
Cdd:TIGR00958 449 GASEKVFE-YLDRKPNIPLTGTLAPLNLEGL--IEFQDVSFSYP-NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVA 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 528 NTLSGLSPPTTGSVTIYNQTVSEMDDSdAVLTITGVCPQSNVQFGfLTVRENlrlfakIKGILPHEVEQEVQQVLQ---- 603
Cdd:TIGR00958 525 ALLQNLYQPTGGQVLLDGVPLVQYDHH-YLHRQVALVGQEPVLFS-GSVREN------IAYGLTDTPDEEIMAAAKaana 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 604 -DLEMENIQDI------LAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKerRAGRVIVFSTQFM 676
Cdd:TIGR00958 597 hDFIMEFPNGYdtevgeKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRL 674
|
250 260 270
....*....|....*....|....*....|....*..
gi 153792543 677 DEADiLADRKVFISNGRLKCAGSSLFLKKKWGIGYHL 713
Cdd:TIGR00958 675 STVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1299-1512 |
3.91e-15 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 76.50 E-value: 3.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1299 FSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLW 1373
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLrsmigVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNlTVKEHLEL---YAAVKGLKKKDAVVTITRLVNalKLQDHLKALVR----TLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:cd03254 90 SG-TIMENIRLgrpNATDEEVIEAAKEAGAHDFIM--KLPNGYDTVLGenggNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1447 STGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLSTIKNA-DKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1309-1517 |
4.96e-15 |
|
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: 80.65 E-value: 4.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWpNLTVKEHLE 1383
Cdd:COG2274 492 DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLrrqigVVLQDVFLF-SGTIRENIT 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYaavkglkkkDAVVTITRLVNALK---LQDHLKALV-----------RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:COG2274 571 LG---------DPDATDEEIIEAARlagLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSA 641
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1450 MDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1517
Cdd:COG2274 642 LDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1303-1498 |
6.51e-15 |
|
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: 74.27 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgflgycpqenvlwPNLTVKEHL 1382
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGV-------------------PVSDLEKAL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVkgLKKKDAVVTITRLVNalklqdhlkaLVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMwqaI 1462
Cdd:cd03247 74 SSLISV--LNQRPYLFDTTLRNN----------LGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQL---L 138
|
170 180 190
....*....|....*....|....*....|....*..
gi 153792543 1463 RATFTNTE-RGALLTTHYMAEAEAVcDRVAIMVSGRL 1498
Cdd:cd03247 139 SLIFEVLKdKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1311-1478 |
7.24e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.84 E-value: 7.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLgycpQENVLW--------PNLTVKEHL 1382
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI----ARGLLYlghapgikTTLSVLENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAVKGlkkKDAVVTITRLVNALKLQDhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:cd03231 95 RFWHADHS---DEQVEEALARVGLNGFED---RPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*...
gi 153792543 1463 RAtftNTERG--ALLTTH 1478
Cdd:cd03231 169 AG---HCARGgmVVLTTH 183
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1305-1498 |
8.43e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 74.39 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG------YCP---QENVLWPN 1375
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAiragiaYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 LTVKEHLelyaavkglkkkdavvtitrlvnalklqdhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03215 93 LSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1456 QQMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:cd03215 141 AEIYRLIREL---ADAGKavLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1307-1503 |
8.63e-15 |
|
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: 75.84 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---SGGGAALGFLGYCPQENVLWPNLTVKEHLE 1383
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGedaTDVPVQERNVGFVFQHYALFRHMTVFDNVA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKGLKKKDAVVTITRLVNAL-------KLQDHLKAlvrTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQ 1456
Cdd:cd03296 97 FGLRVKPRSERPPEAEIRAKVHELlklvqldWLADRYPA---QLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1457 QMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:cd03296 174 ELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
481-702 |
9.46e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 76.67 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSgKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTI 560
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 TGVCPQSNVQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLL 640
Cdd:PRK13642 84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 641 LDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFS-TQFMDEAdILADRKVFISNGRL--KCAGSSLF 702
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEiKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-700 |
1.19e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 75.85 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 477 GKEAIRIKNLKKEYSGKHGKVeALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGL------SPPTTGSVTIYNQTVSE 550
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 551 MDDSDAVLTITGVCPQSNvQFGFLTVRENLRLFAKIKGIL-PHEVEQEVQQVLQDLEM-ENIQDIL---AQNLSGGQKRK 625
Cdd:PRK14246 83 IDAIKLRKEVGMVFQQPN-PFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSS 700
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1312-1509 |
1.44e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.00 E-value: 1.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1312 SFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP---------QENVLWPNLTVKEHL 1382
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP------PsrrpvsmlfQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAAvKGLK----KKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:PRK10771 93 GLGLN-PGLKlnaaQREKLHAIARQMG---IEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1459 WQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKS 1509
Cdd:PRK10771 169 LTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
467-695 |
2.75e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 77.56 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 467 SLEPVSPEFQGKEAIRIKNLKKeYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT-TGSVTIYN 545
Cdd:TIGR02633 244 SLYPHEPHEIGDVILEARNLTC-WDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 546 QTVSEMDDSDAVLTITGVCPQSNVQFGF---LTVRENLRL-----FAKIKGILPHEVEQEVQQVLQDLEMENIQDILA-Q 616
Cdd:TIGR02633 323 KPVDIRNPAQAIRAGIAMVPEDRKRHGIvpiLGVGKNITLsvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLPiG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 617 NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQfMDEADILADRKVFISNGRL 694
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGKL 481
|
.
gi 153792543 695 K 695
Cdd:TIGR02633 482 K 482
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1307-1550 |
3.19e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 77.62 E-value: 3.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLgycpqenvLWPNLTVKEHLELYA 1386
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSG--------LNGQLTGIENIELKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 AVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDpegqqqmwqairATF 1466
Cdd:PRK13545 111 LMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD------------QTF 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1467 TN---------TERGA--LLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGkDYLLEMKVKTPSQVEPLNTEIM 1535
Cdd:PRK13545 179 TKkcldkmnefKEQGKtiFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDFREEQI 257
|
250
....*....|....*
gi 153792543 1536 RLFPQAARQERYSSL 1550
Cdd:PRK13545 258 SQFQHGLLQEDQTGR 272
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1271-1496 |
4.14e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.01 E-value: 4.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1271 MATLQTDEKPVIIASCLRKEYIGRTkrcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF 1350
Cdd:PRK15439 1 MQTSDTTAPPLLCARSISKQYSGVE-----------VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1351 LKGSGGGAALGFLGY------CPQENVLWPNLTVKEHLELyaavkGL-KKKDAVVTITRLVNALKLQDHLKALVRTLsEG 1423
Cdd:PRK15439 70 IGGNPCARLTPAKAHqlgiylVPQEPLLFPNLSVKENILF-----GLpKRQASMQKMKQLLAALGCQLDLDSSAGSL-EV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1424 VKRKLCFVL-SILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSG 1496
Cdd:PRK15439 144 ADRQIVEILrGLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1307-1493 |
5.95e-14 |
|
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: 76.56 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL-----GYCPQENVLWPNlTVKEH 1381
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwrdqiAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1382 LELYaavkglkKKDAvvTITRLVNALK---LQDHLKALV-----------RTLSEGVKRKLCFVLSILGNPPVVLLDEPS 1447
Cdd:TIGR02857 416 IRLA-------RPDA--SDAEIREALEragLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 1448 TGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAvCDRVAIM 1493
Cdd:TIGR02857 487 AHLDAETEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
467-694 |
6.42e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.36 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 467 SLEPVSPEFQGKEAIRIKNLKkeySGKHGKVealRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQ 546
Cdd:PRK09700 252 AMKENVSNLAHETVFEVRNVT---SRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 547 TVSEMDDSDAVLTITGVCPQSNVQFGFL---TVRENLRLFAKIK--------GILPHEVEQ---EVQQVLQDLEMENI-Q 611
Cdd:PRK09700 326 DISPRSPLDAVKKGMAYITESRRDNGFFpnfSIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVnQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 612 DIlaQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFIS 690
Cdd:PRK09700 406 NI--TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVCDRIAVFC 483
|
....
gi 153792543 691 NGRL 694
Cdd:PRK09700 484 EGRL 487
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1303-1498 |
7.18e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 73.97 E-value: 7.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGaalgflgycpQENVLW--------- 1373
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTS----------DEENLWdirnkagmv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 ---PN-----LTVKEHLELYAAVKGLKKKDavvTITRLVNALK---LQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVL 1442
Cdd:PRK13633 91 fqnPDnqivaTIVEEDVAFGPENLGIPPEE---IRERVDESLKkvgMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECII 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1443 LDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1498
Cdd:PRK13633 168 FDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1307-1498 |
7.37e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.57 E-value: 7.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYC----------PQENVLWPnl 1376
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrktvgivfqnPDDQLFAP-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQ 1456
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153792543 1457 QMwqaIRATFTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK13639 175 QI---MKLLYDLNKEGitIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
498-661 |
7.70e-14 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 76.70 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 498 EALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITGVcPQSNVQFGFlTVR 577
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL-PQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 578 ENLRLFAKiKGILPHEVEQEVQQVLQDLEMENIQDIL-------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:TIGR01193 566 ENLLLGAK-ENVSQDEIWAACEIAEIKDDIENMPLGYqtelseeGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170
....*....|..
gi 153792543 651 LSRHRIW-NLLK 661
Cdd:TIGR01193 645 ITEKKIVnNLLN 656
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1304-1516 |
1.02e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 76.70 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF-LKGSGGGAALGFLG-----YCPQ---ENvLWP 1374
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEvLGGDMADARHRRAVcpriaYMPQglgKN-LYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEG 1454
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1455 QQQMWQ---AIRAtftntERGA---LLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1516
Cdd:NF033858 172 RRQFWElidRIRA-----ERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1310-1516 |
1.28e-13 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGflgycPQE--------NV--------LW 1373
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKT-----PSDkairelrrNVgmvfqqynLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP 1452
Cdd:PRK11124 95 PHLTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1453 EGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLK----SKFgKDYL 1516
Cdd:PRK11124 175 EITAQIVSIIRE-LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTqpqtEAF-KNYL 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1288-1513 |
1.49e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.47 E-value: 1.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1288 RKEYIGRTKRCFSKMK-KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIP---TAGQVFLKGSGGGAALGFL 1363
Cdd:TIGR00955 20 WKQLVSRLRGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1364 G--YCPQENVLWPNLTVKEHLELYAAVK---GLKKK------DAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVL 1432
Cdd:TIGR00955 100 IsaYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKekrervDEVLQALGLRKCANTRIGVPGRVKGLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1433 SILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtFTNTERGALLTTHyMAEAEAVC--DRVAIMVSGRLRCIGSIQHLKSK 1510
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVPF 257
|
...
gi 153792543 1511 FGK 1513
Cdd:TIGR00955 258 FSD 260
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1271-1503 |
2.13e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1271 MATLQTDEKPVIIASCLRKEYIGrtkrcfskmkkKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF 1350
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG-----------KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1351 LKGSGGGAAlgflgycPQEN----------VLWPNLTVKEHLELyaavkGLK-KKDAVVTITRLV-NALK---LQDHLKA 1415
Cdd:PRK09452 73 LDGQDITHV-------PAENrhvntvfqsyALFPHMTVFENVAF-----GLRmQKTPAAEITPRVmEALRmvqLEEFAQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1416 LVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA-------TFtntergaLLTTHYMAEAEAVCD 1488
Cdd:PRK09452 141 KPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKAlqrklgiTF-------VFVTHDQEEALTMSD 213
|
250
....*....|....*
gi 153792543 1489 RVAIMVSGRLRCIGS 1503
Cdd:PRK09452 214 RIVVMRDGRIEQDGT 228
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
481-700 |
2.23e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGL--SPPTTGS-VTIYNQTVSE----MDD 553
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitGDKSAGShIELLGRTVQRegrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 554 SDAVLTITGVCPQsnvQFGF---LTVRENLRLFAKikGILP----------HEVEQEVQQVLQDLEMENIQDILAQNLSG 620
Cdd:PRK09984 81 IRKSRANTGYIFQ---QFNLvnrLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 621 GQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAG 698
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDinQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
..
gi 153792543 699 SS 700
Cdd:PRK09984 236 SS 237
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
486-685 |
2.46e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 71.67 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 486 LKKEYSGKHGKVEalrglGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMddsdavltitgvcP 565
Cdd:cd03237 6 MKKTLGEFTLEVE-----GGSISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYK-------------P 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 566 QSnVQFGF-LTVRENLRLFAKIKGILPheveQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEP 644
Cdd:cd03237 68 QY-IKADYeGTVRDLLSSITKDFYTHP----YFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEP 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 645 TAGLDplSRHRIwnllkerRAGRVI------VFSTQFMDEADI-----LADR 685
Cdd:cd03237 143 SAYLD--VEQRL-------MASKVIrrfaenNEKTAFVVEHDIimidyLADR 185
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1309-1517 |
4.57e-13 |
|
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: 70.59 E-value: 4.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWpNLTVKEHLE 1383
Cdd:cd03252 19 DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLrrqvgVVLQENVLF-NRSIRDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKGLKKkdaVVTITRLVNA----LKLQDHLKALV----RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03252 98 LADPGMSMER---VIEAAKLAGAhdfiSELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1456 QQMWQAIRATFTNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1517
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
493-693 |
4.70e-13 |
|
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: 69.60 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 493 KHGKVEA--LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT---TGSVTIYNQTVSEMD---DSDAVLtitgvC 564
Cdd:cd03233 14 GKGRSKIpiLKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAekyPGEIIY-----V 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 565 PQSNVQFGFLTVRENLRLFAKIKGilpheveqevqqvlqdleMENIQDIlaqnlSGGQKRKLTLGIAILGDPQVLLLDEP 644
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKG------------------NEFVRGI-----SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 645 TAGLDPLSRHRIWNLLKE--RRAGRVIVFS-TQFMDEADILADRKVFISNGR 693
Cdd:cd03233 146 TRGLDSSTALEILKCIRTmaDVLKTTTFVSlYQASDEIYDLFDKVLVLYEGR 197
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1311-1478 |
5.45e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.88 E-value: 5.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG--SGGGAALGFLGYCPQENVLWPNLTVKEHLELYAAV 1388
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGktATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCGL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 KGLKKKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIrATFTN 1468
Cdd:PRK13543 110 HGRRAKQMPGSALAIVG---LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI-SAHLR 185
|
170
....*....|
gi 153792543 1469 TERGALLTTH 1478
Cdd:PRK13543 186 GGGAALVTTH 195
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1305-1504 |
7.44e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 70.85 E-value: 7.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENVL---WPNL----- 1376
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLvfqYPEYqlfee 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLELYAAVKGLKKKDAVVTITRLVNALKLqDHLKALVRT---LSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGL-DYEDYKDKSpfeLSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSI 1504
Cdd:PRK13637 179 GRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
500-649 |
7.87e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 73.24 E-value: 7.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTItGVCPQsNVQF--GflTVR 577
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHI-GYLPQ-DVELfdG--TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 578 ENLRLF-----------AKIKGIlpHEVeqevqqVLQdlemeniqdiLAQ-----------NLSGGQKRKLTLGIAILGD 635
Cdd:COG4618 424 ENIARFgdadpekvvaaAKLAGV--HEM------ILR----------LPDgydtrigeggaRLSGGQRQRIGLARALYGD 485
|
170
....*....|....
gi 153792543 636 PQVLLLDEPTAGLD 649
Cdd:COG4618 486 PRLVVLDEPNSNLD 499
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
494-699 |
8.22e-13 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 70.40 E-value: 8.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 494 HGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTItGVCPQSNVQFGF 573
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRI-GLLAQNATTPGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 574 LTVREnlrLFAkiKGILPHEV------EQEVQQVLQDLEMENIQDILAQN---LSGGQKRKLTLGIAILGDPQVLLLDEP 644
Cdd:PRK10253 96 ITVQE---LVA--RGRYPHQPlftrwrKEDEEAVTKAMQATGITHLADQSvdtLSGGQRQRAWIAMVLAQETAIMLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 645 TAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK10253 171 TTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1310-1496 |
8.38e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.14 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVflkgsgGGAALGFLGYCPQENVLWPN--LTVKEHLELYAa 1387
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRIGYVPQKLYLDTTlpLTVNRFLRLRP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1388 vkGLKKKDAVVTITRlVNALKLqdhLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFT 1467
Cdd:PRK09544 95 --GTKKEDILPALKR-VQAGHL---IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRR 168
|
170 180 190
....*....|....*....|....*....|....
gi 153792543 1468 NTERGALLTTH----YMAEA-EAVCDRVAIMVSG 1496
Cdd:PRK09544 169 ELDCAVLMVSHdlhlVMAKTdEVLCLNHHICCSG 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
510-697 |
9.30e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 9.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGL--SPPTTGSVTIYNQTVSEMddsdaVLTITGVCPQSNVQFGFLTVRENLRLFAKIK 587
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTKQ-----ILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 588 giLPHEVEQEV-----QQVLQDLEMENIQDILAQN-----LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHR-I 656
Cdd:PLN03211 169 --LPKSLTKQEkilvaESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRlV 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 657 WNLLKERRAGRVIVFST--------QFMDEADILAD-RKVFISNGRLKCA 697
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMhqpssrvyQMFDSVLVLSEgRCLFFGKGSDAMA 296
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1315-1490 |
9.58e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 69.74 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVflkgsggGAALGFLGYCPQENVLWPNLTVKEHLElyaavkglKKK 1394
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------EIELDTVSYKPQYIKADYEGTVRDLLS--------SIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1395 DAVVT----ITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTE 1470
Cdd:cd03237 87 KDFYThpyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENNE 166
|
170 180
....*....|....*....|
gi 153792543 1471 RGALLTTHYMAEAEAVCDRV 1490
Cdd:cd03237 167 KTAFVVEHDIIMIDYLADRL 186
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1288-1510 |
1.09e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 70.26 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1288 RKEYIGRTKR-CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFL---------KGSGGG 1357
Cdd:PRK13636 1 MEDYILKVEElNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFdgkpidysrKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1358 AALGFLGYCPQENVLWpNLTVKEHLELYAAVKGLKKKDAVvtiTRLVNALKLQ--DHLK-ALVRTLSEGVKRKLCFVLSI 1434
Cdd:PRK13636 81 RESVGMVFQDPDNQLF-SASVYQDVSFGAVNLKLPEDEVR---KRVDNALKRTgiEHLKdKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1435 LGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1510
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1307-1498 |
1.11e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 72.64 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG--------YcpQENVLWPNLTV 1378
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAAlaagvaiiY--QELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHL---ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:PRK11288 97 AENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 1456 QQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK11288 177 EQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1307-1498 |
1.37e-12 |
|
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: 70.47 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITG---DTIPTAGQVFLKGSGGGAALGFLG---------YCPQE--NVL 1372
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKLSEKELrkirgreiqMIFQDpmTSL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVR---TLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:COG0444 100 NPVMTVGDQIaEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIARALALEPKLLIADEPTT 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1449 GMDPEGQQQ---MWQAIRAtftntERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG0444 180 ALDVTIQAQilnLLKDLQR-----ELGLaiLFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
481-699 |
1.55e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 70.04 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHG-KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYN-------QTVSEMD 552
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipanlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 DSDAVLTITGVCPQSNVqfgFLTVRENLRLFAKIK-GILPHEVEQEVQQVLQDLEMEniQDILAQN---LSGGQKRKLTL 628
Cdd:PRK13645 87 RLRKEIGLVFQFPEYQL---FQETIEKDIAFGPVNlGENKQEAYKKVPELLKLVQLP--EDYVKRSpfeLSGGQKRRVAL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
476-699 |
2.12e-12 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 69.06 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 476 QGKEAIRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD 555
Cdd:COG4598 4 TAPPALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 AVLTitgVCPQSNVQ---------F-GF-----LTVRENLrLFAKI--KGILPHEVEQEVQQVLQDLEMENIQDILAQNL 618
Cdd:COG4598 80 GELV---PADRRQLQrirtrlgmvFqSFnlwshMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 619 SGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPlsrHRIWNLLKERRA----GRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKVMRDlaeeGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
....*
gi 153792543 695 KCAGS 699
Cdd:COG4598 233 EEQGP 237
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1309-1498 |
2.16e-12 |
|
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: 66.86 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNlTVKEHLe 1383
Cdd:cd03246 19 RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELgdhvgYLPQDDELFSG-SIAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 lyaavkglkkkdavvtitrlvnalklqdhlkalvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIR 1463
Cdd:cd03246 97 ------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 153792543 1464 ATftnTERGA--LLTTHYMaEAEAVCDRVAIMVSGRL 1498
Cdd:cd03246 141 AL---KAAGAtrIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
499-694 |
2.48e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLT----------ITGVcpQSN 568
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHgfalvteerrSTGI--YAY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 569 VQFGFLTVRENLRLFAKIKGILPHE-VEQEVQQVLQDLEMEN-IQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTA 646
Cdd:PRK10982 341 LDIGFNSLISNIRNYKNKVGLLDNSrMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 647 GLDPLSRHRIWNLLKE--RRAGRVIVFSTQfMDEADILADRKVFISNGRL 694
Cdd:PRK10982 421 GIDVGAKFEIYQLIAElaKKDKGIIIISSE-MPELLGITDRILVMSNGLV 469
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1299-1526 |
2.94e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 68.69 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1299 FSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLgycpqenvLWPNLTV 1378
Cdd:PRK13546 31 KHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAG--------LSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1459 WQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFgKDYLLEMKVKTPSQ 1526
Cdd:PRK13546 183 LDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAE 248
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1306-1516 |
3.95e-12 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 70.06 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---------SGGGAALGFLGYCPQENVLWPNL 1376
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiakisdaELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEH----LELyAAVKGLKKKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP 1452
Cdd:PRK10070 122 TVLDNtafgMEL-AGINAEERREKALDALRQVG---LENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDP 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1453 EGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKFGKDYL 1516
Cdd:PRK10070 198 LIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1303-1498 |
4.99e-12 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 69.06 E-value: 4.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqENVLwpNLTVKE-- 1380
Cdd:PRK11153 16 RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDG---------------QDLT--ALSEKElr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 -----------HLELYAA------------VKGLKKKDavvtITRLVNAL----KLQDHLKALVRTLSEGVKRKlcfvLS 1433
Cdd:PRK11153 79 karrqigmifqHFNLLSSrtvfdnvalpleLAGTPKAE----IKARVTELlelvGLSDKADRYPAQLSGGQKQR----VA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1434 I---LGNPPVVLL-DEPSTGMDPEGQQQMWQAIRAtfTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK11153 151 IaraLASNPKVLLcDEATSALDPATTRSILELLKD--INRELGltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
459-699 |
5.67e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 5.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 459 DSDPSLNDSLEPVSPE-FQGkeAIRIKNLKKEYSGKHgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT 537
Cdd:PRK13657 314 DAVPDVRDPPGAIDLGrVKG--AVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQ 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 538 TGSVTIynqtvSEMDDSDavLTITGVCPQSNVQF---GFL--TVRENLRLfAKikgilPHEVEQEvqqVLQDLEMENIQD 612
Cdd:PRK13657 389 SGRILI-----DGTDIRT--VTRASLRRNIAVVFqdaGLFnrSIEDNIRV-GR-----PDATDEE---MRAAAERAQAHD 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 613 ILAQN--------------LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRvivfsTQFMDe 678
Cdd:PRK13657 453 FIERKpdgydtvvgergrqLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII- 526
|
250 260
....*....|....*....|....*.
gi 153792543 679 ADIL-----ADRKVFISNGRLKCAGS 699
Cdd:PRK13657 527 AHRLstvrnADRILVFDNGRVVESGS 552
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1309-1505 |
7.72e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.45 E-value: 7.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaaLGFLGYCPQE-----NVLwP-------NL 1376
Cdd:COG4559 18 DDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNG------RPLAAWSPWElarrrAVL-PqhsslafPF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLELYAAVKGLKKKDAVVTITRlvnALKLQD--HLKA-LVRTLSEGVK------RKLCFVL-SILGNPPVVLLDEP 1446
Cdd:COG4559 91 TVEEVVALGRAPHGSSAAQDRQIVRE---ALALVGlaHLAGrSYQTLSGGEQqrvqlaRVLAQLWePVDGGPRWLFLDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1447 STGMDPEGQQQMWQAIRaTFTNTERGAL-------LTTHYmaeaeavCDRVAIMVSGRLRCIGSIQ 1505
Cdd:COG4559 168 TSALDLAHQHAVLRLAR-QLARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1304-1524 |
8.10e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 67.71 E-value: 8.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGaalgflgycpQENVLW---------- 1373
Cdd:PRK13632 21 ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS----------KENLKEirkkigiifq 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 -PN-----LTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCfVLSILG-NPPVVLLDEp 1446
Cdd:PRK13632 91 nPDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA-IASVLAlNPEIIIFDE- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1447 STGM-DPEGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQH-LKSkfgKDYLLEMKVKTP 1524
Cdd:PRK13632 169 STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNN---KEILEKAKIDSP 244
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1309-1499 |
8.22e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 69.71 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalGFLGYCPQENVLWPNLTVKE-----HLE 1383
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG------LRIGYLPQEPPLDDDLTVLDtvldgDAE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAvkgLKKKDAVVT------------------------------ITRLVNALKL-QDHLKALVRTLSEGVKRK--LCF 1430
Cdd:COG0488 89 LRAL---EAELEELEAklaepdedlerlaelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRvaLAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1431 VLsiLGNPPVVLLDEPSTGMDPEgqqqmwqAIR--ATFTNTERGALLT-TH--YMaeAEAVCDRVAIMVSGRLR 1499
Cdd:COG0488 166 AL--LSEPDLLLLDEPTNHLDLE-------SIEwlEEFLKNYPGTVLVvSHdrYF--LDRVATRILELDRGKLT 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
482-693 |
9.59e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 67.26 E-value: 9.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 482 RIKNLKKEYSGKHGkveaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvsEMDDSDAVLTIT 561
Cdd:PRK11701 8 SVRGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV--------HYRMRDGQLRDL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 GVCPQSNVQF------GFltVREN----LRLF----AKIKGIL-----PH--EVEQEVQQVLQDLEM--ENIQDiLAQNL 618
Cdd:PRK11701 76 YALSEAERRRllrtewGF--VHQHprdgLRMQvsagGNIGERLmavgaRHygDIRATAGDWLERVEIdaARIDD-LPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 619 SGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1305-1497 |
1.03e-11 |
|
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: 66.82 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG--------YCPQENVLWPNL 1376
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlrrqigMIFQQFNLIERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKE--------HLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:cd03256 94 SVLEnvlsgrlgRRSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1449 GMDPEGQQQMWQAIRAtfTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:cd03256 174 SLDPASSRQVMDLLKR--INREEGitVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1310-1507 |
1.14e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.21 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-YCP--QENVLWPNLTVKEHLELYA 1386
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRdICMvfQSYALFPHMSLGENVGYGL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 AVKGLKKKDAVvtiTRLVNALKLQDhLKAL----VRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:PRK11432 104 KMLGVPKEERK---QRVKEALELVD-LAGFedryVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMREKI 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1463 RATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:PRK11432 180 RELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
481-700 |
1.46e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 66.74 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHG-----KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMD--- 552
Cdd:PRK15112 5 LEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 DSDAVLTI-----TGVCPQSNV-QFGFLTVRENLRLfakikgiLPHEVEQEVQQVLQDLEMENIQ-DILAQNLSGGQKRK 625
Cdd:PRK15112 85 RSQRIRMIfqdpsTSLNPRQRIsQILDFPLRLNTDL-------EPEQREKQIIETLRQVGLLPDHaSYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGSS 700
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLElqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGST 234
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
510-649 |
1.46e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 66.73 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMdDSDAVLTITGVCPQSNVQFGFLTVREnlrLFAKIK-- 587
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW-SSKAFARKVAYLPQQLPAAEGMTVRE---LVAIGRyp 112
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 588 -----GILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK10575 113 whgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1309-1497 |
1.46e-11 |
|
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: 65.36 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKST---TISMITGDTIPTAGQVFLKGSGGGAALGF----LGYCPQENVLWPNLTVKEH 1381
Cdd:cd03233 24 KDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIPYKEFAEKypgeIIYVSEEDVHFPTLTVRET 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1382 LELyaavkglkkkdavvtitrlvnALKLQDHlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQA 1461
Cdd:cd03233 104 LDF---------------------ALRCKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEILKC 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 153792543 1462 IRaTFTNTERGALLTTHYMA--EAEAVCDRVAIMVSGR 1497
Cdd:cd03233 161 IR-TMADVLKTTTFVSLYQAsdEIYDLFDKVLVLYEGR 197
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
505-694 |
1.49e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 69.06 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdsdavltitgvcpqsnvqfgfltvRENLR--- 581
Cdd:COG4615 353 LTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADN------------------------REAYRqlf 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 582 --------LFAKIKGILPHEVEQEVQQVLQDLEMEN---IQD--ILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:COG4615 409 savfsdfhLFDRLLGLDGEADPARARELLERLELDHkvsVEDgrFSTTDLSQGQRKRLALLVALLEDRPILVFDEWAADQ 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 649 DPLSRHRIWN-LLKE-RRAGR-VIVFS--TQFMDeadiLADRKVFISNGRL 694
Cdd:COG4615 489 DPEFRRVFYTeLLPElKARGKtVIAIShdDRYFD----LADRVLKMDYGKL 535
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1306-1478 |
1.69e-11 |
|
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: 68.93 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQEnvlwPNL---T 1377
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVrrrvsVCAQD----AHLfdtT 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1378 VKEHLElyaavkgLKKKDAV-VTITRLVNALKLQDHLKALV-----------RTLSEGVKRKLCFVLSILGNPPVVLLDE 1445
Cdd:TIGR02868 425 VRENLR-------LARPDATdEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 153792543 1446 PSTGMDPEGQQQMWQAIRAtfTNTERGALLTTH 1478
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLA--ALSGRTVVLITH 528
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
500-667 |
1.94e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 68.69 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDdSDAVLTITGVCPQSNVQFGfLTVREN 579
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASLRAAIGIVPQDTVLFN-DTIAYN 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LRlFAKikgilPHEVEQEVQQVLQdleMENIQDILAQ--------------NLSGGQKRKLtlGIA--ILGDPQVLLLDE 643
Cdd:COG5265 452 IA-YGR-----PDASEEEVEAAAR---AAQIHDFIESlpdgydtrvgerglKLSGGEKQRV--AIArtLLKNPPILIFDE 520
|
170 180
....*....|....*....|....
gi 153792543 644 PTAGLDPLSRHRIWNLLKERRAGR 667
Cdd:COG5265 521 ATSALDSRTERAIQAALREVARGR 544
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1307-1507 |
2.01e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.73 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTT-ISMI-----TGDTIPTAGQVFLKGSGGGAALGFLGYCPQENV--------- 1371
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTaLALMrlleqAGGLVQCDKMLLRRRSRQVIELSEQSAAQMRHVrgadmamif 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 ------LWPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVR---TLSEGVKRKLCFVLSILGNPPVV 1441
Cdd:PRK10261 111 qepmtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1442 LLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
510-687 |
2.07e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AVLTITGVCPQSNVQFGFLTVRENLRLFAKIK 587
Cdd:PRK11831 33 GKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDMNVFDNVAYPLREH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 588 GILPHEVEQEVqqVLQDLE---MENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERR 664
Cdd:PRK11831 113 TQLPAPLLHST--VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELN 190
|
170 180 190
....*....|....*....|....*....|..
gi 153792543 665 AG---RVIVFS------TQFMDEADILADRKV 687
Cdd:PRK11831 191 SAlgvTCVVVShdvpevLSIADHAYIVADKKI 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1309-1498 |
2.20e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL------GYCP---QENVLWPNLTVK 1379
Cdd:COG1129 269 RDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiAYVPedrKGEGLVLDLSIR 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 E-----HLELYAAVKGLKKKDAVVTITRLVNALKLQ-DHLKALVRTLSEGVKRKLcfVLS--ILGNPPVVLLDEPSTGMD 1451
Cdd:COG1129 349 EnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKV--VLAkwLATDPKVLILDEPTRGID 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1452 PEGQQQMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG1129 427 VGAKAEIYRLIREL---AAEGKavIVISSELPELLGLSDRILVMREGRI 472
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
481-649 |
2.22e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.91 E-value: 2.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvsemdDSDAVLTI 560
Cdd:PRK09544 5 VSLENVSVSF----GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 561 tGVCPQS-NVQFGF-LTVRENLRLFAKIKG--ILPheveqevqqVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDP 636
Cdd:PRK09544 70 -GYVPQKlYLDTTLpLTVNRFLRLRPGTKKedILP---------ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRP 139
|
170
....*....|...
gi 153792543 637 QVLLLDEPTAGLD 649
Cdd:PRK09544 140 QLLVLDEPTQGVD 152
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
512-694 |
2.44e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 66.27 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 512 ITALLGHSGAGKTTLINTLSGLSPPTTG-----SVTIYNQTVSEMDDSDAVLTITGVCPQSNVQFGfLTVRENLRLFAKI 586
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 587 KGILPHEVEQEVQQV-LQDLEM-ENIQDILAQN---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK 661
Cdd:PRK14271 128 HKLVPRKEFRGVAQArLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR 207
|
170 180 190
....*....|....*....|....*....|...
gi 153792543 662 ERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK14271 208 SLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1309-1503 |
2.73e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.47 E-value: 2.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITG--DTIPTAGQVFLKGsgggaalgflgycpqENVLwpNLTVKEH--LEL 1384
Cdd:cd03217 17 KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKG---------------EDIT--DLPPEERarLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 Y------AAVKGLKKKDAVvtitRLVNAlklqdhlkalvrTLSEGvKRKLCFVLSILG-NPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:cd03217 80 FlafqypPEIPGVKNADFL----RYVNE------------GFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLDIDALRL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1458 MWQAIRaTFTNTERGALLTTHYMAEAEAV-CDRVAIMVSGRLRCIGS 1503
Cdd:cd03217 143 VAEVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1305-1497 |
3.00e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.88 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpqENVL-W---------- 1373
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---------------KDVTkLpeykrakyig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 -----------PNLTVKEHLELyAAVKG--------LKKKDavvtITRLVNALK-----LQDHLKALVRTLSEGVKRKLC 1429
Cdd:COG1101 84 rvfqdpmmgtaPSMTIEENLAL-AYRRGkrrglrrgLTKKR----RELFRELLAtlglgLENRLDTKVGLLSGGQRQALS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1430 FVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAiratfTN---TERG--ALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:COG1101 159 LLMATLTKPKLLLLDEHTAALDPKTAALVLEL-----TEkivEENNltTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1309-1499 |
3.22e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 67.78 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLkGSGGGAAlgflgYCPQEN-VLWPNLTVKEHLELYAa 1387
Cdd:COG0488 332 DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG-----YFDQHQeELDPDKTVLDELRDGA- 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1388 vKGLKKKDAVvtitrlvNALKL----QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIr 1463
Cdd:COG0488 405 -PGGTEQEVR-------GYLGRflfsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEAL- 475
|
170 180 190
....*....|....*....|....*....|....*.
gi 153792543 1464 ATFTNTergALLTTHYMAEAEAVCDRVAIMVSGRLR 1499
Cdd:COG0488 476 DDFPGT---VLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1311-1498 |
4.45e-11 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 65.16 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV-----FLKGSGGGAALGFLGYCPQENV--------LWPNLT 1377
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQKGLIRQLRQHVgfvfqnfnLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1378 VKEH-LELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQ 1456
Cdd:PRK11264 102 VLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 1457 QMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK11264 182 EVLNTIRQ-LAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1307-1505 |
4.70e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGY------CPQENVLWPNLTVKE 1380
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAqlgigiIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HleLYAAVKGLKK---------KDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:PRK09700 100 N--LYIGRHLTKKvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1452 PEGQQQMWqAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1505
Cdd:PRK09700 178 NKEVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
505-695 |
4.79e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 67.26 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSP-PTTGSVTIYNQTVSEMDDSDAVLTitGVC--PQSNVQFGFLT---VRE 578
Cdd:PRK13549 283 FSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQ--GIAmvPEDRKRDGIVPvmgVGK 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 579 NLRL-----FAKIkGILPHEVEQE-VQQVLQDLEMENIQDILA-QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPL 651
Cdd:PRK13549 361 NITLaaldrFTGG-SRIDDAAELKtILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVG 439
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 652 SRHRIWNLLKE--RRAGRVIVFSTQfMDEADILADRKVFISNGRLK 695
Cdd:PRK13549 440 AKYEIYKLINQlvQQGVAIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1298-1517 |
5.02e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 65.21 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1298 CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG--------YCPQE 1369
Cdd:PRK13652 10 CYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrkfvglvfQNPDD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1370 NVLWPnlTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTG 1449
Cdd:PRK13652 90 QIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1450 MDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLkskFGKDYLL 1517
Cdd:PRK13652 168 LDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
500-670 |
5.02e-11 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTiynqtvseMDDSDAVLTItgvcPQ-SNVQFGflTVRE 578
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIA--------RPAGARVLFL----PQrPYLPLG--TLRE 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 579 NLrlfakikgILPHEVEQ----EVQQVLQDLEMENIQDIL------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 648
Cdd:COG4178 445 AL--------LYPATAEAfsdaELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
|
170 180
....*....|....*....|..
gi 153792543 649 DPLSRHRIWNLLKERRAGRVIV 670
Cdd:COG4178 517 DEENEAALYQLLREELPGTTVI 538
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1309-1503 |
5.03e-11 |
|
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: 64.05 E-value: 5.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISM-----------ITGDTIPTAgQVFLKgsgggAALGFLGYCPQENVLWPNlT 1377
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLAlfrlvelssgsILIDGVDIS-KIGLH-----DLRSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1378 VKEHL---------ELYAAVKGLKKKDAVVTitrlvNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:cd03244 94 IRSNLdpfgeysdeELWQALERVGLKEFVES-----LPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1449 GMDPEGQQQMWQAIRATFTNTergALLT-THYMaeaEAV--CDRVAIMVSGRLRCIGS 1503
Cdd:cd03244 169 SVDPETDALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1311-1502 |
6.35e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.40 E-value: 6.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTVKE----- 1380
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAsrrvaSVPQDTSLSFEFDVRQvvemg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 ---HLELYAAVKglKKKDAVVtiTRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:PRK09536 102 rtpHRSRFDTWT--ETDRAAV--ERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1458 MWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:PRK09536 178 TLELVR-RLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
483-671 |
7.62e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.50 E-value: 7.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKHGK---------VEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDD 553
Cdd:PRK15079 11 VADLKVHFDIKDGKqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 554 SDAVLTitgvcpQSNVQFGF----------LTV----RENLRLFAkikgilPHEVEQEVQQVLQDLEM-----ENIQDIL 614
Cdd:PRK15079 91 DEWRAV------RSDIQMIFqdplaslnprMTIgeiiAEPLRTYH------PKLSRQEVKDRVKAMMLkvgllPNLINRY 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 615 AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVF 671
Cdd:PRK15079 159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlqREMGLSLIF 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1301-1511 |
9.57e-11 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 66.36 E-value: 9.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITG--DTIPTAGQVFL------KGSGGGAALGFLGYCP----- 1367
Cdd:TIGR03269 9 KFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalceKCGYVERPSKVGEPCPvcggt 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1368 ---QENVLW-PNLTVKEHLELYAAVK------------------------GLKKKDAVVTITRLVNALKLQDHLKALVRT 1419
Cdd:TIGR03269 89 lepEEVDFWnLSDKLRRRIRKRIAIMlqrtfalygddtvldnvlealeeiGYEGKEAVGRAVDLIEMVQLSHRITHIARD 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1420 LSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1499
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIK 248
|
250
....*....|..
gi 153792543 1500 CIGSIQHLKSKF 1511
Cdd:TIGR03269 249 EEGTPDEVVAVF 260
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1287-1501 |
1.02e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 66.35 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1287 LRKEYIGRTKRCFSKMKKKIatRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------SGGGAAL 1360
Cdd:PRK09700 260 LAHETVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdisprSPLDAVK 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1361 GFLGYCPQ---ENVLWPNLTVKEHLELYAAVKGLKKKDAVVTITRlVNALKLQDHLKAL-----------VRTLSEGVKR 1426
Cdd:PRK09700 338 KGMAYITEsrrDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHE-VDEQRTAENQRELlalkchsvnqnITELSGGNQQ 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1427 KLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1501
Cdd:PRK09700 417 KVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
500-656 |
1.18e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 63.19 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSV------------TIYNQTVSemddsdavltitgVCPQS 567
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLlfegedistlkpEIYRQQVS-------------YCAQT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 568 NVQFGfLTVRENLRLFAKIKGILPHEveqevQQVLQDLEMENI-QDILAQN---LSGGQKRKLTLGIAILGDPQVLLLDE 643
Cdd:PRK10247 90 PTLFG-DTVYDNLIFPWQIRNQQPDP-----AIFLDDLERFALpDTILTKNiaeLSGGEKQRISLIRNLQFMPKVLLLDE 163
|
170
....*....|...
gi 153792543 644 PTAGLDPLSRHRI 656
Cdd:PRK10247 164 ITSALDESNKHNV 176
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1304-1537 |
1.33e-10 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 63.88 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGaalgflgycpQENVlW---------- 1373
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS----------EETV-Wdvrrqvgmvf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 --PN-----LTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:PRK13635 88 qnPDnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1447 STGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGsiqhlkskfgkdyllemkvkTPSQ 1526
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEG--------------------TPEE 226
|
250
....*....|.
gi 153792543 1527 VEPLNTEIMRL 1537
Cdd:PRK13635 227 IFKSGHMLQEI 237
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
458-662 |
1.59e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 65.48 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 458 IDSDPSLndslEPVSPEFQGKEAIRIKNLKKEYSGKHG-------KVEALRGLGFDIYEGQITALLGHSGAGKTTLINTL 530
Cdd:COG4172 257 LAAEPRG----DPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLAL 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 531 SGLSpPTTGSVTIYNQTVSEMDDSD--AVltitgvcpQSNVQ------FGFL--------TVRENLRLFAkiKGILPHEV 594
Cdd:COG4172 333 LRLI-PSEGEIRFDGQDLDGLSRRAlrPL--------RRRMQvvfqdpFGSLsprmtvgqIIAEGLRVHG--PGLSAAER 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 595 EQEVQQVLQDLEMeniqDILAQN-----LSGGQK-RkltLGIA---ILgDPQVLLLDEPTAGLDPLSRHRIWNLLKE 662
Cdd:COG4172 402 RARVAEALEEVGL----DPAARHrypheFSGGQRqR---IAIAralIL-EPKLLVLDEPTSALDVSVQAQILDLLRD 470
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
503-699 |
2.44e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 62.64 E-value: 2.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 503 LGFDIYEGQITALLGHSGAGKTTLINTLSGLSpPTTGSVTIYNQTVSEMDDSDAVLTITGVCPQSNVQFGfLTVRENLRL 582
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 583 FakikgiLP-HEVEQEVQQVLQDL-EMENIQDILA---QNLSGGQKRKLTLGIAIL-----GDP--QVLLLDEPTAGLDP 650
Cdd:PRK03695 93 H------QPdKTRTEAVASALNEVaEALGLDDKLGrsvNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 651 LSRHRIWNLLKER-RAGRVIVFSTQFMDEADILADRKVFISNGRLKCAGS 699
Cdd:PRK03695 167 AQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1304-1510 |
2.65e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 63.31 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFL-----------KGSGGGAALGFLGYCPQENVL 1372
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgnKNLKKLRKKVSLVFQFPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNlTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHL--KALVRtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1451 DPEGQQQMWQairaTFTNTERGA---LLTTHYMAEAEAVCDRVAIMVSGRLrcigsIQHLKSK 1510
Cdd:PRK13641 177 DPEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL-----IKHASPK 230
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
483-692 |
2.84e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSG--LSPPTTGSVTIYNQTVSE---------- 550
Cdd:COG2401 31 LEAFGVELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGReaslidaigr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 551 MDDSDAVLTITGVCPQSNVQFGFLTVREnlrlfakikgilpheveqevqqvlqdlemeniqdilaqnLSGGQKRKLTLGI 630
Cdd:COG2401 109 KGDFKDAVELLNAVGLSDAVLWLRRFKE---------------------------------------LSTGQKFRFRLAL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 631 AILGDPQVLLLDEPTAGLDPLSRHRI-WNLLKE-RRAGRVIVFSTQFMD-EADILADRKVFISNG 692
Cdd:COG2401 150 LLAERPKLLVIDEFCSHLDRQTAKRVaRNLQKLaRRAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
481-699 |
3.09e-10 |
|
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: 61.39 E-value: 3.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLS--PPTTGSVTIYNQTVSEMDDSDAVL 558
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 559 TITGVCPQSNVQFGFLTVRENLRLfakikgilpheveqevqqvlqdlemeniqdiLAQNLSGGQKRKLTLGIAILGDPQV 638
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLRY-------------------------------VNEGFSGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 639 LLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEAD-ILADRKVFISNGRLKCAGS 699
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1309-1503 |
3.96e-10 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 64.42 E-value: 3.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---------------SgggaalgflgYCPQENVLW 1373
Cdd:COG1132 357 KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdltleslrrqiG----------VVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 pNLTVKEHLeLYAavkglkKKDA----VVTITRLVNA----LKLQDHLKALV----RTLSEGVKRKLCFVLSILGNPPVV 1441
Cdd:COG1132 427 -SGTIRENI-RYG------RPDAtdeeVEEAAKAAQAhefiEALPDGYDTVVgergVNLSGGQRQRIAIARALLKDPPIL 498
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1442 LLDEPSTGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGS 1503
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
470-649 |
4.10e-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: 64.42 E-value: 4.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 470 PVSPEFQGKEAIRIKNLKKEYSGKHGKVEAlrglGfDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvs 549
Cdd:COG1245 331 APRREKEEETLVEYPDLTKSYGGFSLEVEG----G-EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 550 emddsDAVLTITgVCPQSNVQFGFLTVRENLRlfAKIKGILPHEVEQEvqQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:COG1245 398 -----DEDLKIS-YKPQYISPDYDGTVEEFLR--SANTDDFGSSYYKT--EIIKPLGLEKLLDKNVKDLSGGELQRVAIA 467
|
170 180
....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLD 649
Cdd:COG1245 468 ACLSRDADLYLLDEPSAHLD 487
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1309-1478 |
4.19e-10 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 59.38 E-value: 4.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVflkgsgggaalgflgycpqenvlwpnltvkehlelyaav 1388
Cdd:cd03221 17 KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV--------------------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 kglkKKDAVVTItrlvnalklqdhlkALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQqqmwQAIRATFTN 1468
Cdd:cd03221 58 ----TWGSTVKI--------------GYFEQLSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESI----EALEEALKE 115
|
170
....*....|
gi 153792543 1469 TERGALLTTH 1478
Cdd:cd03221 116 YPGTVILVSH 125
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
484-690 |
4.26e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 63.06 E-value: 4.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYS------GKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAV 557
Cdd:PRK11308 9 IDLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTitgvcpQSNVQ------FGFLTVREnlrlfaKIKGILpheveQEVQQVLQDL----EMENIQDILAQ----------- 616
Cdd:PRK11308 89 LL------RQKIQivfqnpYGSLNPRK------KVGQIL-----EEPLLINTSLsaaeRREKALAMMAKvglrpehydry 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 617 --NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLlkerragrvivfstqFMDEADILADRKVFIS 690
Cdd:PRK11308 152 phMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNL---------------MMDLQQELGLSYVFIS 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1295-1498 |
4.47e-10 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 63.17 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1295 TKRcFSKMKKKI-ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaalgflgycpQE---- 1369
Cdd:COG1135 8 SKT-FPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDG--------------VDltal 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1370 -------------------NVLWpNLTVKEH----LELyaavKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVK- 1425
Cdd:COG1135 73 serelraarrkigmifqhfNLLS-SRTVAENvalpLEI----AGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKq 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1426 -----RKLCfvlsilGNPPVVLLDEPSTGMDPEGQQQMWQAIRAtfTNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG1135 148 rvgiaRALA------NNPKVLLCDEATSALDPETTRSILDLLKD--INRELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1304-1498 |
5.12e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 61.72 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMIT--GDTIP---TAGQVFLKGSGGgaalgflgYCPQENVL------ 1372
Cdd:PRK14239 17 KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGHNI--------YSPRTDTVdlrkei 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 -----WPN---LTVKEHLELYAAVKGLKKK---DAVVTiTRLVNAL---KLQDHLKALVRTLSEGVKRKLCFVLSILGNP 1438
Cdd:PRK14239 89 gmvfqQPNpfpMSIYENVVYGLRLKGIKDKqvlDEAVE-KSLKGASiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1439 PVVLLDEPSTGMDPEGQQQmwqaIRATFTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK14239 168 KIILLDEPTSALDPISAGK----IEETLLGLKDDytMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
465-705 |
5.84e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.61 E-value: 5.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 465 NDSLEPVSPefqgkeAIRIKNLKKEYSGKHGKvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSG-LSPPTTGSVTI 543
Cdd:PLN03232 605 NPPLQPGAP------AISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 544 YNQTvsemddsdavltitGVCPQSNVQFGfLTVRENLrLFAKikgilPHEVEQ-----EVQQVLQDLEMENIQDIL---- 614
Cdd:PLN03232 678 RGSV--------------AYVPQVSWIFN-ATVRENI-LFGS-----DFESERywraiDVTALQHDLDLLPGRDLTeige 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 615 -AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWN-LLKERRAGRVIVFST---QFMDeadiLADRKVFI 689
Cdd:PLN03232 737 rGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTnqlHFLP----LMDRIILV 812
|
250
....*....|....*.
gi 153792543 690 SNGRLKCAGSSLFLKK 705
Cdd:PLN03232 813 SEGMIKEEGTFAELSK 828
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1307-1512 |
6.16e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 63.69 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGsgggaaLGFLGYCpqENVLWPNLTV-------- 1378
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNG------QPIADYS--EAALRQAISVvsqrvhlf 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 ----KEHLELYAAvkglKKKDAvvtitRLVNALK---LQDHL---KALV-------RTLSEGVKRKLCFVLSILGNPPVV 1441
Cdd:PRK11160 427 satlRDNLLLAAP----NASDE-----ALIEVLQqvgLEKLLeddKGLNawlgeggRQLSGGEQRRLGIARALLHDAPLL 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1442 LLDEPSTGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:PRK11160 498 LLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
500-674 |
6.99e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 60.35 E-value: 6.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVsemdDSDA---------VLTITGVCPqsnvq 570
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLctyqkqlcfVGHRSGINP----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 571 fgFLTVRENLrLFakikGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK13540 88 --YLTLRENC-LY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*.
gi 153792543 651 LSRHRIWNLLKERRA--GRVIVFSTQ 674
Cdd:PRK13540 161 LSLLTIITKIQEHRAkgGAVLLTSHQ 186
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1307-1528 |
7.16e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 61.93 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENVLWPN-------LTVK 1379
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpetqfvgRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 EHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMW 1459
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1460 QAIRATFtntERGALL--TTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLlemKVKTPSQVE 1528
Cdd:PRK13644 177 ERIKKLH---EKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQTL---GLTPPSLIE 240
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1307-1503 |
7.29e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 61.95 E-value: 7.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF------------LKGSGGGAALGFLGYCPQENVLWP 1374
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdyaipanlkkIKEVKRLRKEIGLVFQFPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NlTVKEHLELYAAVKGLKKKDAVVTITRLVNALKL-QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:PRK13645 106 E-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1305-1528 |
8.10e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 8.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKgsgggaalgflgycpqENVLWPNLTVKEhlel 1384
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIG----------------ERVITAGKKNKK---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 yaaVKGLKKKDAVV-----------TITRLV------------NALKLQDHLKALVrTLSEGVKRKLCFVLS-------- 1433
Cdd:PRK13634 80 ---LKPLRKKVGIVfqfpehqlfeeTVEKDIcfgpmnfgvseeDAKQKAREMIELV-GLPEELLARSPFELSggqmrrva 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1434 ILG----NPPVVLLDEPSTGMDPEGQQQMWQairaTFTNTERGALLT----THYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1505
Cdd:PRK13634 156 IAGvlamEPEVLVLDEPTAGLDPKGRKEMME----MFYKLHKEKGLTtvlvTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
250 260
....*....|....*....|...
gi 153792543 1506 HLKSKfgKDYLLEMKVKTPSQVE 1528
Cdd:PRK13634 232 EIFAD--PDELEAIGLDLPETVK 252
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
493-656 |
8.58e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.38 E-value: 8.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 493 KHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSG-LSPP-------TTGSVTIYNQTVSEMdDSDAVLTITGVC 564
Cdd:PRK13547 12 RHRAI--LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGgaprgarVTGDVTLNGEPLAAI-DAPRLARLRAVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 565 PQ-SNVQFGFlTVRENLRL----FAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAI------- 632
Cdd:PRK13547 89 PQaAQPAFAF-SAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180
....*....|....*....|....*.
gi 153792543 633 --LGDPQVLLLDEPTAGLDPLSRHRI 656
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRL 193
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1310-1463 |
9.37e-10 |
|
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: 59.95 E-value: 9.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKST---------TISMITGDtiptagqVFLKGSGGGAALGFLG-YCPQENVLWPNLTVK 1379
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTlldvlagrkTAGVITGE-------ILINGRPLDKNFQRSTgYVEQQDVHSPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 EHLELYAAVKGLkkkdavvtitrlvnalklqdhlkalvrTLSEgvKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMW 1459
Cdd:cd03232 98 EALRFSALLRGL---------------------------SVEQ--RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
....
gi 153792543 1460 QAIR 1463
Cdd:cd03232 149 RFLK 152
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
480-649 |
9.42e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.20 E-value: 9.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLkkEYSGKHGKVeALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMddSDAVLT 559
Cdd:PRK10790 340 RIDIDNV--SFAYRDDNL-VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL--SHSVLR 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 iTGVC--PQSNVQFGfLTVRENLRLFAKIKgilphevEQEVQQVLQDLEM--------ENIQDILAQ---NLSGGQKRKL 626
Cdd:PRK10790 415 -QGVAmvQQDPVVLA-DTFLANVTLGRDIS-------EEQVWQALETVQLaelarslpDGLYTPLGEqgnNLSVGQKQLL 485
|
170 180
....*....|....*....|...
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANID 508
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1307-1497 |
1.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 60.90 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGaalgflgycpQENVLW-----------PN 1375
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN----------AENEKWvrskvglvfqdPD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 -----LTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:PRK13647 90 dqvfsSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1451 DPEGQQQMwQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:PRK13647 170 DPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGR 215
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1309-1498 |
1.28e-09 |
|
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: 60.18 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGY-----CPQENVLWPNlTVKEHLE 1383
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHskvslVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKGLKK-KDAVVTITRLVNALKLQDHLKALV----RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:cd03248 110 YGLQSCSFECvKEAAQKAHAHSFISELASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQV 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 153792543 1459 WQAIRAtfTNTERGALLTTHYMAEAEAVcDRVAIMVSGRL 1498
Cdd:cd03248 190 QQALYD--WPERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
505-649 |
1.33e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 505 FDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtIYNQ--TVS--EMDdsdavltitgvcPQSNVQ---FGFLT-- 575
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-IYEQdlIVArlQQD------------PPRNVEgtvYDFVAeg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 576 VRE----------------------NLRLFAKIKGILPHE----VEQEVQQVLQDLEMEniQDILAQNLSGGQKRKLTLG 629
Cdd:PRK11147 91 IEEqaeylkryhdishlvetdpsekNLNELAKLQEQLDHHnlwqLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALG 168
|
170 180
....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLD 649
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLD 188
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
481-678 |
1.40e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVS---EMDDSDAV 557
Cdd:PRK10762 5 LQLKGIDKAFPG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 LTIT----GVCPQsnvqfgfLTVRENL---RLFAKIKG-ILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLG 629
Cdd:PRK10762 81 IGIIhqelNLIPQ-------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRA-GRVIVFSTQFMDE 678
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSqGRGIVYISHRLKE 203
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
985-1181 |
1.45e-09 |
|
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: 61.64 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 985 LMDIISNGLLGIFNSSERIQTDRSTVFEEHMLYEYGFMSnAFFWIPVAASLTpYIAMGSISDHKKKVLSQLWTSGLYPSA 1064
Cdd:pfam12698 127 LNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVG-LILMIIILIGAA-IIAVSIVEEKESRIKERLLVSGVSPLQ 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1065 YWCGQALVDIPIYFLILFLMQIMdsVFSseEFISVMESLLIqIPCSIGYASSLIFMTYVISFIFRNGRKNSGIWSFFFLI 1144
Cdd:pfam12698 205 YWLGKILGDFLVGLLQLLIILLL--LFG--IGIPFGNLGLL-LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILL 279
|
170 180 190
....*....|....*....|....*....|....*..
gi 153792543 1145 VTIFFIIATDINeyGFLELLICTFLVPPFTLIGSLLI 1181
Cdd:pfam12698 280 LSGFFGGLFPLE--DPPSFLQWIFSIIPFFSPIDGLL 314
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1294-1513 |
1.93e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.82 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1294 RTKRCFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDT----IPTAGQVFLKG----SGGGAALGFLGY 1365
Cdd:TIGR00956 63 RKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDGitpeEIKKHYRGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1366 CPQENVLWPNLTVKEHLELYAA-------VKGLKKKDAVVTITRLVNALKLQDHLK------ALVRTLSEGVKRKLCFVL 1432
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMATYGLSHTRntkvgnDFVRGVSGGERKRVSIAE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1433 SILGNPPVVLLDEPSTGMDPEGQQQMWQAIR--ATFTNTergALLTTHYMAEAEA--VCDRVAIMVSGRLRCIGSIQHLK 1508
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKtsANILDT---TPLVAIYQCSQDAyeLFDKVIVLYEGYQIYFGPADKAK 299
|
....*
gi 153792543 1509 SKFGK 1513
Cdd:TIGR00956 300 QYFEK 304
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
503-650 |
2.14e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 2.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 503 LGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSD--AVLTITGVCPQSnvqfgfLTVRENL 580
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRfmAYLGHLPGLKAD------LSTLENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 581 RLFAKIKGILPhevEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:PRK13543 104 HFLCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
480-649 |
2.20e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.83 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 480 AIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvSEmddsDAVLt 559
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----SE----NANI- 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 560 itGVCPQ-SNVQF-GFLTVRENLRLFAKikgilPHEVEQEVQQVLQDLEMENiQDIL--AQNLSGGQKRKLTLGIAILGD 635
Cdd:PRK15064 385 --GYYAQdHAYDFeNDLTLFDWMSQWRQ-----EGDDEQAVRGTLGRLLFSQ-DDIKksVKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....
gi 153792543 636 PQVLLLDEPTAGLD 649
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
445-700 |
2.37e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 445 KRRGASHVVLENEIDSDPS--LNDSLEPVSPEFQGKEAIRIKNLKKEYSGKHGKVEA-----LRGLGFDIYEGQITALLG 517
Cdd:PTZ00243 614 KRHPSPSVVVEDTDYGSPSsaSRHIVEGGTGGGHEATPTSERSAKTPKMKTDDFFELepkvlLRDVSVSVPRGKLTVVLG 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 518 HSGAGKTTLINTLSGLSPPTTGSVTiynqtvsemddsdAVLTITGVCPQSNVQFGflTVRENLRLF-----AKI-KGILP 591
Cdd:PTZ00243 694 ATGSGKSTLLQSLLSQFEISEGRVW-------------AERSIAYVPQQAWIMNA--TVRGNILFFdeedaARLaDAVRV 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 592 HEVEQEVQQVLQDLEMEnIQDiLAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIW-NLLKERRAGRVIV 670
Cdd:PTZ00243 759 SQLEADLAQLGGGLETE-IGE-KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVVeECFLGALAGKTRV 836
|
250 260 270
....*....|....*....|....*....|..
gi 153792543 671 FSTQfmdEADIL--ADRKVFISNGRLKCAGSS 700
Cdd:PTZ00243 837 LATH---QVHVVprADYVVALGDGRVEFSGSS 865
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1309-1503 |
2.56e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 58.96 E-value: 2.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTIS-------------MITGDTIPTAGQVFLKGSGGGAalgflgycPQENVLWPN 1375
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILalfrfleaeegkiEIDGIDISTIPLEDLRSSLTII--------PQDPTLFSG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 lTVKEHLELYAavkglKKKDAvvtitRLVNALKLqdhlKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03369 97 -TIRSNLDPFD-----EYSDE-----EIYGALRV----SEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153792543 1456 QQMWQAIRATFTNTergALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:cd03369 162 ALIQKTIREEFTNS---TILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
481-694 |
2.64e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 59.71 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEysgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPP----TTGSVTIYNQTVSEMD-DSD 555
Cdd:PRK10418 5 IELRNIALQ-----AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCAlRGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 556 AVLTItgvcpQSNVQFGF---LTVRENLRLFAKIKGILPheVEQEVQQVLQDLEMENIQDIL---AQNLSGGQKRKLTLG 629
Cdd:PRK10418 80 KIATI-----MQNPRSAFnplHTMHTHARETCLALGKPA--DDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 630 IAILGDPQVLLLDEPTAGLDPLSRHRIWNLL----KERRAGRVIVfsTQFMDEADILADRKVFISNGRL 694
Cdd:PRK10418 153 LALLCEAPFIIADEPTTDLDVVAQARILDLLesivQKRALGMLLV--THDMGVVARLADDVAVMSHGRI 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1309-1451 |
3.05e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 59.06 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG---------YCPQENVLWPNLTVK 1379
Cdd:PRK11629 26 HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnqklgFIYQFHHLLPDFTAL 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1380 EHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:PRK11629 106 ENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1311-1498 |
4.40e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 4.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAalgflgycpqENVlWpNL-------------- 1376
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA----------ENV-W-NLrrkigmvfqnpdnq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 ----TVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDP 1452
Cdd:PRK13642 94 fvgaTVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 1453 EGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSGRL 1498
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1305-1483 |
4.70e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 58.94 E-value: 4.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENVLWPNLTVKEHLEL 1384
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGVVFQNEGLLPWRNVQDNVAF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 YAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:PRK11248 94 GLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLK 173
|
170
....*....|....*....
gi 153792543 1465 TFTNTERGALLTTHYMAEA 1483
Cdd:PRK11248 174 LWQETGKQVLLITHDIEEA 192
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1309-1478 |
4.71e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 58.04 E-value: 4.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSG----GGAALGFLGYCPQENVLWPNLTVKEHLeL 1384
Cdd:PRK13540 18 QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikkdLCTYQKQLCFVGHRSGINPYLTLRENC-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 YaavkGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:PRK13540 97 Y----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQE 172
|
170
....*....|....*
gi 153792543 1465 tfTNTERGA-LLTTH 1478
Cdd:PRK13540 173 --HRAKGGAvLLTSH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1309-1517 |
4.80e-09 |
|
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: 58.71 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNlTVKEHLe 1383
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLrsqigLVSQEPVLFDG-TIAENI- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 lyaavkGLKKKDA----VVTITRLVNA----LKLQDHLKALV----RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:cd03249 98 ------RYGKPDAtdeeVEEAAKKANIhdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1452 PEGQQQMWQAI------RATFTNTERgaLLTTHYmaeaeavCDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1517
Cdd:cd03249 172 AESEKLVQEALdramkgRTTIVIAHR--LSTIRN-------ADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1307-1498 |
4.97e-09 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 58.35 E-value: 4.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF--------LKGSGGGAALGFLGYCPQENVLWPNLTV 1378
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghditrLKNREVPFLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD---PEGQ 1455
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDdalSEGI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 153792543 1456 QQMWQairaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK10908 177 LRLFE----EFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1309-1498 |
5.14e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.94 E-value: 5.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIP----TAGQVFLKGsgggaalgfLGYCPQE--------------N 1370
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDG---------KPVAPCAlrgrkiatimqnprS 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1371 VLWPNLTVKEHLELYAAVKGLKKKDAvvTITRLVNALKLQDHLKALVR---TLSEGVKRKLCFVLSILGNPPVVLLDEPS 1447
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDA--TLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1448 TGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
470-649 |
5.20e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.98 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 470 PVSPEFQGKEAIRIKNLKKEYSGKHGKVEAlrglGFdIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvs 549
Cdd:PRK13409 330 PPRDESERETLVEYPDLTKKLGDFSLEVEG----GE-IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 550 emddsDAVLTITgVCPQ--SNVQFGflTVRENLRlfaKIKGIL---PHEVEqevqqVLQDLEMENIQDILAQNLSGGQKR 624
Cdd:PRK13409 397 -----DPELKIS-YKPQyiKPDYDG--TVEDLLR---SITDDLgssYYKSE-----IIKPLQLERLLDKNVKDLSGGELQ 460
|
170 180
....*....|....*....|....*
gi 153792543 625 KLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK13409 461 RVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
470-694 |
5.51e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 60.76 E-value: 5.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 470 PVSPEFQGKEAIRIKNLKKEYsgkHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVS 549
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 550 EMDdsdavltitgvcpQSNVQFGFLTVRENLRLFAKIKGILPHEVEQE-VQQVLQDLEMEN---IQD--ILAQNLSGGQK 623
Cdd:PRK10522 389 AEQ-------------PEDYRKLFSAVFTDFHLFDQLLGPEGKPANPAlVEKWLERLKMAHkleLEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 624 RKLTLGIAILGDPQVLLLDEPTAGLDPLSRhRIW--NLLKERRAGRVIVFSTQFMDEADILADRKVFISNGRL 694
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFR-REFyqVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
481-673 |
5.88e-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: 60.47 E-value: 5.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTtlINTLS--GLSPP----TTGSVTIYNQTVSEMDDS 554
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKS--VTALSilRLLPDpaahPSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 555 DA---------------------VLTItgvCPQsnvqfgfltVRENLRLfakIKGILPHEVEQEVQQVLQDLEMENIQDI 613
Cdd:COG4172 85 ELrrirgnriamifqepmtslnpLHTI---GKQ---------IAEVLRL---HRGLSGAAARARALELLERVGIPDPERR 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 614 LAQ---NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFST 673
Cdd:COG4172 150 LDAyphQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDlqRELGMALLLIT 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1309-1497 |
6.08e-09 |
|
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: 57.86 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgfLGYCPQENvlW-PNLTVKEHL----- 1382
Cdd:cd03250 22 KDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------IAYVSQEP--WiQNGTIRENIlfgkp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ---ELYAAVkglkkkdavvtitrlVNALKLQDHLKALVR-----------TLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:cd03250 92 fdeERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 153792543 1449 GMDPE-GQQQMWQAIRATFTNtERGALLTTHYMAEAEAvCDRVAIMVSGR 1497
Cdd:cd03250 157 AVDAHvGRHIFENCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
470-699 |
7.10e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 60.64 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 470 PVSPEFQGKEAIRIKNLKKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI------ 543
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 544 --YNQTVSEMDDSDAVL-TITGVC-------PQSNVQFGFLT---VRENLRLFakiKGILPHEVEQEVQQVLQDLEMENI 610
Cdd:PRK10261 82 rrSRQVIELSEQSAAQMrHVRGADmamifqePMTSLNPVFTVgeqIAESIRLH---QGASREEAMVEAKRMLDQVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 611 QDILAQ---NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK--ERRAGRVIVFSTQFMDEADILADR 685
Cdd:PRK10261 159 QTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIADR 238
|
250
....*....|....
gi 153792543 686 KVFISNGRLKCAGS 699
Cdd:PRK10261 239 VLVMYQGEAVETGS 252
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1311-1451 |
8.41e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.02 E-value: 8.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGdTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTVKEHLELY 1385
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELarhraYLSQQQTPPFAMPVFQYLTLH 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1386 AAVkGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSIL-----GNP--PVVLLDEPSTGMD 1451
Cdd:PRK03695 94 QPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1307-1498 |
1.13e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 58.71 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLK----GSGGGAALGFLGYCPQ-------------- 1368
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSKkiknfkelrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1369 -----ENVLWPNlTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLkaLVRT---LSEGVKRKLCF--VLSIlgNP 1438
Cdd:PRK13631 121 vfqfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSY--LERSpfgLSGGQKRRVAIagILAI--QP 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1439 PVVLLDEPSTGMDPEGQQQMWQAIRATFTNtERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1309-1498 |
1.25e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 59.63 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAAlgflgyCPQENV---------------LW 1373
Cdd:PRK10762 269 NDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTR------SPQDGLangivyisedrkrdgLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHLELYA------AVKGLKKKDAVVTITRLVNALKLQD-HLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:PRK10762 343 LGMSVKENMSLTAlryfsrAGGSLKHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1447 STGMDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK10762 423 TRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
479-670 |
1.42e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.44 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGK--H--GKVealrglGFDIY------EGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtv 548
Cdd:PRK13409 64 DAISIVNLPEELEEEpvHryGVN------GFKLYglpipkEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY------- 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 549 SEMDDSDAVLT-ITGvcpqSNVQFGFLTVRENlrlfaKIKGIL-PHEVEQ--------------------EVQQVLQDLE 606
Cdd:PRK13409 131 EEEPSWDEVLKrFRG----TELQNYFKKLYNG-----EIKVVHkPQYVDLipkvfkgkvrellkkvdergKLDEVVERLG 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 607 MENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR-VIV 670
Cdd:PRK13409 202 LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKyVLV 266
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1306-1497 |
1.43e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 57.69 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAAlgflgycPQENV-------------L 1372
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-------PGHQIarmgvvrtfqhvrL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKE------HLELYAAV-KGLKK--------KDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGN 1437
Cdd:PRK11300 92 FREMTVIEnllvaqHQQLKTGLfSGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1438 PPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
481-693 |
1.54e-08 |
|
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: 59.07 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIY-------NQTVSEMDD 553
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsgsplkASNIRDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 554 SDAVltitgVCPQSNVQFGFLTVRENLRLFAKI--KGILPH--EVEQEVQQVLQDLEMENIQDILA-QNLSGGQKRKLTL 628
Cdd:TIGR02633 78 AGIV-----IIHQELTLVPELSVAENIFLGNEItlPGGRMAynAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 629 GIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
481-672 |
1.59e-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: 57.56 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSgkHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPpTTGSVTIYN---QTVSEMDDSDAV 557
Cdd:cd03289 3 MTVKDLTAKYT--EGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGvswNSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 ltitGVCPQSNVQFGFlTVRENLRLFAKIKgilphevEQEVQQVLQDLEMENIQDILAQNL-----------SGGQKRKL 626
Cdd:cd03289 80 ----GVIPQKVFIFSG-TFRKNLDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 627 TLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFS 672
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILS 193
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1284-1513 |
1.61e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 57.77 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1284 ASCLRKEYigRTKRCFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL 1363
Cdd:PRK10419 6 VSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1364 GYCPQENV----------LWPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQD-HLKALVRTLSEGVKRKLCFV 1431
Cdd:PRK10419 84 RKAFRRDIqmvfqdsisaVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1432 LSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL---RCIGSIQHLK 1508
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFS 243
|
....*
gi 153792543 1509 SKFGK 1513
Cdd:PRK10419 244 SPAGR 248
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1307-1507 |
1.73e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 57.33 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTI----SMITGDTIPTAgQVFLKGSGGG----------AALGFLGYCPQENVL 1372
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGS-HIELLGRTVQregrlardirKSRANTGYIFQQFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKEHLELYAavkgLKKKDAVVTITRLVNALKLQDHLKALVR------------TLSEGVKRKLCFVLSILGNPPV 1440
Cdd:PRK09984 98 VNRLSVLENVLIGA----LGSTPFWRTCFSWFTREQKQRALQALTRvgmvhfahqrvsTLSGGQQQRVAIARALMQQAKV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1441 VLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:PRK09984 174 ILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
500-649 |
1.82e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 1.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDaVLTITGVCPQSNVQFGFlTVREN 579
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LRLFAkikgilphevEQEVQQVLQDLEMENIQDIL--------------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPT 645
Cdd:PLN03232 1330 IDPFS----------EHNDADLWEALERAHIKDVIdrnpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDEAT 1399
|
....
gi 153792543 646 AGLD 649
Cdd:PLN03232 1400 ASVD 1403
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1304-1498 |
2.66e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.12 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENV--LWPN------ 1375
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREKVgiVFQNpdnqfv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 -LTVKEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCfVLSILG-NPPVVLLDEPSTGMDPE 1453
Cdd:PRK13640 99 gATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEaVCDRVAIMVSGRL 1498
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
463-699 |
2.79e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 463 SLNDSLEPVSPefqgkeAIRIKNLKKEYSGKhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVT 542
Cdd:PLN03130 603 LPNPPLEPGLP------AISIKNGYFSWDSK-AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 543 IYNQTVSEMddsdavltitgvcPQSNVQFGfLTVRENLrLFAkikgiLPHEVEQ-----EVQQVLQDLEMENIQDIL--- 614
Cdd:PLN03130 676 VIRGTVAYV-------------PQVSWIFN-ATVRDNI-LFG-----SPFDPERyeraiDVTALQHDLDLLPGGDLTeig 735
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 615 --AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP-LSRHRIWNLLKE--RRAGRVIVFST-QFMDEadilADRKVF 688
Cdd:PLN03130 736 erGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDelRGKTRVLVTNQlHFLSQ----VDRIIL 811
|
250
....*....|.
gi 153792543 689 ISNGRLKCAGS 699
Cdd:PLN03130 812 VHEGMIKEEGT 822
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
466-649 |
2.97e-08 |
|
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: 58.80 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 466 DSLE--PVSPefQGKEAIRIKNlkKEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGlsppttgsvti 543
Cdd:TIGR00957 622 DSIErrTIKP--GEGNSITVHN--ATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA----------- 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 544 ynqtvsEMDDSDAVLTITG----VCPQSNVQFGflTVRENLrLFAKikGILPHEVEQEVQQ--VLQDLEMENIQDIL--- 614
Cdd:TIGR00957 687 ------EMDKVEGHVHMKGsvayVPQQAWIQND--SLRENI-LFGK--ALNEKYYQQVLEAcaLLPDLEILPSGDRTeig 755
|
170 180 190
....*....|....*....|....*....|....*..
gi 153792543 615 --AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:TIGR00957 756 ekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
483-672 |
2.98e-08 |
|
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: 58.77 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKHGKVeaLRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPpTTGSVTIynqtvsemdDSDAVLTIT- 561
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQI---------DGVSWNSVTl 1287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 562 -------GVCPQSNVQFGFlTVRENLRlfakikgilPHE--VEQEVQQVLQDLEMENIQDILAQNL-----------SGG 621
Cdd:TIGR01271 1288 qtwrkafGVIPQKVFIFSG-TFRKNLD---------PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNG 1357
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 622 QKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFS 672
Cdd:TIGR01271 1358 HKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILS 1408
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
479-695 |
3.39e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 56.75 E-value: 3.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEY----------------SGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVT 542
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 543 IYNQTvsemddsdAVLTITGVCPqsnvqfGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQ 622
Cdd:PRK13546 83 RNGEV--------SVIAISAGLS------GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 623 KRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIVFSTQFMDEADILADRKVFISNGRLK 695
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEfKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
500-649 |
3.97e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.60 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDaVLTITGVCPQSNVQFGFlTVREN 579
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-LRKVLGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LRLFAkikgilphevEQEVQQVLQDLEMENIQDIL--------------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPT 645
Cdd:PLN03130 1333 LDPFN----------EHNDADLWESLERAHLKDVIrrnslgldaevseaGENFSVGQRQLLSLARALLRRSKILVLDEAT 1402
|
....
gi 153792543 646 AGLD 649
Cdd:PLN03130 1403 AAVD 1406
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
462-672 |
4.18e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 462 PSLNDSLEPVsPEFQGKEAIRIKnlkkEYSGKHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSV 541
Cdd:PRK10789 298 PVVKDGSEPV-PEGRGELDVNIR----QFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 542 TIYNQTVSE--MDDSDAVLTITGVCPqsnvqfgFL---TVRENLRLFAkikgilPHEVEQEVQQVLQdleMENI-QDIL- 614
Cdd:PRK10789 373 RFHDIPLTKlqLDSWRSRLAVVSQTP-------FLfsdTVANNIALGR------PDATQQEIEHVAR---LASVhDDILr 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 615 ------------AQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFS 672
Cdd:PRK10789 437 lpqgydtevgerGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIIS 506
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1307-1463 |
5.12e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGS------GGGAALGFLGYCPQENVLWPNLTVKE 1380
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKditdwqTAKIMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLelyaAVKGL--KKKDAVVTITRLVNAL-KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:PRK11614 100 NL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
....*.
gi 153792543 1458 MWQAIR 1463
Cdd:PRK11614 176 IFDTIE 181
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1309-1498 |
5.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 55.69 E-value: 5.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITG--DTIPTA---GQVFLKGSGGGAALGFLGYCPQENVLW-----PNLTV 1378
Cdd:PRK14247 20 DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKMDVIELRRRVQMVFQipnpiPNLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTiTRLVNALK-------LQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:PRK14247 100 FENVALGLKLNRLVKSKKELQ-ERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1452 PEGQQQmwqaIRATF--TNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK14247 179 PENTAK----IESLFleLKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1304-1536 |
5.39e-08 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 55.79 E-value: 5.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG-----SGGGAALGFLGYCPQENVLWPNLTV 1378
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpismLSSRQLARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KE--------HLELYAAvkgLKKKDavvtiTRLVNALKLQDHLKALV-RTLSE--GVKRKLCFVLSILG-NPPVVLLDEP 1446
Cdd:PRK11231 94 RElvaygrspWLSLWGR---LSAED-----NARVNQAMEQTRINHLAdRRLTDlsGGQRQRAFLAMVLAqDTPVVLLDEP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1447 STGMDPEGQQQMWQAIRAtfTNTERGALLTT-HYMAEAEAVCDRVAIMVSGRLRCIGSIQhlkskfgkdyllemKVKTPS 1525
Cdd:PRK11231 166 TTYLDINHQVELMRLMRE--LNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGTPE--------------EVMTPG 229
|
250
....*....|....
gi 153792543 1526 ---QVEPLNTEIMR 1536
Cdd:PRK11231 230 llrTVFDVEAEIHP 243
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1309-1517 |
5.79e-08 |
|
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: 55.31 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGS-----GGGAALGFLGYCPQENVLWpNLTVKEHLe 1383
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHdvrdyTLASLRRQIGLVSQDVFLF-NDTVAENI- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKGlkKKDAVVTITRLVNAL----KLQDHLKALV----RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQ 1455
Cdd:cd03251 97 AYGRPGA--TREEVEEAARAANAHefimELPEGYDTVIgergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1456 QQMWQAIRATFTNteRGALLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFGKDYLL 1517
Cdd:cd03251 175 RLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1409-1509 |
6.27e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 6.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1409 LQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTErgALLTTHYMAEAEAVCD 1488
Cdd:PRK14271 153 VKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNLAQAARISD 230
|
90 100
....*....|....*....|.
gi 153792543 1489 RVAIMVSGRLRCIGSIQHLKS 1509
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQLFS 251
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1298-1512 |
6.77e-08 |
|
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: 55.31 E-value: 6.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1298 CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVL 1372
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLrraigVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WpNLTVKEHL----------ELYAAVKGLKKKDAVvtitrlvnaLKLQDHLKALV--R--TLSEGVKRKLCFVLSILGNP 1438
Cdd:cd03253 87 F-NDTIGYNIrygrpdatdeEVIEAAKAAQIHDKI---------MRFPDGYDTIVgeRglKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1439 PVVLLDEPSTGMDPEGQQQMWQAIRATFTNteRGALLTTHYMAEAeAVCDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGG 227
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
483-649 |
6.80e-08 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 55.42 E-value: 6.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYsgkhGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGlSPP---TTGSVTIYNQTVSEMDDSDAV-- 557
Cdd:CHL00131 10 IKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGESILDLEPEERAhl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 ---------LTITGVcpqSNVQFGFLTVRENlRLFAKIKGILPHEVEQEVQQVLQDLEMEniQDILAQNL----SGGQ-K 623
Cdd:CHL00131 85 giflafqypIEIPGV---SNADFLRLAYNSK-RKFQGLPELDPLEFLEIINEKLKLVGMD--PSFLSRNVnegfSGGEkK 158
|
170 180
....*....|....*....|....*.
gi 153792543 624 RKLTLGIAILgDPQVLLLDEPTAGLD 649
Cdd:CHL00131 159 RNEILQMALL-DSELAILDETDSGLD 183
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1306-1451 |
6.81e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 55.23 E-value: 6.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATR--NISFCVKKGEVLGLLGHNGAGKSTTISMITGdTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLWPNLTV 1378
Cdd:COG4138 8 VAGRlgPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELarhraYLSQQQSPPFAMPV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAvKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSIL-----GNPP--VVLLDEPSTGMD 1451
Cdd:COG4138 87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
484-648 |
6.94e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 484 KNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIY----NQTVSEMDDSDAV-- 557
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeELQASNIRDTERAgi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 ------LTITgvcPQsnvqfgfLTVRENLRLFAKI--KGILPH-EVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTL 628
Cdd:PRK13549 85 aiihqeLALV---KE-------LSVLENIFLGNEItpGGIMDYdAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180
....*....|....*....|
gi 153792543 629 GIAILGDPQVLLLDEPTAGL 648
Cdd:PRK13549 155 AKALNKQARLLILDEPTASL 174
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1315-1492 |
7.02e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 54.12 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTagqvflkgsgggaalgflgycpQENVLWPNLTVkehlelyaAVKGLKKK 1394
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN----------------------GDNDEWDGITP--------VYKPQYID 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1395 davvtitrlvnalklqdhlkalvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGAL 1474
Cdd:cd03222 72 -------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126
|
170
....*....|....*...
gi 153792543 1475 LTTHYMAEAEAVCDRVAI 1492
Cdd:cd03222 127 VVEHDLAVLDYLSDRIHV 144
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
481-656 |
9.14e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 481 IRIKNLKKEYSGKHgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI----------------- 543
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIndshnlkdinlkwwrsk 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 544 -----------------------------------YNQ-TVSEMDDSDAVLTITGVCP-------QSNVQFGFLTVRENL 580
Cdd:PTZ00265 462 igvvsqdpllfsnsiknnikyslyslkdlealsnyYNEdGNDSQENKNKRNSCRAKCAgdlndmsNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 581 RLFAKI------KGILPHEVEQEVQQVLQDLEMENiqdilAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRH 654
Cdd:PTZ00265 542 QTIKDSevvdvsKKVLIHDFVSALPDKYETLVGSN-----ASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEY 616
|
..
gi 153792543 655 RI 656
Cdd:PTZ00265 617 LV 618
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1307-1496 |
9.71e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 55.27 E-value: 9.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG--SGGGAALGFLGYCPQ-ENVLWPNLTVKEHLE 1383
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQALQKNLVAYVPQsEEVDWSFPVLVEDVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 L---YAAVKGL---KKKDAVVtITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:PRK15056 102 MmgrYGHMGWLrraKKRDRQI-VTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEAR 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 153792543 1458 MWQAIRaTFTNTERGALLTTHYMAEAEAVCDrVAIMVSG 1496
Cdd:PRK15056 181 IISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
470-649 |
9.98e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 56.48 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 470 PVSPEFqGKEAIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTI------ 543
Cdd:TIGR03719 313 PPGPRL-GDKVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgetvkl 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 544 --YNQTVSEMDDSDAV----------LTITGVCPQSNV---QFGFltvrenlrlfakiKGilpheveqevqqvlQDleme 608
Cdd:TIGR03719 388 ayVDQSRDALDPNKTVweeisggldiIKLGKREIPSRAyvgRFNF-------------KG--------------SD---- 436
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 153792543 609 niQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:TIGR03719 437 --QQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1315-1494 |
1.06e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF--LKGSgggaalgflgYCPQENVLWPNLTVKEHleLYAAVKglK 1392
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDedLKIS----------YKPQYISPDYDGTVEEF--LRSANT--D 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1393 KKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERG 1472
Cdd:COG1245 429 DFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKT 508
|
170 180
....*....|....*....|..
gi 153792543 1473 ALLTTHYMAEAEAVCDRvaIMV 1494
Cdd:COG1245 509 AMVVDHDIYLIDYISDR--LMV 528
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1315-1499 |
1.06e-07 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 54.40 E-value: 1.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAA---------LGFLGYCPQENVLWPNLTVKEHLELY 1385
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeearaklrAKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1386 AAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAT 1465
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSL 192
|
170 180 190
....*....|....*....|....*....|....
gi 153792543 1466 FTNTERGALLTTHYMAEAeAVCDRVAIMVSGRLR 1499
Cdd:PRK10584 193 NREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
479-669 |
1.09e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 479 EAIRIKNLKKEYSGK--H--GKVealrglGFDIY------EGQITALLGHSGAGKTTLINTLSGLSPPTTGSvtiynqtV 548
Cdd:COG1245 64 DAISIVNLPEELEEDpvHryGEN------GFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGD-------Y 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 549 SEMDDSDAVLT-ITGvcpqSNVQFGFLTVREN-LRLFAKIKGI--LPHEVEQEVQQVL-------------QDLEMENI- 610
Cdd:COG1245 131 DEEPSWDEVLKrFRG----TELQDYFKKLANGeIKVAHKPQYVdlIPKVFKGTVRELLekvdergkldelaEKLGLENIl 206
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 611 -QDIlaQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDplsrhriwnlLKER-RAGRVI 669
Cdd:COG1245 207 dRDI--SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD----------IYQRlNVARLI 255
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1307-1528 |
1.14e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.17 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCP-----------QENVLWPN 1375
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPvrkrigmvfqfPESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 lTVKEHLELYAAVKGLKKKDAVVTITRLVNALKL-QDHLKALVRTLSEGVKRKLCFVlSILG-NPPVVLLDEPSTGMDPE 1453
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIV-SILAmNPDIIVLDEPTAGLDPQ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1454 GQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHLKSKfgKDYLLEMKVKTPSQVE 1528
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD--KKKLADWHIGLPEIVQ 252
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1311-1506 |
1.17e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------SGGGAALGFLGYCP----QENVLwPNLTVKE 1380
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpidirSPRDAIRAGIMLCPedrkAEGII-PVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLK----------KKDAVVTITRLvnALKLQDHlKALVRTLSEGVKRKlcfvlSILG-----NPPVVLLDE 1445
Cdd:PRK11288 351 NINISARRHHLRagclinnrweAENADRFIRSL--NIKTPSR-EQLIMNLSGGNQQK-----AILGrwlseDMKVILLDE 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1446 PSTGMDPEGQQQMWQAIratFTNTERG--ALLTTHYMAEAEAVCDRVAIMVSGRLRciGSIQH 1506
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVI---YELAAQGvaVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
478-667 |
1.32e-07 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 56.18 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 478 KEAIRIKNLKKEYSGKhgKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVT-----IYNQTVSEMD 552
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILldghdLRDYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 553 DSDAVLTitgvcpqSNVQFGFLTVRENLrLFAKIKGILPHEVEQ--EVQQVLQDLE-MENIQD-ILAQN---LSGGQKRK 625
Cdd:PRK11176 417 NQVALVS-------QNVHLFNDTIANNI-AYARTEQYSREQIEEaaRMAYAMDFINkMDNGLDtVIGENgvlLSGGQRQR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 626 LTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGR 667
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNR 530
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
458-661 |
1.35e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 56.25 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 458 IDSDPSLndslEPVSPEFQGKEAIRIKNLKKEYSGKHGKV-------EALRGLGFDIYEGQITALLGHSGAGKTTlintl 530
Cdd:PRK15134 257 LNSEPSG----DPVPLPEPASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKST----- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 531 SGLS----PPTTGSVTIYNQTVSEMD----------------DSDAVLTitgvcPQSNVQfgfLTVRENLRLFAKIkgIL 590
Cdd:PRK15134 328 TGLAllrlINSQGEIWFDGQPLHNLNrrqllpvrhriqvvfqDPNSSLN-----PRLNVL---QIIEEGLRVHQPT--LS 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 591 PHEVEQEVQQVLQD--LEMENIQDILAQnLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLK 661
Cdd:PRK15134 398 AAQREQQVIAVMEEvgLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLK 469
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1310-1503 |
1.36e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 55.12 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCP-----------QENVLWPNLTV 1378
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPvrkkvgvvfqfPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEhLELYAAVKGLKKKDAVVTITRLVNALKL-QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:PRK13643 104 KD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 153792543 1458 MWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:PRK13643 183 MMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1315-1494 |
1.53e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.97 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVF--LKGSgggaalgflgYCPQENVLWPNLTVKEHLElyaavkglK 1392
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpeLKIS----------YKPQYIKPDYDGTVEDLLR--------S 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1393 KKDAVVT---ITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNT 1469
Cdd:PRK13409 424 ITDDLGSsyyKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170 180
....*....|....*....|....*
gi 153792543 1470 ERGALLTTHYMAEAEAVCDRvaIMV 1494
Cdd:PRK13409 504 EATALVVDHDIYMIDYISDR--LMV 526
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1309-1512 |
1.56e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 56.27 E-value: 1.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGY-----CPQENVLWpNLTVKEHLe 1383
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHrqvalVGQEPVLF-SGSVRENI- 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYaavkGLKK--KDAVVTITRLVNALKLQDHLKALVRT--------LSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:TIGR00958 576 AY----GLTDtpDEEIMAAAKAANAHDFIMEFPNGYDTevgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1454 GQQQMWQAIRAtftnTERGALLTTHYMAEAEAvCDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:TIGR00958 652 CEQLLQESRSR----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
483-649 |
1.94e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLS--PPTTGSVTIYNQTVSEMDDSDAV--- 557
Cdd:PRK09580 4 IKDLHVSVEDK----AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAgeg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 558 --------LTITGVcpqSNvQFGFLTVRENLRLFAKIKGILPHEVEQEVQQVLQDLEMEniQDILAQNL----SGGQ-KR 624
Cdd:PRK09580 80 ifmafqypVEIPGV---SN-QFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVnvgfSGGEkKR 153
|
170 180
....*....|....*....|....*
gi 153792543 625 KLTLGIAILgDPQVLLLDEPTAGLD 649
Cdd:PRK09580 154 NDILQMAVL-EPELCILDESDSGLD 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1289-1505 |
1.94e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1289 KEYIGRTKrcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG---SGGGAALGFLGY 1365
Cdd:PRK10851 9 KKSFGRTQ----------VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1366 CPQENVLWPNLTVKEHLELYAAV---------KGLKKKdavvtITRLVNALKLqDHLKALVRT-LSEGVKRKLCFVLSIL 1435
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGLTVlprrerpnaAAIKAK-----VTQLLEMVQL-AHLADRYPAqLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1436 GNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQ 1505
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1309-1478 |
3.01e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.04 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITG--DTIPTAGQVFLkgsgggaalgflgycpQENVLWPNLTVKEHLElya 1386
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV----------------PDNQFGREASLIDAIG--- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1387 avkglkKKDAVVTITRLVNALKLQDH--LKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRA 1464
Cdd:COG2401 108 ------RKGDFKDAVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQK 181
|
170
....*....|....
gi 153792543 1465 TFTNTERGALLTTH 1478
Cdd:COG2401 182 LARRAGITLVVATH 195
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
493-694 |
3.38e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 55.62 E-value: 3.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 493 KHGKVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPT---TGSVTIYNQTVSEMDDSDAVLTITgvcpQSNV 569
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYIS----QNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 570 QFGFLTVRENLRLFAKIKGI-----LPHEV-----------EQEVQQVLQDLEMENIQ---------------------- 611
Cdd:PLN03140 250 HVGVMTVKETLDFSARCQGVgtrydLLSELarrekdagifpEAEVDLFMKATAMEGVKsslitdytlkilgldickdtiv 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 612 -DILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE---RRAGRVIVFSTQFMDEADILADRKV 687
Cdd:PLN03140 330 gDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivhLTEATVLMSLLQPAPETFDLFDDII 409
|
....*..
gi 153792543 688 FISNGRL 694
Cdd:PLN03140 410 LLSEGQI 416
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
499-643 |
4.67e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 54.51 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 499 ALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIynqtvsemDDSDAVLTItgvcpqSNVQFGFLTVRE 578
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI--------KGSAALIAI------SSGLNGQLTGIE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 579 NLRLFAKIKGILPHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDE 643
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1309-1478 |
5.51e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.85 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMI----TGDTIptAGQVFLKG--SGGGAALGFLGYCPQENVLWPNLTVKEHL 1382
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISGfpKKQETFARISGYCEQNDIHSPQVTVRESL 974
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 eLYAAVKGLKKK----------DAVVTITRLVNalkLQDHLKAL--VRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:PLN03140 975 -IYSAFLRLPKEvskeekmmfvDEVMELVELDN---LKDAIVGLpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*...
gi 153792543 1451 DPEGQQQMWQAIRATfTNTERGALLTTH 1478
Cdd:PLN03140 1051 DARAAAIVMRTVRNT-VDTGRTVVCTIH 1077
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1309-1352 |
5.74e-07 |
|
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: 52.44 E-value: 5.74e-07
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLK 1352
Cdd:COG4778 28 DGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVR 71
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1309-1498 |
6.58e-07 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 6.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------SGGGAALGFLGYCP---QENVLwpnltvk 1379
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeinalSTAQRLARGLVYLPedrQSSGL------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 eHLE--LYAAVKGL-----------KKKDAVVTITRLVNALKLqDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:PRK15439 353 -YLDapLAWNVCALthnrrgfwikpARENAVLERYRRALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1447 STGMDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK15439 431 TRGVDVSARNDIYQLIR-SIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1318-1507 |
6.99e-07 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 52.48 E-value: 6.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1318 GEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL-----GYCPQENVLWPNLTVKEHLEL-----YAA 1387
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAfarkvAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1388 VK--GLKKKDAVVTITRLVNalkLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRAt 1465
Cdd:PRK10575 117 LGrfGAADREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHR- 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 153792543 1466 fTNTERGALLTT--HYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:PRK10575 193 -LSQERGLTVIAvlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
500-665 |
8.10e-07 |
|
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: 50.62 E-value: 8.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVtiynqtvsEMDDSDAVLTItgvcPQSNVqFGFLTVREN 579
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMPEGEDLLFL----PQRPY-LPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LrlfakikgILPheveqevqqvlqdlemeniqdiLAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNL 659
Cdd:cd03223 84 L--------IYP----------------------WDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
....*.
gi 153792543 660 LKERRA 665
Cdd:cd03223 134 LKELGI 139
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1297-1503 |
9.12e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 51.97 E-value: 9.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1297 RCFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISM------ITGDTIPTAGQVFLKGSG-----GGAALGFLGY 1365
Cdd:PRK14246 15 RLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDifqidAIKLRKEVGM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1366 CPQENVLWPNLTVKEHLELYAAVKGLKKKDAVVTIT----RLVNALK-LQDHLKALVRTLSEGVKRKLCFVLSILGNPPV 1440
Cdd:PRK14246 95 VFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVeeclRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKV 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1441 VLLDEPSTGMDPEGQQQMWQAIraTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:PRK14246 175 LLMDEPTSMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1320-1503 |
9.68e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 52.32 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1320 VLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGS----------GGGAALGFLGYCPQENVLWPNLTVkehlELYAAVK 1389
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKpldyskrgllALRQQVATVFQDPEQQIFYTDIDS----DIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1390 GLKKKDAVVTiTRLVNALKLQD--HLKAL-VRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATF 1466
Cdd:PRK13638 105 NLGVPEAEIT-RRVDEALTLVDaqHFRHQpIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 153792543 1467 TNTERgALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:PRK13638 184 AQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
462-660 |
1.06e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 462 PSLNDSlEPVSPEFQ------GKEAIRIKNLKKEYSGKHG-------KVEALRGLGFDIYEGQITALLGHSGAGKTTLIN 528
Cdd:PRK10261 290 ISLEHP-AKQEPPIEqdtvvdGEPILQVRNLVTRFPLRSGllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGR 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 529 TLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTitgvcpQSNVQFGF----------LTVRENLRLFAKIKGILPHEVEQEv 598
Cdd:PRK10261 369 ALLRLVESQGGEIIFNGQRIDTLSPGKLQAL------RRDIQFIFqdpyasldprQTVGDSIMEPLRVHGLLPGKAAAA- 441
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 599 qQVLQDLEMENIQDILA----QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:PRK10261 442 -RVAWLLERVGLLPEHAwrypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1309-1453 |
1.12e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVflKGSgggaALGFLGYCPQENVLW--PNLTVKEHLELYa 1386
Cdd:PRK15064 336 KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--KWS----ENANIGYYAQDHAYDfeNDLTLFDWMSQW- 408
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1387 avKGLKKKDAVV--TITRLvnaLKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPE 1453
Cdd:PRK15064 409 --RQEGDDEQAVrgTLGRL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDME 472
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1310-1478 |
1.21e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKST---------TISMITGDTIPTAGqvflkGSGGGAALGFLGYCPQENVLWPNLTVKE 1380
Cdd:TIGR00956 781 NVDGWVKPGTLTALMGASGAGKTTllnvlaervTTGVITGGDRLVNG-----RPLDSSFQRSIGYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1381 HLELYAAVKGLK------KKDAVVTITRLvnaLKLQDHLKALVRTLSEGV----KRKLCFVLSILGNPP-VVLLDEPSTG 1449
Cdd:TIGR00956 856 SLRFSAYLRQPKsvskseKMEYVEEVIKL---LEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKlLLFLDEPTSG 932
|
170 180
....*....|....*....|....*....
gi 153792543 1450 MDPEGQQQMWQAIRATfTNTERGALLTTH 1478
Cdd:TIGR00956 933 LDSQTAWSICKLMRKL-ADHGQAILCTIH 960
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1325-1478 |
1.21e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.64 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1325 GHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFL-GYCPQENVLWPNLTVKEHLELYAAVkglkkKDAVVTITRL 1403
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYcTYIGHNLGLKLEMTVFENLKFWSEI-----YNSAETLYAA 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1404 VNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIrATFTNTERGALLTTH 1478
Cdd:PRK13541 108 IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI-VMKANSGGIVLLSSH 181
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1309-1510 |
1.58e-06 |
|
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: 51.78 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITgDTIPTAGQVFLKGSGGGAALGFL-----GYCPQENVLWPNlTVKEHLE 1383
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSVPLQKwrkafGVIPQKVFIFSG-TFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKG---LKKKDAV---VTITRLVNALKLQDHLKALVrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:cd03289 99 PYGKWSDeeiWKVAEEVglkSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1458 MWQAIRATFTNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHLKSK 1510
Cdd:cd03289 177 IRKTLKQAFADCT--VILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1310-1496 |
1.66e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 51.29 E-value: 1.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKgsgggaalgflgycpQENVLWPNLT-VKEHLEL---- 1384
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYN---------------NQAITDDNFEkLRKHIGIvfqn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1385 -----------YAAVKGL--------KKKDAVVTITRLVNALKLQDHLKalvRTLSEGVKRKLCFVLSILGNPPVVLLDE 1445
Cdd:PRK13648 92 pdnqfvgsivkYDVAFGLenhavpydEMHRRVSEALKQVDMLERADYEP---NALSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1446 PSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAeAVCDRVAIMVSG 1496
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKG 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1309-1507 |
1.83e-06 |
|
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: 52.99 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITgDTIPTAGQVFLKGSGGGAALGFL-----GYCPQENVLWPNlTVKEHLE 1383
Cdd:TIGR01271 1236 QDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTwrkafGVIPQKVFIFSG-TFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYA--AVKGLKKKDAVVTITRLVNAL--KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMW 1459
Cdd:TIGR01271 1314 PYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIR 1393
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 153792543 1460 QAIRATFTNTErgALLTTHYMaEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:TIGR01271 1394 KTLKQSFSNCT--VILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKL 1438
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1299-1513 |
1.99e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 52.66 E-value: 1.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1299 FSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLG-----YCPQENVLW 1373
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLrrniaVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 pNLTVKEHL----------ELYAAVKGLKKKDAVvtitrLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLL 1443
Cdd:PRK13657 422 -NRSIEDNIrvgrpdatdeEMRAAAERAQAHDFI-----ERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1444 DEPSTGMDPEGQQQMWQAI------RATFTNTERgalLTThyMAEAeavcDRVAIMVSGRLRCIGSIQHLKSKFGK 1513
Cdd:PRK13657 496 DEATSALDVETEAKVKAALdelmkgRTTFIIAHR---LST--VRNA----DRILVFDNGRVVESGSFDELVARGGR 562
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1373-1502 |
2.18e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 51.00 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKEH----LELYAAVKGLKKKDAVVTITRLVNAL--KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:PRK14267 97 FPHLTIYDNvaigVKLNGLVKSKKELDERVEWALKKAALwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1447 STGMDPEGQQQMWQAIRAtfTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:PRK14267 177 TANIDPVGTAKIEELLFE--LKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1277-1349 |
2.26e-06 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 51.08 E-value: 2.26e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1277 DEKPVIIASCLRKEYIGRtkrcfskmkkkIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV 1349
Cdd:PRK11701 2 MDQPLLSVRGLTKLYGPR-----------KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1310-1498 |
2.35e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 50.48 E-value: 2.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQEN-------VLWPNLTVKEHL 1382
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAgmvfqqfYLFPHLTALENV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELYAA-VKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQA 1461
Cdd:PRK09493 99 MFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKV 178
|
170 180 190
....*....|....*....|....*....|....*....
gi 153792543 1462 IRATftnTERG--ALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK09493 179 MQDL---AEEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1309-1516 |
2.41e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.80 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGD---TIpTAGQVFLKGSGGGAALgflgycPQEN------------VLW 1373
Cdd:CHL00131 24 KGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpayKI-LEGDILFKGESILDLE------PEERahlgiflafqypIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVKEHLEL-YAAVK---GLKKKDAVVTITRLVNALKLQDhLKA--LVRTLSEGV-----KRKLCFVLSILgNPPVVL 1442
Cdd:CHL00131 97 PGVSNADFLRLaYNSKRkfqGLPELDPLEFLEIINEKLKLVG-MDPsfLSRNVNEGFsggekKRNEILQMALL-DSELAI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1443 LDEPSTGMDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVC-DRVAIMVSGRLRCIGSIQ--HLKSKFGKDYL 1516
Cdd:CHL00131 175 LDETDSGLDIDALKIIAEGIN-KLMTSENSIILITHYQRLLDYIKpDYVHVMQNGKIIKTGDAElaKELEKKGYDWL 250
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1318-1451 |
2.52e-06 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 52.19 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1318 GEVLGLLGHNGAGKSTTISMITGDTIPT--AGQVFLKGSGGGAALGFLG-YCPQENVLWPNLTVKEHL---ELYAAVKGL 1391
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKRTgFVTQDDILYPHLTVRETLvfcSLLRLPKSL 173
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 1392 KKKDAVVTITRLVNALKLQDHLKALV-----RTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
509-670 |
3.92e-06 |
|
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: 50.06 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 509 EGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTiynqtvsEMDDSDAVLT-ITGvcpqSNVQFGFLTVRENlRLFAKIK 587
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-------DPPDWDEILDeFRG----SELQNYFTKLLEG-DVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 588 ----GILPHEVEQEVQQVL-------------QDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:cd03236 93 pqyvDLIPKAVKGKVGELLkkkdergkldelvDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDI 172
|
170 180
....*....|....*....|....
gi 153792543 651 LSRHR----IWNLLKERRAgrVIV 670
Cdd:cd03236 173 KQRLNaarlIRELAEDDNY--VLV 194
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
582-674 |
4.28e-06 |
|
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: 50.47 E-value: 4.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 582 LFAKIKGILPHEVEQEVQQVLqdLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQ---VLLLDEPTAGLDPLSRHRIWN 658
Cdd:pfam13304 203 GEGIEKSLLVDDRLRERGLIL--LENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLIDEPESGLHPKLLRRLLE 280
|
90
....*....|....*..
gi 153792543 659 LLKERRAGRV-IVFSTQ 674
Cdd:pfam13304 281 LLKELSRNGAqLILTTH 297
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1303-1453 |
5.58e-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: 51.09 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIaTRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalGFLGYCPQENVLWPNLTVKEHL 1382
Cdd:TIGR03719 17 KKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPG------IKVGYLPQEPQLDPTKTVRENV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1383 ELyaavkGLKKKDAVVTITRLVNAL----------------KLQDHLKAL------------------------VRTLSE 1422
Cdd:TIGR03719 90 EE-----GVAEIKDALDRFNEISAKyaepdadfdklaaeqaELQEIIDAAdawdldsqleiamdalrcppwdadVTKLSG 164
|
170 180 190
....*....|....*....|....*....|...
gi 153792543 1423 GVKRK--LCFVLsiLGNPPVVLLDEPSTGMDPE 1453
Cdd:TIGR03719 165 GERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1309-1451 |
5.89e-06 |
|
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: 51.45 E-value: 5.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgfLGYCPQENVLWPNlTVKEHLelyaaV 1388
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------ISFSPQTSWIMPG-TIKDNI-----I 508
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 153792543 1389 KGLKKKDavVTITRLVNALKLQDHLKALVR-----------TLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMD 1451
Cdd:TIGR01271 509 FGLSYDE--YRYTSVIKACQLEEDIALFPEkdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1309-1498 |
6.80e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 50.80 E-value: 6.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG------SGGGAALGFLGYCPQE---NVLWPNLTVK 1379
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGeditglSPRERRRLGVAYIPEDrlgRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1380 EH--LELYA----AVKGLKKKDAVVTIT-RLVNALKLQ-DHLKALVRTLSEGVKRKlcFVLS--ILGNPPVVLLDEPSTG 1449
Cdd:COG3845 355 ENliLGRYRrppfSRGGFLDRKAIRAFAeELIEEFDVRtPGPDTPARSLSGGNQQK--VILAreLSRDPKLLIAAQPTRG 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1450 MDPEGQQQMWQAIRATftnTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:COG3845 433 LDVGAIEFIHQRLLEL---RDAGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1308-1502 |
7.47e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 50.03 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1308 TRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycP---------QENVLWPNLTV 1378
Cdd:PRK11000 19 SKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP------PaergvgmvfQSYALYPHLSV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDavvtITRLVN--ALKLQ-DHL-----KAlvrtLSEGVKRKLCFVLSILGNPPVVLLDEPSTGM 1450
Cdd:PRK11000 93 AENMSFGLKLAGAKKEE----INQRVNqvAEVLQlAHLldrkpKA----LSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1451 DPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIG 1502
Cdd:PRK11000 165 DAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1307-1507 |
7.82e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 49.72 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGdtiPTAGQVFLKGSGGGAALGFLGYcPQENV--------------- 1371
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMG---LLAANGRIGGSATFNGREILNL-PEKELnklraeqismifqdp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 ---LWPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALV---RTLSEGVKRKLCFVLSILGNPPVVLLD 1444
Cdd:PRK09473 107 mtsLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792543 1445 EPSTGMDPEGQQQ---MWQAIRATFtNTerGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGSIQHL 1507
Cdd:PRK09473 187 EPTTALDVTVQAQimtLLNELKREF-NT--AIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
465-649 |
8.47e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 465 NDSLE---PVSPEFqGKEAIRIKNLKKEYSGKhgkvEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSV 541
Cdd:PRK11819 307 NETNEifiPPGPRL-GDKVIEAENLSKSFGDR----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 542 TI-------Y-NQTVSEMDDSDAV----------LTITGVCPQSNV---QFGFltvrenlrlfakiKGilpheveqevqq 600
Cdd:PRK11819 382 KIgetvklaYvDQSRDALDPNKTVweeisggldiIKVGNREIPSRAyvgRFNF-------------KG------------ 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 601 vlQDlemeniQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 649
Cdd:PRK11819 437 --GD------QQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1287-1498 |
1.14e-05 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 48.91 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1287 LRKEYIGRTkrcfskmkkkiATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYC 1366
Cdd:PRK11247 18 VSKRYGERT-----------VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1367 PQENVLWPNLTVKEHLELyaAVKGLKKKDAVvtitRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEP 1446
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGL--GLKGQWRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 1447 STGMDP----EGQQ---QMWQaiRATFTntergALLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK11247 161 LGALDAltriEMQDlieSLWQ--QHGFT-----VLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1309-1498 |
1.28e-05 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 48.81 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGG------------------AALGFLGYCPQEN 1370
Cdd:PRK10619 22 KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadknqlrLLRTRLTMVFQHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1371 VLWPNLTVKEH-LELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRT-LSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:PRK10619 102 NLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVLLFDEPTS 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 153792543 1449 GMDPEgqqQMWQAIRATFTNTERGA--LLTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK10619 182 ALDPE---LVGEVLRIMQQLAEEGKtmVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1306-1491 |
1.48e-05 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 48.62 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1306 IATRNISFCVKKGEVLGLLGHNGAGKSTTISMI--TGDTIPTA---GQVFLKGSGGgaalgflgYCPQENVLW------- 1373
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGFrveGKVTFHGKNL--------YAPDVDPVEvrrrigm 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 ----PN---LTVKEHLELYAAVKGLKKK-DAVVTITRLVNAL--KLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLL 1443
Cdd:PRK14243 96 vfqkPNpfpKSIYDNIAYGARINGYKGDmDELVERSLRQAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1444 DEPSTGMDPEGQ---QQMWQAIRATFTntergALLTTHYMAEAEAVCDRVA 1491
Cdd:PRK14243 176 DEPCSALDPISTlriEELMHELKEQYT-----IIIVTHNMQQAARVSDMTA 221
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
510-662 |
1.49e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.11 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGL---SPPTTGSVTIYNQtvseMDDSDAVLTITG---VCPQSNVQFGFLTVRENLRLF 583
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNtdgFHIGVEGVITYDG----ITPEEIKKHYRGdvvYNAETDVHFPHLTVGETLDFA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 584 AKIKGI--LPHEV-EQEVQQVLQDLEME----------NIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 650
Cdd:TIGR00956 163 ARCKTPqnRPDGVsREEYAKHIADVYMAtyglshtrntKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLDS 242
|
170
....*....|..
gi 153792543 651 LSRHRIWNLLKE 662
Cdd:TIGR00956 243 ATALEFIRALKT 254
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1309-1478 |
1.54e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGflgycpQENVLWPNLTVKEHLELYAAV 1388
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFS------QHHVDGLDLSSNPLLYMMRCF 599
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 KGLKKKdavvtitrlvnalKLQDHLKAL----------VRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:PLN03073 600 PGVPEQ-------------KLRAHLGSFgvtgnlalqpMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAL 666
|
170 180
....*....|....*....|
gi 153792543 1459 WQAIrATFtntERGALLTTH 1478
Cdd:PLN03073 667 IQGL-VLF---QGGVLMVSH 682
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
512-668 |
1.96e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 1.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 512 ITALLGHSGAGKTTLIN----TLSGLSPPTTGSVTIYNQTVSEmDDSDAVLTITgvcpQSNVQFGFLTVRENLRLFAKIk 587
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIRE-GEVRAQVKLA----FENANGKKYTITRSLAILENV- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 588 gILPHEveqevqqvlqdlemENIQDILAQN---LSGGQKRKLTLGIAI-----LGDP-QVLLLDEPTAGLDPLSR-HRIW 657
Cdd:cd03240 98 -IFCHQ--------------GESNWPLLDMrgrCSGGEKVLASLIIRLalaetFGSNcGILALDEPTTNLDEENIeESLA 162
|
170
....*....|.
gi 153792543 658 NLLKERRAGRV 668
Cdd:cd03240 163 EIIEERKSQKN 173
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
491-532 |
1.97e-05 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 48.57 E-value: 1.97e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 153792543 491 SGKHGK-VEALRglgfDIYEGQITALLGHSGAGKTTLINTLSG 532
Cdd:COG1162 150 SAKTGEgLDELR----ELLKGKTSVLVGQSGVGKSTLINALLP 188
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
509-532 |
2.07e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.39 E-value: 2.07e-05
10 20
....*....|....*....|....
gi 153792543 509 EGQITALLGHSGAGKTTLINTLSG 532
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
500-649 |
2.46e-05 |
|
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: 49.17 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 500 LRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITgVCPQSNVQFGFlTVREN 579
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKIT-IIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 580 LRLFAKIKGilpheveqevQQVLQDLEMENIQDILA--------------QNLSGGQKRKLTLGIAILGDPQVLLLDEPT 645
Cdd:TIGR00957 1380 LDPFSQYSD----------EEVWWALELAHLKTFVSalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
....
gi 153792543 646 AGLD 649
Cdd:TIGR00957 1450 AAVD 1453
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1309-1461 |
2.90e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 47.93 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgfLGYCPQENVLWPNlTVKEHLELYAAV 1388
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------ISFSSQFSWIMPG-TIKENIIFGVSY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 KGLKKKDavvtitrLVNALKLQDHLKALVR-----------TLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQ 1457
Cdd:cd03291 125 DEYRYKS-------VVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKE 197
|
....
gi 153792543 1458 MWQA 1461
Cdd:cd03291 198 IFES 201
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1311-1445 |
3.15e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.64 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGgaalgflgycPQENVLWpnltvkeHLELYAAV-- 1388
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV----------TADNREA-------YRQLFSAVfs 413
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1389 --------KGLKKKDAVVTITRLVNALKLQDHLK----ALVRT-LSEGVKRKLCFVLSILGNPPVVLLDE 1445
Cdd:COG4615 414 dfhlfdrlLGLDGEADPARARELLERLELDHKVSvedgRFSTTdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1311-1503 |
3.43e-05 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 47.49 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCPQENV------------------L 1372
Cdd:COG4598 27 VSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPADRrqlqrirtrlgmvfqsfnL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEG------VKRKLCFvlsilgNPPVVLLDE 1445
Cdd:COG4598 107 WSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGqqqraaIARALAM------EPEVMLFDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1446 PSTGMDPEGQQQMWQAIRAtFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCIGS 1503
Cdd:COG4598 181 PTSALDPELVGEVLKVMRD-LAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGP 237
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1311-1512 |
3.48e-05 |
|
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: 48.79 E-value: 3.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1311 ISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalgfLGYCPQEnvLW-PNLTVKEHLeLYAAVK 1389
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------VAYVPQQ--AWiQNDSLRENI-LFGKAL 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1390 GLKKKDAVVTITRLVNALKL-----QDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAI-- 1462
Cdd:TIGR00957 726 NEKYYQQVLEACALLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVig 805
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1463 -RATFTNTERgaLLTTHYMAEAEAVcDRVAIMVSGRLRCIGSIQHLKSKFG 1512
Cdd:TIGR00957 806 pEGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1315-1463 |
4.33e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 46.98 E-value: 4.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV-----------FLKGSGGGAALGFLGycpqENVLWPNLTVKEHLE 1383
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNYFTKLL----EGDVKVIVKPQYVDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1384 LYAAVKG-----LKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPSTGMDPEGQQQM 1458
Cdd:cd03236 99 IPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
....*
gi 153792543 1459 WQAIR 1463
Cdd:cd03236 179 ARLIR 183
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1309-1463 |
4.49e-05 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 47.00 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAalgflgyCP------------QENVLWPNL 1376
Cdd:COG4604 18 DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-------TPsrelakrlailrQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1377 TVKEHLEL--YAAVKG-LKKKDAVVtITRLVNALKLQDHLKALVRTLSEGvKRKLCFVLSILG-NPPVVLLDEPSTGMDP 1452
Cdd:COG4604 91 TVRELVAFgrFPYSKGrLTAEDREI-IDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDM 168
|
170
....*....|.
gi 153792543 1453 EGQQQMWQAIR 1463
Cdd:COG4604 169 KHSVQMMKLLR 179
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
618-693 |
5.41e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 5.41e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 618 LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE--RRAGRVIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRElqQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
515-649 |
5.56e-05 |
|
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: 47.62 E-value: 5.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 515 LLGHSGAGKTTLINTLSGLSPPTTGSVTiynqtvsemddsdavltitgvcPQSNVQFGFL----------TVRENLRL-F 583
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEAR----------------------PQPGIKVGYLpqepqldptkTVRENVEEgV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 584 AKIKGILP--HEV----------------EQ-EVQQVLQ-------DLEMENIQDIL--------AQNLSGGQKRKLTLG 629
Cdd:TIGR03719 94 AEIKDALDrfNEIsakyaepdadfdklaaEQaELQEIIDaadawdlDSQLEIAMDALrcppwdadVTKLSGGERRRVALC 173
|
170 180
....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLD 649
Cdd:TIGR03719 174 RLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1310-1497 |
5.90e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKS-TTISMI-----------TGDtIPTAGQVFLKGSGGGAALG---FLGYCPQENV--L 1372
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSvTALSILrllpsppvvypSGD-IRFHGESLLHASEQTLRGVrgnKIAMIFQEPMvsL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1373 WPNLTVKEHL-ELYAAVKGLKKKDAVVTITRLVNALKLQD---HLKALVRTLSEGVKRKLCFVLSILGNPPVVLLDEPST 1448
Cdd:PRK15134 106 NPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPTT 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 153792543 1449 GMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGR 1497
Cdd:PRK15134 186 ALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1300-1499 |
6.15e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.57 E-value: 6.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1300 SKMKKKIATRNISFC-------------VKKGEVLGLLGHNGAGKSTTISMIT-----GDTIPTAGQV-FLKGSGGGAAL 1360
Cdd:PRK14258 2 SKLIPAIKVNNLSFYydtqkilegvsmeIYQSKVTAIIGPSGCGKSTFLKCLNrmnelESEVRVEGRVeFFNQNIYERRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1361 GFLGYCPQENVLWPN-----LTVKEHLELYAAVKGLKKK-------DAVVTITRLVNALKLQDHLKALvrTLSEGVKRKL 1428
Cdd:PRK14258 82 NLNRLRRQVSMVHPKpnlfpMSVYDNVAYGVKIVGWRPKleiddivESALKDADLWDEIKHKIHKSAL--DLSGGQQQRL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 1429 CFVLSILGNPPVVLLDEPSTGMDPEGQQQMWQAIRATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLR 1499
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1266-1353 |
6.78e-05 |
|
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: 47.37 E-value: 6.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1266 RTTGAMATLQTDEKPVIIASCLRKEYIGRTKRCFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGdTIPT 1345
Cdd:COG4172 260 EPRGDPRPVPPDAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPS 338
|
....*...
gi 153792543 1346 AGQVFLKG 1353
Cdd:COG4172 339 EGEIRFDG 346
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
510-693 |
7.60e-05 |
|
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: 44.67 E-value: 7.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 510 GQITALLGHSGAGKTTLINTLSGLSPPTTGSvtiynqtvsemddsdaVLTITGvcpqsnvqfgfltvrenlrlfakikgi 589
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGG----------------VIYIDG--------------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 590 lpheveQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL-------KE 662
Cdd:smart00382 39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*.
gi 153792543 663 RRAGRVIVFSTQFMDEAD-----ILADRKVFISNGR 693
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLIL 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1303-1453 |
8.30e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 8.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1303 KKKIaTRNISFCVKKGEVLGLLGHNGAGKSTTISM-------ITGDTIPTAGqvflkgsgggaalGFLGYCPQENVLWPN 1375
Cdd:PRK11819 19 KKQI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRImagvdkeFEGEARPAPG-------------IKVGYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1376 LTVKEHLElyAAVKGLKKKdavvtITRL--VNAL----------------KLQDHLKAL--------------------- 1416
Cdd:PRK11819 85 KTVRENVE--EGVAEVKAA-----LDRFneIYAAyaepdadfdalaaeqgELQEIIDAAdawdldsqleiamdalrcppw 157
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 153792543 1417 ---VRTLSEGVKRK--LCFVLsiLGNPPVVLLDEPSTGMDPE 1453
Cdd:PRK11819 158 dakVTKLSGGERRRvaLCRLL--LEKPDMLLLDEPTNHLDAE 197
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
483-693 |
8.38e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.03 E-value: 8.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 483 IKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSDAVLTITG 562
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 563 VCPQSNVQFGFLTVRENLRLFA-KIKGILPHE--VEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVL 639
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMWLGRyPTKGMFVDQdkMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 640 LLDEPTAGL-DPLSRH--RIWNLLKERRAGrvIVFSTQFMDEADILADRKVFISNGR 693
Cdd:PRK10982 157 IMDEPTSSLtEKEVNHlfTIIRKLKERGCG--IVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1307-1353 |
1.05e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 45.94 E-value: 1.05e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG 1353
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1298-1452 |
1.05e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 46.89 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1298 CFSKMKKKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAAlgflgycpqenvlwpnlT 1377
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----------------Q 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1378 VKEHLELYAAV-------------KGLKKKDAVV----TITRLVNALKLQDHLKALVRtLSEGVKRKLCFVLSILGNPPV 1440
Cdd:PRK10522 392 PEDYRKLFSAVftdfhlfdqllgpEGKPANPALVekwlERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDI 470
|
170
....*....|..
gi 153792543 1441 VLLDEPSTGMDP 1452
Cdd:PRK10522 471 LLLDEWAADQDP 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1316-1349 |
1.20e-04 |
|
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: 46.70 E-value: 1.20e-04
10 20 30
....*....|....*....|....*....|....
gi 153792543 1316 KKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV 1349
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY 130
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1309-1501 |
1.39e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1309 RNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALgflgycPQENV---------------LW 1373
Cdd:PRK10982 265 RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHN------ANEAInhgfalvteerrstgIY 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 PNLTVkEHLELYAAVKGLKKKDAVVTITRL-------VNALKLQ--DHlKALVRTLSEGVKRKLCFVLSILGNPPVVLLD 1444
Cdd:PRK10982 339 AYLDI-GFNSLISNIRNYKNKVGLLDNSRMksdtqwvIDSMRVKtpGH-RTQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 153792543 1445 EPSTGMDPEGQQQMWQAIrATFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLRCI 1501
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1310-1498 |
1.40e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 45.51 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSGGGAALGFLGYCP-----------QENVLWPNlTV 1378
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQirkkvglvfqfPESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1379 KEHLELYAAVKGLKKKDAVVTITRLVNALKLQDHLkaLVRT---LSEGVKRKLCfVLSILG-NPPVVLLDEPSTGMDPEG 1454
Cdd:PRK13649 104 LKDVAFGPQNFGVSQEEAEALAREKLALVGISESL--FEKNpfeLSGGQMRRVA-IAGILAmEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 153792543 1455 QQQMWQairaTFTNTERGAL---LTTHYMAEAEAVCDRVAIMVSGRL 1498
Cdd:PRK13649 181 RKELMT----LFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1304-1455 |
1.42e-04 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 45.36 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1304 KKIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalGFLGYCPQE----------NVLW 1373
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGE------HIQHYASKEvarrigllaqNATT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1374 P-NLTVKE--------HLELYAAvkgLKKKDAvVTITRLVNALKLQDHLKALVRTLSEGVKRKLCFVLSILGNPPVVLLD 1444
Cdd:PRK10253 93 PgDITVQElvargrypHQPLFTR---WRKEDE-EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170
....*....|.
gi 153792543 1445 EPSTGMDPEGQ 1455
Cdd:PRK10253 169 EPTTWLDISHQ 179
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1307-1521 |
1.54e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKGSgggaalGFLGYCP------------QENVLWP 1374
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK------EVTFNGPkssqeagigiihQELNLIP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1375 NLTVKEHL----ELYAAVKGLKKKDAVVTITRLVNALKLQDHLKALVRTLSEGVKR--KLCFVLSILGNppVVLLDEPST 1448
Cdd:PRK10762 93 QLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQmvEIAKVLSFESK--VIIMDEPTD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 153792543 1449 GMDPEGQQQMWQAIRaTFTNTERGALLTTHYMAEAEAVCDRVAIMVSGRLrcIGsiQHLKSKFGKDYLLEMKV 1521
Cdd:PRK10762 171 ALTDTETESLFRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF--IA--EREVADLTEDSLIEMMV 238
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
509-532 |
1.71e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 44.07 E-value: 1.71e-04
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
617-694 |
2.12e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 617 NLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGR-VIVFSTQfMDEADILADRKVFISNGRL 694
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKgVIVISSE-LPELLGMCDRIYVMNEGRI 482
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
482-535 |
2.14e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 153792543 482 RIKNLKKEYSGkhgkVEALRGLGFDIYEGQITALLGHSGAGKTTLINTLSGLSP 535
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP 52
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1301-1462 |
2.26e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.93 E-value: 2.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1301 KMKK-------KIATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFL-KGsgggaalGFLGYCPQENV- 1371
Cdd:PRK10636 314 KMEKvsagygdRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKG-------IKLGYFAQHQLe 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 1372 -LWPNLTVKEHLelyaavkglkkkdavVTITRLVNALKLQDHLKAL----------VRTLSEGVKRKLCFVLSILGNPPV 1440
Cdd:PRK10636 387 fLRADESPLQHL---------------ARLAPQELEQKLRDYLGGFgfqgdkvteeTRRFSGGEKARLVLALIVWQRPNL 451
|
170 180
....*....|....*....|..
gi 153792543 1441 VLLDEPSTGMDPEGQQQMWQAI 1462
Cdd:PRK10636 452 LLLDEPTNHLDLDMRQALTEAL 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1310-1349 |
2.57e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.70 E-value: 2.57e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV 1349
Cdd:TIGR03719 340 DLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1307-1340 |
3.27e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 3.27e-04
10 20 30
....*....|....*....|....*....|....
gi 153792543 1307 ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITG 1340
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1315-1349 |
3.76e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.18 E-value: 3.76e-04
10 20 30
....*....|....*....|....*....|....*
gi 153792543 1315 VKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV 1349
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDY 130
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
618-692 |
4.23e-04 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 42.73 E-value: 4.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 618 LSGGQKRKLT----LGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKERRAGRVIVFST----QFMDEADILADRKVFI 689
Cdd:cd03227 78 LSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIthlpELAELADKLIHIKKVI 157
|
...
gi 153792543 690 SNG 692
Cdd:cd03227 158 TGV 160
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
512-660 |
4.88e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 512 ITALLGHSGAGKTTLINTLSGLSPPTTGSVTIYNQTVSEMDDSdavltitgVCPQSNVQFGF---LTVRENLRLFAKIkg 588
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP--------YCTYIGHNLGLkleMTVFENLKFWSEI-- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792543 589 ilpHEVEQEVQQVLQDLEMENIQDILAQNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLL 660
Cdd:PRK13541 98 ---YNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
599-653 |
6.01e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 44.24 E-value: 6.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 153792543 599 QQVLQD--LEMENIQDILA----QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSR 653
Cdd:PRK10938 377 QQKLAQqwLDILGIDKRTAdapfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNR 437
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1277-1353 |
6.21e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 43.80 E-value: 6.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 153792543 1277 DEKPVIIASCLRKEYigRTKRCFSKMKKKI-ATRNISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQVFLKG 1353
Cdd:PRK11308 1 SQQPLLQAIDLKKHY--PVKRGLFKPERLVkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1310-1349 |
6.96e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 44.34 E-value: 6.96e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGDTIPTAGQV 1349
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI 381
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
515-649 |
7.32e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 7.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 515 LLGHSGAGKTTLINTLSGLSPPTTGSVTiynqtvsemddsdavltitgvcPQSNVQFGFL----------TVRENLRL-F 583
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEAR----------------------PAPGIKVGYLpqepqldpekTVRENVEEgV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 584 AKIKGILP--HEV----------------EQ-EVQQVLQ-----DLE------MENIQ----DILAQNLSGGQKRKLTLG 629
Cdd:PRK11819 96 AEVKAALDrfNEIyaayaepdadfdalaaEQgELQEIIDaadawDLDsqleiaMDALRcppwDAKVTKLSGGERRRVALC 175
|
170 180
....*....|....*....|
gi 153792543 630 IAILGDPQVLLLDEPTAGLD 649
Cdd:PRK11819 176 RLLLEKPDMLLLDEPTNHLD 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
616-656 |
9.27e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 44.25 E-value: 9.27e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 153792543 616 QNLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRI 656
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
225-369 |
9.97e-04 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 42.26 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792543 225 FFIFFCVISFSSLIYYLSVNITQERQYMTTLMAMMGLRESAFWLSWSLMYAGFILVVAVLMSLIVK---SAQVVVLTGFM 301
Cdd:pfam01061 49 LLFFSILFNAFSALSGISPVFEKERGVLYRELASPLYSPSAYVLAKILSELPLSLLQSLIFLLIVYfmvGLPPSAGRFFL 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792543 302 VVFLLFLFYgLSLITLSFLMSVLIKKPFLTGLAIFILTVFWGSL-GFTALYKHLPAFVEWtLCFLSPFA 369
Cdd:pfam01061 129 FLLVLLLTA-LAASSLGLFISALAPSFEDASQLGPLVLLPLLLLsGFFIPIDSMPVWWQW-IYYLNPLT 195
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
509-541 |
1.04e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 43.38 E-value: 1.04e-03
10 20 30
....*....|....*....|....*....|...
gi 153792543 509 EGQITALLGHSGAGKTTLINTLSGLSPPTTGSV 541
Cdd:PRK01889 194 GGKTVALLGSSGVGKSTLVNALLGEEVQKTGAV 226
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1310-1351 |
1.05e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 1.05e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 153792543 1310 NISfcVKKGE--VLGLLGHNGAGKSTTISMITGDTIPTAGQVFL 1351
Cdd:PRK15064 19 NIS--VKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1305-1334 |
1.13e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|
gi 153792543 1305 KIATRNISFCVKKGEVLGLLGHNGAGKSTT 1334
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTT 328
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
497-532 |
1.73e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 42.50 E-value: 1.73e-03
10 20 30
....*....|....*....|....*....|....*.
gi 153792543 497 VEALRglgfDIYEGQITALLGHSGAGKTTLINTLSG 532
Cdd:PRK00098 155 LDELK----PLLAGKVTVLAGQSGVGKSTLLNALAP 186
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
618-684 |
2.65e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.31 E-value: 2.65e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792543 618 LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPLSRHRIWNLLKE-RRAGRVIV-----FST--QFMDEADILAD 684
Cdd:PRK10938 136 LSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASlHQSGITLVlvlnrFDEipDFVQFAGVLAD 210
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1310-1341 |
9.31e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 40.38 E-value: 9.31e-03
10 20 30
....*....|....*....|....*....|..
gi 153792543 1310 NISFCVKKGEVLGLLGHNGAGKSTTISMITGD 1341
Cdd:PRK10938 278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD 309
|
|
| |
