|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
108-1665 |
0e+00 |
|
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: 872.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 108 KVIGFPSESDFEDYARSTVNSRNILAAIVFGHNFANSSDpLPKKVKYYLRFS-DIKKNINSGAYYQGDTwltkflfhslr 186
Cdd:TIGR01257 524 KFESYDDEVQLTQRALSLLEENRFWAGVVFPDMYPWTSS-LPPHVKYKIRMDiDVVEKTNKIKDRYWDS----------- 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 187 lvGPR-NPYEadggSPGYITEGFLAVQHALDKAIMLHHGGADAAalfndISLFIQRFPYPAYYHDYFYLFATTFIPLTVA 265
Cdd:TIGR01257 592 --GPRaDPVE----DFRYIWGGFAYLQDMVEQGITRSQMQAEPP-----VGIYLQQMPYPCFVDDSFMIILNRCFPIFMV 660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 266 CTFFFNHYVLVWSIVWEKENRLKEYQLMIGLRNWMFWVAYFFTFLCLYFINIIVMCMVlfvkIEPAPIFQYNDPTLVFIF 345
Cdd:TIGR01257 661 LAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIF----IMHGRILHYSDPFILFLF 736
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 346 LLFYAISSIFFSFMVSTLFNKVSLAMSLGSFLFFLTYFPAVAMHQSFERMPSKQKLIWSFDFNVGMAFGFRFLVNTDAKK 425
Cdd:TIGR01257 737 LLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQG 816
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 426 TGMKWSNIFLS-TDSDSFLFAYVLGMLLADAFIYGLVAWYIEAVFPGEYGVPKPWNFFLMHSYWFG-------------- 490
Cdd:TIGR01257 817 LGLQWSNIGNSpLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGgegcstreeralek 896
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 491 -EPPQQKLEITQFYERVESKYFEAEPTDLTAGIQIKHLHKVFQKNNttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLS 569
Cdd:TIGR01257 897 tEPLTEEMEDPEHPEGINDSFFERELPGLVPGVCVKNLVKIFEPSG--RPAVDRLNITFYENQITAFLGHNGAGKTTTLS 974
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 570 ILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEK 649
Cdd:TIGR01257 975 ILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHK 1054
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 650 CDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMV 729
Cdd:TIGR01257 1055 RNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIIS 1134
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 730 RGTLRCCGSSVFLKRLYGVGSHLVMVKE--------------------------PYC------------DIAEISKLIHS 771
Cdd:TIGR01257 1135 QGRLYCSGTPLFLKNCFGTGFYLTLVRKmkniqsqrggcegtcsctskgfstrcPARvdeitpeqvldgDVNELMDLVYH 1214
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 772 YVPTATLETNVGNELSFILP-KEYTHR-FEALFTALEENQENLGISSFGVSITTMEEVFLKVSNLEDS-----------K 838
Cdd:TIGR01257 1215 HVPEAKLVECIGQELIFLLPnKNFKQRaYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSgslfaggaqqkR 1294
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 839 TDI-----------EATQSPSvGSKGNKNGDVESSGRVGFPTQSEDQNIVFNTGCSLYLQQFRAMFMKRLMYNWRNWRGI 907
Cdd:TIGR01257 1295 ENAnlrhpcsgpteKAGQTPQ-ASHTCSPGQPAAHPEGQPPPEPEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDF 1373
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 908 LVQI------------LGLIISTF-----------------------------------LLLKSHEFRYKKIRQMNLDEY 940
Cdd:TIGR01257 1374 LAQIvlpatfvflalmLSIIIPPFgeypaltlhpwmygqqytffsmdepnsehlevladVLLNKPGFGNRCLKEEWLPEY 1453
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 941 -----------------------------------------GQTIVPFSIWGKSNL--------TSSLLTHLENM----- 966
Cdd:TIGR01257 1454 pcgnstpwktpsvspnithlfqkqkwtaahpspscrcstreKLTMLPECPEGAGGLpppqrtqrSTEILQDLTDRnisdf 1533
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 967 ------------LKP---------------GNHQLKEVQGD-LLKYLEGNDECVHLCVIALS----------IKVVANRV 1008
Cdd:TIGR01257 1534 lvktypalirssLKSkfwvneqryggisigGKLPAIPITGEaLVGFLSDLGQMMNVSGGPVTreaskempdfLKHLETED 1613
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1009 NLTVLFNNEAYHSPSLSLTVLDN-ILFMSL----SGSDASITVFNkpQPSPQRKE-------WPGSTDGkIVAFKIQLGM 1076
Cdd:TIGR01257 1614 NIKVWFNNKGWHALVSFLNVAHNaILRASLpkdrDPEEYGITVIS--QPLNLTKEqlseitvLTTSVDA-VVAICVIFAM 1690
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1077 ALLVSGFCILTVTERHNKTKHMQFLSGVSILVYWLSALVFDLIIFFISCCFLLVMFKYCKFDIYVTDYHILDTMLILTLF 1156
Cdd:TIGR01257 1691 SFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLY 1770
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1157 GWSAIPLTYLLSFLFSKSNSAYINLLVFCYLSGTLSLLMDTIIEaristIMSNSTQTFLLNALL-----LFPMYNLGKCI 1231
Cdd:TIGR01257 1771 GWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLE-----LFENNRTLLRFNAMLrklliVFPHFCLGRGL 1845
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1232 SEytviyrkkmLCIQQKNALKYLNCSNKHTKKniySLKKPMLGKYLIAMSIAGFVFLLLiffweniswkvKMFIHQHIYF 1311
Cdd:TIGR01257 1846 ID---------LALSQAVTDVYAQFGEEHSAN---PFQWDLIGKNLVAMAVEGVVYFLL-----------TLLIQHHFFL 1902
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1312 gacKKYKPDIISKELsgTSEDNDVENERREILYQPEKflnCPVL-IKELTKIY--FKSPlilAVKNISLAIQERACFGLL 1388
Cdd:TIGR01257 1903 ---SRWIAEPAKEPI--FDEDDDVAEERQRIISGGNK---TDILrLNELTKVYsgTSSP---AVDRLCVGVRPGECFGLL 1971
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1389 GFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYV 1468
Cdd:TIGR01257 1972 GVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVA 2051
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1469 KKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSME 1548
Cdd:TIGR01257 2052 NWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSME 2131
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1549 ECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYILKAKVKSGE-----TLDEFKNFITLTFPGSELQQENQGILNYCIP 1623
Cdd:TIGR01257 2132 ECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVS 2211
|
1770 1780 1790 1800
....*....|....*....|....*....|....*....|..
gi 46358378 1624 rkNNSWGKVFGILEKAKEQYNLEDYSISQITLDQVFLSFADQ 1665
Cdd:TIGR01257 2212 --SSSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQ 2251
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
522-743 |
6.67e-106 |
|
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: 336.78 E-value: 6.67e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqkNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSVFLK 743
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1354-1575 |
2.99e-98 |
|
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: 314.83 E-value: 2.99e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYfKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGY 1433
Cdd:cd03263 1 LQIRNLTKTY-KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1514 PSTGMDPRARRLLWDTVIKIReSGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLK 1575
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
522-738 |
1.15e-80 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 265.39 E-value: 1.15e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 682 EPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1356-1578 |
3.96e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 249.60 E-value: 3.96e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKsplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCP 1435
Cdd:COG1131 3 VRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:COG1131 80 QEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKF 1578
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
522-733 |
1.21e-64 |
|
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: 216.88 E-value: 1.21e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03230 1 IEVRNLSKRYGK----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYfycrikgvpqkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03230 77 YLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 682 EPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
522-743 |
1.74e-63 |
|
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: 215.70 E-value: 1.74e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03265 1 IEVENLVKKYGDF----EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 682 EPTSGMDPASRRSTWDILQTYK--QNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSVFLK 743
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
539-831 |
1.91e-60 |
|
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: 209.94 E-value: 1.91e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEH 618
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDI 698
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 699 LQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSVFLKRLYGvGSHLVMVKEPYCDI-AEISKLIHSYVPT- 775
Cdd:TIGR01188 167 IRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLkVEVSMLIAELGETg 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 776 -ATLETNVGNELSFILPKEYTHRFEALFTALEENqeNLGISSFGVSITTMEEVFLKV 831
Cdd:TIGR01188 246 lGLLAVTVDSDRIKILVPDGDETVPEIVEAAIRN--GIRIRSISTERPSLDDVFLKL 300
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
522-734 |
3.26e-57 |
|
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: 198.54 E-value: 3.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 682 EPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1356-1565 |
9.45e-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: 194.15 E-value: 9.45e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCP 1435
Cdd:cd03230 3 VRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMimyariwgisehqiqpyvkkylnsldleshanslisTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03230 80 EEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1356-1580 |
1.67e-55 |
|
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: 193.54 E-value: 1.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCP 1435
Cdd:COG4555 4 VENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:COG4555 81 DERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFGN 1580
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1354-1575 |
5.55e-55 |
|
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: 191.04 E-value: 5.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKsplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGY 1433
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1514 PSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLK 1575
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
522-737 |
3.19e-54 |
|
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: 188.56 E-value: 3.19e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGqVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03264 1 LQLENLTKRYGK----KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG 737
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
254-841 |
1.14e-51 |
|
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: 201.78 E-value: 1.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 254 LFATTFIPLTvactfffnhyvLVWSIVWEKENRLKEYQLMIGLRNWMFWVAYFFTFLCLYFIN--IIVMCMVLFVKiePA 331
Cdd:TIGR01257 1687 IFAMSFVPAS-----------FVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSagLVVGIFIGFQK--KA 1753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 332 PIFQYNDPTLVFIFLLF-YAISSIFF--SFMV---STLFNKVSLA-----MSLGSFLFFLTYFPAVAMHQSFERMPSKQK 400
Cdd:TIGR01257 1754 YTSPENLPALVALLMLYgWAVIPMMYpaSFLFdvpSTAYVALSCAnlfigINSSAITFVLELFENNRTLLRFNAMLRKLL 1833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 401 LIWSfDFNVGmafgfRFLVNTDAKKTGMKWSNIFLSTDSDSFLFAYVLGMLLADAFIYGLVAWYIEAVFPgeygvpkpWN 480
Cdd:TIGR01257 1834 IVFP-HFCLG-----RGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEGVVYFLLTLLIQ--------HH 1899
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 481 FFLmhSYWFGEPPQQKL-----EITQFYERVESKyfeAEPTDLtagIQIKHLHKVFqkNNTTKVAIKDLSLNLYEGQVTV 555
Cdd:TIGR01257 1900 FFL--SRWIAEPAKEPIfdeddDVAEERQRIISG---GNKTDI---LRLNELTKVY--SGTSSPAVDRLCVGVRPGECFG 1969
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 556 LLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLE 635
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEK 2049
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 636 ETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWD-ILQTYKQNRTILLTTHY 714
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRAVVLTSHS 2129
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 715 MDEADVLGDRIAIMVRGTLRCCGSSVFLKRLYGVGSHLVM-VKEP----YCDIAEISKLIHSYVPTATLETNVGNELSFI 789
Cdd:TIGR01257 2130 MEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPkddlLPDLNPVEQFFQGNFPGSVQRERHYNMLQFQ 2209
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 790 LPKEYTHRfeaLFTALEENQENLGISSFGVSITTMEEVFLKVSNLEDSKTDI 841
Cdd:TIGR01257 2210 VSSSSLAR---IFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
522-738 |
1.23e-45 |
|
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: 164.81 E-value: 1.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSL 600
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQ--NLLFdHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:COG1122 78 GLVFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1370-1574 |
1.77e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 166.90 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQFDALLEYMTGWEI 1449
Cdd:PRK13537 21 LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQFDNLDPDFTVREN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDT 1529
Cdd:PRK13537 101 LLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWER 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46358378 1530 VIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK13537 181 LRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
522-725 |
3.94e-45 |
|
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: 162.26 E-value: 3.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:COG4133 3 LEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMylEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQN-RTILLTTHymDEADVLGDRI 725
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARV 199
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
523-732 |
5.62e-45 |
|
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: 162.25 E-value: 5.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSLG 601
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQ--QNLLFdHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:cd03225 79 LVFQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGT 732
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
522-728 |
6.43e-45 |
|
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: 162.26 E-value: 6.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHmdqvRNSLG 601
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP----GPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 682 EPTSGMDPASRRSTWD-ILQTYKQNR-TILLTTHYMDEADVLGDRIAIM 728
Cdd:cd03293 157 EPFSALDALTREQLQEeLLDIWRETGkTVLLVTHDIDEAVFLADRVVVL 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
522-831 |
6.97e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 164.90 E-value: 6.97e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHmdqVRNSLG 601
Cdd:COG4152 2 LELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQN-RTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSVFLKRLYGVGSHLVMVKEpyc 760
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKgTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEADG--- 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 761 DIAEISKLihsyvPTATLETNVGNELSFILPKEYTHrfEALFTALeenQENLGISSFGVSITTMEEVFLKV 831
Cdd:COG4152 232 DAGWLRAL-----PGVTVVEEDGDGAELKLEDGADA--QELLRAL---LARGPVREFEEVRPSLNEIFIEV 292
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
522-734 |
1.48e-44 |
|
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: 161.00 E-value: 1.48e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 682 EPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1356-1564 |
4.25e-44 |
|
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: 159.37 E-value: 4.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKsplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTkniVKVRSKIGYCP 1435
Cdd:cd03269 3 VENVTKRFGR---VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03269 77 EERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPF 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:cd03269 157 SGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1356-1659 |
6.50e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 162.20 E-value: 6.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKiYFKSplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKnivKVRSKIGYCP 1435
Cdd:COG4152 4 LKGLTK-RFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP---EDRRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 qfdallE----Y--MTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:COG4152 78 ------EerglYpkMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFG-NIYILKAKV 1588
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGrNTLRLEADG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1589 KSGE--------TLDEFKNFITLTFPGSELQQEnqgilnyciprknnswgkvfgILEKAKEQYNLEDYSISQITLDQVF 1659
Cdd:COG4152 232 DAGWlralpgvtVVEEDGDGAELKLEDGADAQE---------------------LLRALLARGPVREFEEVRPSLNEIF 289
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1354-1565 |
1.11e-43 |
|
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: 158.69 E-value: 1.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIY-FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIG 1432
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
516-728 |
2.35e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 159.10 E-value: 2.35e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 516 TDLTAGIQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsqhmDQ 595
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 VRNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGS 675
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 676 KVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1372-1574 |
1.45e-42 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 159.61 E-value: 1.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQFDALLEYMTGWEIMI 1451
Cdd:PRK13536 57 VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRENLL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1452 MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVI 1531
Cdd:PRK13536 137 VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLR 216
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 1532 KIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK13536 217 SLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
522-731 |
2.70e-42 |
|
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: 154.36 E-value: 2.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqhmDQVRNSLG 601
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 682 EPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1356-1572 |
7.62e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 153.64 E-value: 7.62e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIGYC 1434
Cdd:COG1122 3 LENLSFSYPGGTPAL--DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQF-DALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLstAIAT---MgKPSVI 1509
Cdd:COG1122 81 FQNpDDQLFAPTVEE-DVAFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV--AIAGvlaM-EPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1356-1566 |
2.56e-41 |
|
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: 151.58 E-value: 2.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSpliLAVKNISLAIqERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCP 1435
Cdd:cd03264 3 LENLTKRYGKK---RALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03264 79 QEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1516 TGMDPRARrllwdtvIKIRE------SGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:cd03264 159 AGLDPEER-------IRFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
522-733 |
3.33e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 151.49 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ-----V 596
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQ--TYKQNRTILLTTHYMDEADvLGDRIAIMVRGTL 733
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
523-732 |
6.38e-41 |
|
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: 148.55 E-value: 6.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD-QVRNSLG 601
Cdd:cd00267 1 EIENLSFRYGG----RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQqnllfdhltvsehlyfycrikgvpqkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 682 EPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGT 732
Cdd:cd00267 106 EPTSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1371-1564 |
2.41e-40 |
|
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: 148.77 E-value: 2.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK-VRSKIGYCPQF--DALLEYMTGW 1447
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKeLRRKVGLVFQNpdDQFFGPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1448 EIMImYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLW 1527
Cdd:cd03225 96 EVAF-GLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELL 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 1528 DTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:cd03225 175 ELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
541-685 |
2.62e-40 |
|
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: 146.25 E-value: 2.62e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-QHMDQVRNSLGLCPQQNLLFDHLTVSEHL 619
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 YFYCRIKGVPQKMYLEETNNMLSAFNLM----EKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTS 685
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1356-1565 |
3.71e-40 |
|
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: 148.13 E-value: 3.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKsplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIvKVRSKIGYCP 1435
Cdd:cd03268 3 TNDLTKTYGK---KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQpyvkKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
522-733 |
4.72e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 4.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSL 600
Cdd:COG4619 1 LELEGLSFRVG----GKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHlTVSEHLYFYCRIKGvpQKMYLEETNNMLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIALIGGSKV 677
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRE--RKFDRERALELLERLGLPP--DILDKPverLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
522-732 |
1.98e-39 |
|
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: 145.02 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQV---RN 598
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQNLLFDHLTVSEhlyfycrikgvpqkmyleetnnmlsafNLMEkcdafskSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLE---------------------------NIAL-------GLSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQN--RTILLTTHYMDEADVLGDRIAIMVRGT 732
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
522-734 |
4.52e-39 |
|
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: 145.05 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsQHMDQVRNSLG 601
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKmyleETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIRKK----RIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 682 EPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
522-737 |
8.24e-39 |
|
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: 144.58 E-value: 8.24e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNsLG 601
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-IG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCG 737
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRELgiTTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
519-765 |
5.08e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 145.33 E-value: 5.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 519 TAGIQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRN 598
Cdd:PRK13537 5 VAPIDFRNVEKRYGD----KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQqnllFDHL----TVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGG 674
Cdd:PRK13537 81 RVGVVPQ----FDNLdpdfTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 675 SKVAILDEPTSGMDPASRRSTWDILQT-YKQNRTILLTTHYMDEADVLGDRIAIMVRGtlrccgssvflKRLYGVGSHLV 753
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG-----------RKIAEGAPHAL 225
|
250
....*....|..
gi 46358378 754 MVKEPYCDIAEI 765
Cdd:PRK13537 226 IESEIGCDVIEI 237
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
522-731 |
1.20e-37 |
|
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: 141.95 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRDINRELglTIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
522-738 |
1.39e-37 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 141.87 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:cd03261 1 IELRGLTKSFG----GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGV-PQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
522-738 |
1.92e-36 |
|
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: 138.57 E-value: 1.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknnTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:COG1127 6 IEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRELRDELglTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
539-733 |
3.24e-35 |
|
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: 134.87 E-value: 3.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCP--QQNLLFDHLTV- 615
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtfQIPRLFPELTVl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 -----------SEHLYFYCRIKGVPQkmYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPT 684
Cdd:cd03219 94 envmvaaqartGSGLLLARARREERE--ARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 685 SGMDPASRRSTWDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03219 172 AGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
522-733 |
3.37e-35 |
|
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: 135.12 E-value: 3.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQhMDQV--RNS 599
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE-QDPVelRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEK--CDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
522-733 |
3.53e-35 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 134.40 E-value: 3.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 N-SLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:COG1136 85 RrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADvLGDRIAIMVRGTL 733
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1356-1564 |
6.03e-35 |
|
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: 131.21 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKN-IVKVRSKIGYC 1434
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQFdalleymtgweimimyariwgisehqiqpyvkkylnsldleshanslistySEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1515 STGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
540-731 |
1.22e-34 |
|
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: 132.94 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI---SQHmDQVRNSLGLCPQQNLLFDHLTVS 616
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglPPH-ERARAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHL--YFYCRIKGVPQKMyLEEtnnMLSAF-NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRR 693
Cdd:cd03224 94 ENLllGAYARRRAKRKAR-LER---VYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 694 STWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:cd03224 170 EIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
522-733 |
1.52e-34 |
|
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: 132.63 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 -------------LCPQqnllfdhLTVSEHLY--FYCRIKGVPQKMYLEETNNMLSAFNLMEKC-DAFSKSLSGGMKRKL 665
Cdd:cd03257 82 keiqmvfqdpmssLNPR-------MTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 666 AIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
522-737 |
2.03e-34 |
|
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: 133.92 E-value: 2.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTK--------------------VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGE 581
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAfkllakgkskeeilkktgqtVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 582 AYVHGEDISQHMDQV-----RNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKS 656
Cdd:cd03294 81 VLIDGQDIAAMSRKElrelrRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 657 LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDI---LQTyKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEllrLQA-ELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
....
gi 46358378 734 RCCG 737
Cdd:cd03294 240 VQVG 243
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
538-731 |
2.31e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 135.73 E-value: 2.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSE 617
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDNLDLEFTVRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWD 697
Cdd:PRK13536 134 NLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWE 213
|
170 180 190
....*....|....*....|....*....|....*
gi 46358378 698 ILQT-YKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK13536 214 RLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1356-1545 |
1.35e-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: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLilaVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCP 1435
Cdd:COG4133 5 AENLSCRRGERLL---FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARIWGISEHQIQpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:COG4133 82 HADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPF 159
|
170 180 190
....*....|....*....|....*....|
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSH 1545
Cdd:COG4133 160 TALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
522-733 |
1.99e-33 |
|
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: 129.76 E-value: 1.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQ-----------------KNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYV 584
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 585 HGEDISQHMDQVRNSLGLC-PQQNLLFDHLTVSEHLYFYCRIKGVPQKMY---LEETNNMLsafNLMEKCDAFSKSLSGG 660
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFkkrLDELSELL---DLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 661 MKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
523-733 |
8.92e-33 |
|
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: 128.62 E-value: 8.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGL 602
Cdd:COG0411 6 EVRGLTKRFGGL----VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 603 CP--QQNLLFDHLTVSEHLY--FYCRIKGVPQKMYL-------------EETNNMLSAFNLMEKCDAFSKSLSGGMKRKL 665
Cdd:COG0411 82 ARtfQNPRLFPELTVLENVLvaAHARLGRGLLAALLrlprarreerearERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 666 AIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEadVLG--DRIAIMVRGTL 733
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERgiTILLIEHDMDL--VMGlaDRIVVLDFGRV 231
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
522-738 |
1.05e-32 |
|
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: 128.70 E-value: 1.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLhkVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS--QHMDQVRNS 599
Cdd:TIGR04520 1 IEVENV--SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLdeENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQ----QnllFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAI--IIALig 673
Cdd:TIGR04520 79 VGMVFQnpdnQ---FVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIagVLAM-- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 674 GSKVAILDEPTSGMDPASRRstwDILQTYKQ-----NRTILLTTHYMDEAdVLGDRIAIMVRGTLRCCGS 738
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRK---EVLETIRKlnkeeGITVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
522-734 |
1.89e-32 |
|
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: 126.36 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:TIGR03740 1 LETKNLSKRFGK----QTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDLHKIGSLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQqnlLFDHLTVSEHLYFYCRIKGVPQkmylEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:TIGR03740 77 ESPP---LYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 682 EPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
526-739 |
2.09e-32 |
|
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: 126.50 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 526 HLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQvRNSLGLC- 603
Cdd:cd03218 5 NLSKRYGK----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHK-RARLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 -PQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDE 682
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 683 PTSGMDPASRRSTWDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSS 739
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
519-738 |
2.54e-32 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 130.22 E-value: 2.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 519 TAGIQIKHLHKVFqknnTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS----QHmd 594
Cdd:COG3842 3 MPALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTglppEK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 qvRNsLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGG 674
Cdd:COG3842 77 --RN-VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 675 SKVAILDEPTSGMDPASRRSTW----DILQtyKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:COG3842 154 PRVLLLDEPLSALDAKLREEMReelrRLQR--ELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
522-728 |
2.74e-32 |
|
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: 124.03 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSL 600
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLdLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDhLTVSEhlyfycrikgvpqkmyleetnnmlsafNLmekcdafsksLSGGMKRKLAIIIALIGGSKVAIL 680
Cdd:cd03228 79 AYVPQDPFLFS-GTIRE---------------------------NI----------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 681 DEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADvLGDRIAIM 728
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVL 167
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1370-1572 |
3.37e-32 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 126.36 E-value: 3.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSKIGYCPQ---FDALLeYMTG 1446
Cdd:COG1121 20 PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQraeVDWDF-PITV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIMIMYA-------RIWGISEHQIqpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:COG1121 95 RDVVLMGRygrrglfRRPSRADREA---VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAGVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1520 PRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLsIMVRGRLTCLGSPQ 1572
Cdd:COG1121 172 AATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPE 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
522-733 |
5.88e-32 |
|
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: 132.72 E-value: 5.88e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKV-AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH----MDQV 596
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrsLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQ--QNLLFDHLTVSEHLYFYCRIKGV-PQKMYLEETNNMLSAFNLMEKC-DAFSKSLSGGMKRKLAIIIALI 672
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLaDRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 673 GGSKVAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
522-733 |
1.02e-31 |
|
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: 131.95 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPT---SGEAYVHGEDISQHMDQVR- 597
Cdd:COG1123 5 LEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLL-FDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:COG1123 83 RRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
522-733 |
4.43e-31 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 122.25 E-value: 4.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI---SQHMDQVRN 598
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQNLLFDHLTVSEHLYFYCR-IKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 678 AILDEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1369-1572 |
4.59e-31 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 122.93 E-value: 4.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQF--DALLEYMTG 1446
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFqiPRLFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WE-IMI---------MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:cd03219 93 LEnVMVaaqartgsgLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:cd03219 173 GLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPD 228
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
522-734 |
8.37e-31 |
|
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: 121.59 E-value: 8.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNsLG 601
Cdd:cd03301 1 VELENVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQ---KMYLEETNNMLSAFNLMEKcdaFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKdeiDERVREVAELLQIEHLLDR---KPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 679 ILDEPTSGMDPASR---RSTWDILQTyKQNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:cd03301 153 LMDEPLSNLDAKLRvqmRAELKRLQQ-RLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
522-733 |
1.17e-30 |
|
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: 119.07 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03216 1 LELRGITKRFGGV----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 lcpqqnllfdhltvsehlyfycrIKGVPQkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03216 77 -----------------------IAMVYQ--------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 682 EPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
522-748 |
3.47e-30 |
|
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: 120.92 E-value: 3.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqHMD--QVRNS 599
Cdd:COG1120 2 LEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSrrELARR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSE--------HLyfycRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIAL 671
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRElvalgrypHL----GLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 672 IGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS--SVF----LK 743
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLarERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPpeEVLtpelLE 232
|
....*
gi 46358378 744 RLYGV 748
Cdd:COG1120 233 EVYGV 237
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
531-737 |
3.56e-30 |
|
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: 120.07 E-value: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 531 FQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP---TSGEAYVHGEDISQHmdQVRNSLGLCPQQN 607
Cdd:cd03234 13 AKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 608 LLFDHLTVSEHLYFYCRI-------KGVPQKMyleETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAIL 680
Cdd:cd03234 91 ILLPGLTVRETLTYTAILrlprkssDAIRKKR---VEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 681 DEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHyMDEADV--LGDRIAIMVRGTLRCCG 737
Cdd:cd03234 168 DEPTSGLDSFTALNLVSTLsQLARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
523-728 |
3.79e-30 |
|
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: 119.28 E-value: 3.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHkvFQKNNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDqvRNSLGL 602
Cdd:cd03226 1 RIENIS--FSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER--RKSIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 603 CPQQ---NLLFDhlTVSEHLYFycRIKGVPQKmyLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:cd03226 76 VMQDvdyQLFTD--SVREELLL--GLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 680 LDEPTSGMDPASRRSTWD-ILQTYKQNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:cd03226 150 FDEPTSGLDYKNMERVGElIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1359-1576 |
1.20e-29 |
|
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: 118.80 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1359 LTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK--IGYCPQ 1436
Cdd:cd03218 6 LSKRYGKRK---VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARlgIGYLPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1437 FDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:cd03218 83 EASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN 1576
Cdd:cd03218 163 GVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
522-733 |
1.38e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 118.23 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTtkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 678 AILDEPTSGMDPAsrrSTWDILQTYKQ-NR---TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG2884 159 LLADEPTGNLDPE---TSWEIMELLEEiNRrgtTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
522-738 |
1.66e-29 |
|
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: 118.49 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsQHMDQVRNSLG 601
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03300 76 TVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKELgiTFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
540-731 |
3.50e-29 |
|
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: 117.39 E-value: 3.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ---HmDQVRNSLGLCPQQNLLFDHLTVS 616
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlppH-RIARLGIGYVPEGRRIFPSLTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLY--FYCRIKGVPQKMYLEEtnnMLSAF-NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRR 693
Cdd:COG0410 97 ENLLlgAYARRDRAEVRADLER---VYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 694 STWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:COG0410 174 EIFEIIRRLNrEGVTILLVEQNARFALEIADRAYVLERG 212
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
522-733 |
4.62e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 120.29 E-value: 4.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD----QVR 597
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEkelrKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQ-NLLFDHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:PRK11153 82 RQIGMIFQHfNLLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 677 VAILDEPTSGMDPASRRStwdILQTYKQ-NR----TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK11153 161 VLLCDEATSALDPATTRS---ILELLKDiNRelglTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
524-733 |
5.25e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 119.42 E-value: 5.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 524 IKHLhkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLC 603
Cdd:COG4586 24 LKGL---FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 -PQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDE 682
Cdd:COG4586 101 fGQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDE 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 683 PTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG4586 181 PTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMDDIEALCDRVIVIDHGRI 233
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
504-733 |
6.62e-29 |
|
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: 125.33 E-value: 6.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 504 ERVESKYFeAEPTDLTAGIQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAY 583
Cdd:COG2274 457 EREEGRSK-LSLPRLKGDIELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRIL 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 584 VHGEDISQ-HMDQVRNSLGLCPQQNLLF-----DHLTVS------EHLYFYCRIKGVpqkmyLEETNNMLSAFN--LMEk 649
Cdd:COG2274 534 IDGIDLRQiDPASLRRQIGVVLQDVFLFsgtirENITLGdpdatdEEIIEAARLAGL-----HDFIEALPMGYDtvVGE- 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 650 cdaFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH---YMDEAdvlgDRIA 726
Cdd:COG2274 608 ---GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRII 680
|
....*..
gi 46358378 727 IMVRGTL 733
Cdd:COG2274 681 VLDKGRI 687
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
538-753 |
8.00e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 116.73 E-value: 8.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsqhmDQVRNSLGLCPQQnLLFDH---LT 614
Cdd:COG1121 19 RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP----RRARRRIGYVPQR-AEVDWdfpIT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSE----HLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCD-AFSkSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:COG1121 94 VRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADrPIG-ELSGGQQQRVLLARALAQDPDLLLLDEPFAGVDA 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 690 ASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIaIMVRGTLRCCGS--SVF----LKRLYGVGSHLV 753
Cdd:COG1121 173 ATEEALYELLRELrREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPpeEVLtpenLSRAYGGPVALL 242
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1371-1569 |
1.15e-28 |
|
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: 115.32 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSKIGYCPQ-FDALLEY-MTGWE 1448
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG----KPLEKERKRIGYVPQrRSIDRDFpISVRD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIM--YARIWGIsehqiQPYVKKY-------LNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:cd03235 90 VVLMglYGHKGLF-----RRLSKADkakvdeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1520 PRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLsIMVRGRLTCLG 1569
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRV-LLLNRTVVASG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1354-1565 |
1.24e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 115.31 E-value: 1.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTkNIVKVRSKIGY 1433
Cdd:cd03259 1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03259 77 VFQDYALFPHLTVAE-NIAFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03259 156 EPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
512-738 |
1.41e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 122.95 E-value: 1.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 512 EAEPTDLTAGIQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ 591
Cdd:COG4987 324 EPAPAPGGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 HM-DQVRNSLGLCPQQNLLFDHlTVSEHLyfycRIkGVPQ----KMY--LEETNnmLSAF--NLMEKCDAF----SKSLS 658
Cdd:COG4987 402 LDeDDLRRRIAVVPQRPHLFDT-TLRENL----RL-ARPDatdeELWaaLERVG--LGDWlaALPDGLDTWlgegGRRLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 659 GGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADvLGDRIAIMVRGTLRCCGS 738
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGT 552
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
533-731 |
3.45e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 533 KNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS--QHMDQVRNSLGLCPQQ--NL 608
Cdd:PRK13633 18 EESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQNpdNQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LFDHLtVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:PRK13633 98 IVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 689 PASRRstwDILQTYKQ-----NRTILLTTHYMDEAdVLGDRIAIMVRG 731
Cdd:PRK13633 177 PSGRR---EVVNTIKElnkkyGITIILITHYMEEA-VEADRIIVMDSG 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
519-733 |
3.76e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 115.47 E-value: 3.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 519 TAGIQIKHLhkVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVR 597
Cdd:PRK13632 5 SVMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQ----QnllFDHLTVSEHLYFYCRIKGV-PQKM------YLEETNnmlsafnlMEK-CDAFSKSLSGGMKRKL 665
Cdd:PRK13632 83 KKIGIIFQnpdnQ---FIGATVEDDIAFGLENKKVpPKKMkdiiddLAKKVG--------MEDyLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 666 AIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEAdVLGDRIAIMVRGTL 733
Cdd:PRK13632 152 AIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKL 220
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1353-1571 |
5.81e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 115.53 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVLIKELTKIYFK-SPL-ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK---V 1427
Cdd:PRK13637 2 SIKIENLTHIYMEgTPFeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKlsdI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1428 RSKIGYCPQFDallEYMTGWEIM---IMYA-RIWGISEHQIQPYVKKYLN--SLDLESHANSLISTYSEGNKRRLSTAIA 1501
Cdd:PRK13637 82 RKKVGLVFQYP---EYQLFEETIekdIAFGpINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1502 TMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGK-AIIITSHSMEECEALCTRLSIMVRGRLTCLGSP 1571
Cdd:PRK13637 159 VAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1356-1572 |
6.40e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.97 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK--IGY 1433
Cdd:COG1137 6 AENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWE-IMIMyARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:COG1137 83 LPQEASIFRKLTVEDnILAV-LELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1513 EPSTGMDPRA----RRLlwdtVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG1137 162 EPFAGVDPIAvadiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPE 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
523-737 |
7.19e-28 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 111.76 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQhmdqvrnslgl 602
Cdd:cd03214 1 EVENLSVGYGG----RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 603 cpqqnllFDHLTVSEHLYFycrikgVPQkmyleetnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDE 682
Cdd:cd03214 66 -------LSPKELARKIAY------VPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 683 PTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG 737
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1372-1516 |
8.79e-28 |
|
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: 110.43 E-value: 8.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK-VRSKIGYCPQFDALLEYMTGWEIM 1450
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IMYARIWGISEHQIQPYVKKYLNSLDLESHANSLI----STYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
541-733 |
1.09e-27 |
|
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: 113.20 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNsLGLCPQQNLLFDHLTVSEHLY 620
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD-ISYVPQNYALFPHMTVYKNIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 621 FYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQ 700
Cdd:cd03299 94 YGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELK 173
|
170 180 190
....*....|....*....|....*....|....*
gi 46358378 701 TYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03299 174 KIRKEFgvTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1371-1572 |
2.20e-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: 112.82 E-value: 2.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIVK---VRSkigYcpQFDALLEY 1443
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphRIARlgiART---F--QNPRLFPE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MT---------------GWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSV 1508
Cdd:COG0411 94 LTvlenvlvaaharlgrGLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1509 IFLDEPSTGMDPRARRLLWDTVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG0411 174 LLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-733 |
2.21e-27 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 112.59 E-value: 2.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQV-RNSL 600
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLL-FD-HLTVSEHLYFYCRIKGVPQKMylEETNNMLSAFNLMEKC-DAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:COG1124 82 QMVFQDPYAsLHpRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLREERglTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1356-1571 |
2.80e-27 |
|
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: 112.39 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYC 1434
Cdd:cd03295 3 FENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLE--SHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSP 1571
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1356-1576 |
3.29e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 111.98 E-value: 3.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK--IGY 1433
Cdd:TIGR04406 4 AENLIKSYKKRK---VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARlgIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWE-IMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:TIGR04406 81 LPQEASIFRKLTVEEnIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN 1576
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
540-733 |
4.97e-27 |
|
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: 111.12 E-value: 4.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP-----PTSGEAYVHGEDISQHMDQV---RNSLGLCPQQNLLFd 611
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVlelRRRVGMVFQKPNPF- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 612 HLTVSEHLYFYCRIKGVPQKMYLEEtnnmlsafnLMEKC------------DAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:cd03260 94 PGSIYDNVAYGLRLHGIKLKEELDE---------RVEEAlrkaalwdevkdRLHALGLSGGQQQRLCLARALANEPEVLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03260 165 LDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
520-738 |
1.06e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 1.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 520 AGIQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNs 599
Cdd:COG3839 2 ASLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 680 LDEPTSGMDPASR---RStwDI--LQTyKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:COG3839 157 LDEPLSNLDAKLRvemRA--EIkrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1356-1570 |
1.64e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.59 E-value: 1.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYF-KSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRSK 1430
Cdd:cd03258 4 LKNVSKVFGdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1431 IGYCPQFDALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFE-NVALPlEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGS 1570
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGT 224
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1354-1560 |
1.68e-26 |
|
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: 109.10 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYF-KSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSKIG 1432
Cdd:cd03293 1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFL 1511
Cdd:cd03293 77 YVFQQDALLPWLTVLD-NVALGlELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIM 1560
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
541-733 |
1.87e-26 |
|
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: 108.41 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGL--YPPTSGEAYVHGedISQHMDQVRNSLGLCPQQNLLFDHLTVSEH 618
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING--RPLDKRSFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYFYCRIKGvpqkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDI 698
Cdd:cd03213 103 LMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 699 LQTY-KQNRTILLTTHYM-DEADVLGDRIAIMVRGTL 733
Cdd:cd03213 154 LRRLaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
522-731 |
2.49e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.18 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKN-NTTKVAIKDLSLNLYEGQ-VTVLlGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNS 599
Cdd:COG1101 2 LELKNLSKTFNPGtVNEKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 ----------LGLCPqqnllfdHLTVSEHLYF-YCRIK------GVPQKMYlEETNNMLSAFNL-ME-KCDAFSKSLSGG 660
Cdd:COG1101 81 yigrvfqdpmMGTAP-------SMTIEENLALaYRRGKrrglrrGLTKKRR-ELFRELLATLGLgLEnRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 661 MKRKLAIIIALIGGSKVAILDEPTSGMDPASRRS----TWDILQtyKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALvlelTEKIVE--ENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
522-728 |
4.61e-26 |
|
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: 108.81 E-value: 4.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVR 597
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEH-----LYFYCRIKGVPQKMYLEETNNMLSA---FNLMEKCDAFSKSLSGGMKRKLAIII 669
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAAlerVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 670 ALIGGSKVAILDEPTSGMDPASRRSTWDILQ--TYKQNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGL 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
522-733 |
4.67e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 111.32 E-value: 4.67e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQhMD-----QV 596
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTA-LSerelrAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQQ-NLLfDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGS 675
Cdd:COG1135 81 RRKIGMIFQHfNLL-SSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 676 KVAILDEPTSGMDPASRRStwdILQTYKQ-NR----TILLTTHymdEADV---LGDRIAIMVRGTL 733
Cdd:COG1135 160 KVLLCDEATSALDPETTRS---ILDLLKDiNRelglTIVLITH---EMDVvrrICDRVAVLENGRI 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
522-731 |
5.56e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.44 E-value: 5.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ-VRNSL 600
Cdd:PRK13647 5 IEVEDLH--FRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQ--QNLLFDhLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK13647 82 GLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 679 ILDEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
542-734 |
6.07e-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: 107.38 E-value: 6.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 542 KDLSLNL---YEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE---DISQHMD---QVRnSLGLCPQQNLLFDH 612
Cdd:cd03297 11 PDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKKINlppQQR-KIGLVFQQYALFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 613 LTVSEHLYF-YCRIKGVPQKMYLEEtnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS 691
Cdd:cd03297 90 LNVRENLAFgLKRKRNREDRISVDE---LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 692 RrstwDILQTYKQ------NRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:cd03297 167 R----LQLLPELKqikknlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
538-731 |
6.24e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 107.23 E-value: 6.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqhmdQVRNSLGLCPQQnLLFDH---LT 614
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE----KERKRIGYVPQR-RSIDRdfpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSE----HLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA 690
Cdd:cd03235 87 VRDvvlmGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 691 SRRSTWDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:cd03235 167 TQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
522-741 |
6.57e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.75 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNT-TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ---HMDQVR 597
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQ--QNLLFDHlTVSEHLYFycrikGvPQKMYLEE---TNNMLSAFNL--MEKCDAFSKS---LSGGMKRKLAI 667
Cdd:PRK13637 83 KKVGLVFQypEYQLFEE-TIEKDIAF-----G-PINLGLSEeeiENRVKRAMNIvgLDYEDYKDKSpfeLSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 668 --IIALigGSKVAILDEPTSGMDPASRRstwDILQTYKQ-----NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG--S 738
Cdd:PRK13637 156 agVVAM--EPKILILDEPTAGLDPKGRD---EILNKIKElhkeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGtpR 230
|
...
gi 46358378 739 SVF 741
Cdd:PRK13637 231 EVF 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
522-728 |
6.91e-26 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.57 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH--MDQVRNS 599
Cdd:COG1129 5 LEMRGISKSFGGV----KALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSEHLYF--YCRIKGV--PQKMYlEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGS 675
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLgrEPRRGGLidWRAMR-RRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 676 KVAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKaQGVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
521-738 |
7.13e-26 |
|
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: 108.20 E-value: 7.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 521 GIQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNsL 600
Cdd:cd03296 2 SIEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHLTVSEHLYFYCRIKGV----PQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 677 VAILDEPTSGMDPASRRS--TWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:cd03296 157 VLLLDEPFGALDAKVRKElrRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1356-1564 |
9.45e-26 |
|
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: 105.73 E-value: 9.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKsplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT---KNIVKVRSKIG 1432
Cdd:cd03229 3 LKNVSKRYGQ---KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdleDELPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEImIMYAriwgisehqiqpyvkkylnsldleshanslistYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03229 80 MVFQDFALFPHLTVLEN-IALG---------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRE-SGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1371-1579 |
1.13e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 115.61 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQFDALLEYMTGWEIM 1450
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTV 1530
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1531 IKI-RESGKAIIITSHSMEECEaLCTRLSIMVRGRLTCLGSPQYLKNKFG 1579
Cdd:NF033858 441 IELsREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
539-733 |
1.18e-25 |
|
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: 106.72 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ----VRNSLGLCPQQNLLFDHLT 614
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRS 694
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46358378 695 TWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03292 175 IMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
530-731 |
1.81e-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: 1.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 530 VFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNL 608
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LF-----DHLTVS------EHLYFYCRIKGVpqkmyLEETNNMLSAFNLM--EKCDafskSLSGGMKRKLAIIIALIGGS 675
Cdd:cd03245 89 LFygtlrDNITLGapladdERILRAAELAGV-----TDFVNKHPNGLDLQigERGR----GLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 676 KVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMdEADVLGDRIAIMVRG 731
Cdd:cd03245 160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
522-733 |
3.59e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 106.76 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSL 600
Cdd:PRK13648 8 IVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQ--QNLlFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK13648 86 GIVFQnpDNQ-FVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEAdVLGDRIAIMVRGTL 733
Cdd:PRK13648 165 ILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1354-1577 |
3.71e-25 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 105.78 E-value: 3.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSpliLAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTkNIVKVRSKIGY 1433
Cdd:cd03300 1 IELENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03300 77 VFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1514 PSTGMDPRARRllwDTVIKI----RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:cd03300 157 PLGALDLKLRK---DMQLELkrlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
522-731 |
3.88e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 111.66 E-value: 3.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknnTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE--DISQHMDQVRNS 599
Cdd:COG3845 6 LELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSEHLyfycrIKGVPQKMY----LEETNNMLSAfnLMEKC------DAFSKSLSGGMKRKLAIII 669
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENI-----VLGLEPTKGgrldRKAARARIRE--LSERYgldvdpDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 670 ALIGGSKVAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1372-1564 |
4.01e-25 |
|
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: 106.32 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAG-DVFIDGISLTK-NIVKVRSKIGYC-PQF-DALLEYMTGW 1447
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRIGLVsPALqLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1448 EIMI--MYARI--WG-ISEHQIQpYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:COG1119 99 DVVLsgFFDSIglYRePTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 1523 RRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:COG1119 178 RELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1368-1566 |
4.30e-25 |
|
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: 105.88 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1368 LILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYC-PQFDALLEYMTG 1446
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLL 1526
Cdd:cd03267 113 IDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46358378 1527 WDTV-IKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:cd03267 193 RNFLkEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
522-744 |
5.97e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 107.03 E-value: 5.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNT-TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ----- 595
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 VRNSLGLCPQ--QNLLFDHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIA 670
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPE--ELLARSpfeLSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 671 LIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS--SVFLKR 744
Cdd:PRK13634 160 LAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhkEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADP 237
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
489-738 |
6.30e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 109.35 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 489 FGEPPQQKLeitQFYERVESKYFEAEPTDLTAGIqikhlhkvfqknnttkvaiKDLSLNLYEGQVTVLLGHNGAGKSTTL 568
Cdd:PRK10070 14 FGEHPQRAF---KYIEQGLSKEQILEKTGLSLGV-------------------KDASLAIEEGEIFVIMGLSGSGKSTMV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 569 SILSGLYPPTSGEAYVHGEDISQHMDQV-----RNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSA 643
Cdd:PRK10070 72 RLLNRLIEPTRGQVLIDGVDIAKISDAElrevrRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 644 FNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVL 721
Cdd:PRK10070 152 VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRI 231
|
250
....*....|....*..
gi 46358378 722 GDRIAIMVRGTLRCCGS 738
Cdd:PRK10070 232 GDRIAIMQNGEVVQVGT 248
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
557-731 |
6.32e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 113.30 E-value: 6.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 557 LGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEE 636
Cdd:NF033858 298 LGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAAR 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 637 TNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHY 714
Cdd:NF033858 378 VAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELsrEDGVTIFISTHF 457
|
170
....*....|....*..
gi 46358378 715 MDEADvLGDRIAIMVRG 731
Cdd:NF033858 458 MNEAE-RCDRISLMHAG 473
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
540-741 |
6.47e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 106.37 E-value: 6.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-----MDQVRNSLGLCPQ--QNLLFDH 612
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkdIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 613 lTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISE--SLFEKNpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 690 ASRRSTWDILQTYKQN-RTILLTTHYMDEADVLGDRIAIMVRGTLRCCG--SSVF 741
Cdd:PRK13649 179 KGRKELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGkpKDIF 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1356-1565 |
7.39e-25 |
|
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: 104.49 E-value: 7.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPL-ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRS----- 1429
Cdd:cd03255 3 LKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 KIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEEcEALCTRLSIMVRGRL 1565
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
538-738 |
8.12e-25 |
|
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: 111.39 E-value: 8.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFdHLTVS 616
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLF-AGTIR 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLYFYcRIKGVPQKMY--LEETNnmlsafnlmekCDAFSKS---------------LSGGMKRKLAIIIALIGGSKVAI 679
Cdd:COG4988 429 ENLRLG-RPDASDEELEaaLEAAG-----------LDEFVAAlpdgldtplgeggrgLSGGQAQRLALARALLRDAPLLL 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHymDEADV-LGDRIAIMVRGTLRCCGS 738
Cdd:COG4988 497 LDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1372-1572 |
9.35e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 104.98 E-value: 9.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFID--GISLTKNIVKVRSKIGYCPQFDALLEYMTGWEI 1449
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdeDISLLPLHARARRGIGYLPQEASIFRRLSVYDN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARIW-GISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWD 1528
Cdd:PRK10895 99 LMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 1529 TVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK10895 179 IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPT 222
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
522-737 |
1.18e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 110.26 E-value: 1.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ--HMDQVRNS 599
Cdd:PRK09700 6 ISMAGIGKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNLLFDHLTVSEHLYF-------YCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALI 672
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhltkkVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 673 GGSKVAILDEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG 737
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMnQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
518-731 |
1.44e-24 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 107.61 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 518 LTAGIQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqHMDQVR 597
Cdd:PRK11607 16 LTPLLEIRNLTKSFDGQH----AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:PRK11607 91 RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 678 AILDEPTSGMDPASRR----STWDILQtyKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK11607 171 LLLDEPMGALDKKLRDrmqlEVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
522-731 |
1.66e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 105.10 E-value: 1.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLhkVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-QHMDQVRNSL 600
Cdd:PRK13635 6 IRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQ----QnllFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAI--IIALigG 674
Cdd:PRK13635 84 GMVFQnpdnQ---FVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIagVLAL--Q 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 675 SKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEAdVLGDRIAIMVRG 731
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKgiTVLSITHDLDEA-AQADRVIVMNKG 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1353-1572 |
2.07e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 109.61 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTkIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTG---ENIPTAGDVFIDGISLTKNIVKVR 1428
Cdd:COG1123 3 PLLeVRDLS-VRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEALR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1429 SK-IGYCPQ-FDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKP 1506
Cdd:COG1123 82 GRrIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1507 SVIFLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1355-1565 |
2.62e-24 |
|
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: 102.24 E-value: 2.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1355 LIKELTKIYFKSPLILaVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTA--GDVFIDGISLTKNivKVRSKIG 1432
Cdd:cd03213 9 LTVTVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKR--SFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEIMIMYARIWGIsehqiqpyvkkylnsldleshanslistySEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSM-EECEALCTRLSIMVRGRL 1565
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1356-1565 |
2.70e-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: 2.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY-FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKV----RSK 1430
Cdd:cd03257 4 VKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1431 IGYCPQ--FDALLEYMTGWEIMIMYARIWGI--SEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIATMGK 1505
Cdd:cd03257 84 IQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKlsKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1506 PSVIFLDEPSTGMDPRARRLLWDTVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1356-1576 |
4.35e-24 |
|
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: 102.58 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKiYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK----VRSKI 1431
Cdd:cd03261 3 LRGLTK-SFGGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQFDALLEYMTGWEIMIMYARIWGI-SEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKIRES-GKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN 1576
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
520-689 |
4.68e-24 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 102.80 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 520 AGIQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQ-VR 597
Cdd:COG1137 2 MTLEAENLVKSYGK----RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpMHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170
....*....|..
gi 46358378 678 AILDEPTSGMDP 689
Cdd:COG1137 158 ILLDEPFAGVDP 169
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1353-1572 |
4.97e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.45 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIY--FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIV 1425
Cdd:COG1123 259 PLLeVRNLSKRYpvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1426 KVRSKIGYCPQ--FDALLEYMTGWEIMIMYARIWGI-SEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIA 1501
Cdd:COG1123 339 ELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1502 TMGKPSVIFLDEPSTGMDPRAR----RLLWDTVikiRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQaqilNLLRDLQ---RELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTE 490
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1369-1658 |
8.51e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.40 E-value: 8.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKI----GycpQFDALLEYM 1444
Cdd:COG4586 35 VEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIgvvfG---QRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARR 1524
Cdd:COG4586 112 PAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1525 LLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYILKAKVKSGETLDEFKNFItl 1603
Cdd:COG4586 192 AIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGG-- 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1604 tfpgsELQQENQGILNYCIPRKNNswgkVFGILEKAKEQYNLEDYSISQITLDQV 1658
Cdd:COG4586 270 -----EVIEREGNRVRLEVDPRES----LAEVLARLLARYPVRDLTIEEPPIEEV 315
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1372-1572 |
2.11e-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: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQFDALLEYMTGWEIM 1450
Cdd:COG1120 17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVPQEPPAPFGLTVRELV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IM----YARIWGI---SEHQIqpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRAR 1523
Cdd:COG1120 97 ALgrypHLGLFGRpsaEDREA---VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1524 RLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:COG1120 174 LEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
520-728 |
2.39e-23 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.48 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 520 AGIQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsQHMDQVRns 599
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 lGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
522-733 |
2.43e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.17 E-value: 2.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNT-TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-----QHMDQ 595
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 VRNSLGLC---PQQNLLFDhlTVSEHLYFYcrikgvPQ--KMYLEETNNmlSAFNLMEKC----DAFSKS---LSGGMKR 663
Cdd:PRK13646 83 VRKRIGMVfqfPESQLFED--TVEREIIFG------PKnfKMNLDEVKN--YAHRLLMDLgfsrDVMSQSpfqMSGGQMR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 664 KLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK13646 153 KIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqtDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
521-733 |
2.96e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 100.47 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 521 GIQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE--DISQHMD---- 594
Cdd:COG4161 2 SIQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSekai 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 -QVRNSLGLCPQQNLLFDHLTVSEHLYFY-CRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALI 672
Cdd:COG4161 78 rLLRQKVGMVFQQYNLWPHLTVMENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 673 GGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR-TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGiTQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
522-769 |
4.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 101.42 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAY---VHGEDISQH-MDQVR 597
Cdd:PRK13640 6 VEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAKtVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQ-NLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEAdVLGDRIAIMVRGTLRCCGSSVflkrlyGVGSHLVM 754
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPV------EIFSKVEM 236
|
250
....*....|....*
gi 46358378 755 VKEPYCDIAEISKLI 769
Cdd:PRK13640 237 LKEIGLDIPFVYKLK 251
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
522-746 |
4.51e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.88 E-value: 4.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNslg 601
Cdd:PRK11432 7 VVLKNITKRFGSN----TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCP--QQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:PRK11432 80 ICMvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSvflKRLY 746
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP---QELY 225
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
508-737 |
4.85e-23 |
|
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: 99.53 E-value: 4.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 508 SKYFeaePTDLTAGIQIKHLHKVF-QKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHG 586
Cdd:cd03220 7 SKSY---PTYKGGSSSLKKLGILGrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 587 edisqhmdQVRNSLGLcpqqNLLFD-HLTVSEHLYFYCRIKGVPQKmYLEEtnnmlsafnLMEKCDAFS----------K 655
Cdd:cd03220 84 --------RVSSLLGL----GGGFNpELTGRENIYLNGRLLGLSRK-EIDE---------KIDEIIEFSelgdfidlpvK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 656 SLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQN-RTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:cd03220 142 TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
|
...
gi 46358378 735 CCG 737
Cdd:cd03220 222 FDG 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1356-1560 |
5.69e-23 |
|
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: 98.48 E-value: 5.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKnivKVRSK-IGYC 1434
Cdd:cd03226 2 IENISFSYKKGTEIL--DDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKsIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQ-FDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKY-LNSLDlESHANSListySEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03226 77 MQdVDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLdLYALK-ERHPLSL----SGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIM 1560
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLL 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
541-731 |
7.60e-23 |
|
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: 99.08 E-value: 7.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMdqvrnslgLCPQQNLLFDHLTVS 616
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpdRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLYFycRIKGVPQKMYLEETNNM----LSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:TIGR01184 73 ENIAL--AVDRVLPDLSKSERRAIveehIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46358378 693 RSTWD-ILQTYKQNR-TILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:TIGR01184 151 GNLQEeLMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
538-713 |
8.91e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 98.02 E-value: 8.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsqHMDQVRNS---LGlcpQQNLLFDHLT 614
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEAchyLG---HRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLYFYCRIKGVPQKMyLEETnnmLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRS 694
Cdd:PRK13539 90 VAENLEFWAAFLGGEELD-IAAA---LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 46358378 695 TWDILQTY-KQNRTILLTTH 713
Cdd:PRK13539 166 FAELIRAHlAQGGIVIAATH 185
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
543-733 |
1.08e-22 |
|
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: 97.95 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqHMDQVRNSLGLCPQQNLLFDHLTVSEHLYFy 622
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT-AAPPADRPVSMLFQENNLFAHLTVEQNVGL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 623 crikGVPQKMYLEETNN-----MLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWD 697
Cdd:cd03298 94 ----GLSPGLKLTAEDRqaievALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 46358378 698 ILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03298 170 LVLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1371-1571 |
1.09e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.00 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltknivkvrsKIGycpqfdALLEY------- 1443
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG------------RVS------ALLELgagfhpe 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEP-STGmDP-- 1520
Cdd:COG1134 103 LTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAaf 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1521 --RARRLLwdtvIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSP 1571
Cdd:COG1134 182 qkKCLARI----RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
522-689 |
1.18e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 98.93 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE--DISQHMD----- 594
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdkair 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 QVRNSLGLCPQQNLLFDHLTVSEHLYFY-CRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIG 673
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170
....*....|....*.
gi 46358378 674 GSKVAILDEPTSGMDP 689
Cdd:PRK11124 159 EPQVLLFDEPTAALDP 174
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
513-731 |
1.22e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 101.95 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 513 AEPTDLTAGIQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ- 591
Cdd:PRK09452 6 KQPSSLSPLVELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 -----HMDQVRnslglcpQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLA 666
Cdd:PRK09452 82 paenrHVNTVF-------QSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 667 IIIALIGGSKVAILDEPTSGMDPASRR---STWDILQTyKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK09452 155 IARAVVNKPKVLLLDESLSALDYKLRKqmqNELKALQR-KLGITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
522-753 |
1.25e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 99.81 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLhKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-QHMDQVRNSL 600
Cdd:PRK13650 5 IEVKNL-TFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQ-NLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 680 LDEPTSGMDPASRRstwDILQTYKQNR-----TILLTTHYMDEAdVLGDRIAIMVRGTLRccgSSVFLKRLYGVGSHLV 753
Cdd:PRK13650 164 LDEATSMLDPEGRL---ELIKTIKGIRddyqmTVISITHDLDEV-ALSDRVLVMKNGQVE---STSTPRELFSRGNDLL 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
522-733 |
1.73e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.69 E-value: 1.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTL-SI--LSGLYP--PTSGEAYVHGEDI-SQHMDQ 595
Cdd:PRK14239 6 LQVSDLSVYYNK----KKALNSVSLDFYPNEITALIGPSGSGKSTLLrSInrMNDLNPevTITGSIVYNGHNIySPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 V--RNSLGLCPQQNLLFDhLTVSEHLYFYCRIKGVPQKMYLEET--NNMLSAFNLMEKCDAFSKS---LSGGMKRKLAII 668
Cdd:PRK14239 82 VdlRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAveKSLKGASIWDEVKDRLHDSalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 669 IALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
522-717 |
2.14e-22 |
|
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: 96.23 E-value: 2.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLG 601
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHlTVSEHLyfycrikgvpqkmyleetnnmlsafnlmekcdafSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKQNRTILLTTH------YMDE 717
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTLIWITHhltgieHMDK 165
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1344-1583 |
3.59e-22 |
|
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: 98.10 E-value: 3.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1344 YQPEKFLNCPVLIKELTKIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-- 1421
Cdd:cd03294 12 KNPQKAFKLLAKGKSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAam 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1422 --KNIVKVRSK-IGYCPQFDALLEYMT-------GWEIMimyariwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEG 1491
Cdd:cd03294 92 srKELRELRRKkISMVFQSFALLPHRTvlenvafGLEVQ-------GVPRAEREERAAEALELVGLEGWEHKYPDELSGG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1492 NKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGS 1570
Cdd:cd03294 165 MQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
250
....*....|...
gi 46358378 1571 PQYLKNKFGNIYI 1583
Cdd:cd03294 245 PEEILTNPANDYV 257
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1356-1566 |
3.93e-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: 94.80 E-value: 3.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYfksPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK--VRSKIGy 1433
Cdd:cd03216 3 LRGITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRdaRRAGIA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 cpqfdalleymtgweiMImyariwgiseHQIqpyvkkylnsldleshanslistySEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03216 79 ----------------MV----------YQL------------------------SVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1514 PSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1369-1579 |
4.25e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 99.81 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTfQILTGENIPTAGDVFIDGISLTKNIVKVRSKIG-YCPQFDALLEYMTGW 1447
Cdd:NF000106 26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1448 EIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLW 1527
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1528 DTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFG 1579
Cdd:NF000106 185 DEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
541-738 |
4.53e-22 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 97.27 E-value: 4.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS---QHmDQVRNSLGLCPQQNLLFDHLTVSE 617
Cdd:PRK10895 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllpLH-ARARRGIGYLPQEASIFRRLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTW 696
Cdd:PRK10895 98 NLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 697 DILQTYKQNRT-ILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:PRK10895 178 RIIEHLRDSGLgVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1355-1583 |
5.49e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.49 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1355 LIKELtkIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIVKV-RS 1429
Cdd:PRK10070 29 LSKEQ--ILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVrRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 KIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYI 1583
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1354-1627 |
7.48e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 7.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSkIGY 1433
Cdd:PRK11432 7 VVLKNITKRFGSNTVI---DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD-ICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:PRK11432 83 VFQSYALFPHMSLGE-NVGYGlKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1513 EPSTGMDPRARRLLWDtviKIRESGKAIIITS----HSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYIlkakv 1588
Cdd:PRK11432 162 EPLSNLDANLRRSMRE---KIRELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFM----- 233
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 46358378 1589 ksgetldefKNFI--TLTFPGSeLQQENQGILNYCIPRKNN 1627
Cdd:PRK11432 234 ---------ASFMgdANIFPAT-LSGDYVDIYGYRLPRPAA 264
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
538-717 |
8.94e-22 |
|
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: 96.31 E-value: 8.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSG-EAYVHGEDISQH-MDQVRNSLGLC-PQQNLLFD-HL 613
Cdd:COG1119 16 KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdVWELRKRIGLVsPALQLRFPrDE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVSEHLY--FYCRIkGVPQKmYLEE----TNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:COG1119 96 TVLDVVLsgFFDSI-GLYRE-PTDEqrerARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGL 173
|
170 180 190
....*....|....*....|....*....|..
gi 46358378 688 DPASRRSTWDILQTY--KQNRTILLTTHYMDE 717
Cdd:COG1119 174 DLGARELLLALLDKLaaEGAPTLVLVTHHVEE 205
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1369-1569 |
1.19e-21 |
|
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: 95.29 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltknivKVRSKIGYCPQFDALLeymTGWE 1448
Cdd:cd03220 35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG--------RVSSLLGLGGGFNPEL---TGRE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEP-STGmDPRARRLLW 1527
Cdd:cd03220 104 NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQ 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 1528 DTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:cd03220 183 RRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1356-1592 |
2.23e-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: 97.86 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKV---RSKIG 1432
Cdd:COG3842 8 LENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppeKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEImIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRR--LSTAIATmgKPSVI 1509
Cdd:COG3842 81 MVFQDYALFPHLTVAEN-VAFGlRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRvaLARALAP--EPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL----KNKF-----G 1579
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATRFvadfiG 237
|
250
....*....|...
gi 46358378 1580 NIYILKAKVKSGE 1592
Cdd:COG3842 238 EANLLPGTVLGDE 250
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
522-738 |
2.49e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 95.15 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQ------------------KNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAY 583
Cdd:COG1134 5 IEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 584 VHGEdISqhmdqvrnSL-----GLCPQqnllfdhLTVSEHLYFYCRIKGVPQKMYLEetnnmlsafnLMEKCDAFS---- 654
Cdd:COG1134 85 VNGR-VS--------ALlelgaGFHPE-------LTGRENIYLNGRLLGLSRKEIDE----------KFDEIVEFAelgd 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 655 ------KSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA-SRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAI 727
Cdd:COG1134 139 fidqpvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|.
gi 46358378 728 MVRGTLRCCGS 738
Cdd:COG1134 219 LEKGRLVMDGD 229
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
522-744 |
2.52e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 96.07 E-value: 2.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI---SQHMDQVRN 598
Cdd:PRK13636 6 LKVEELN--YNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQ--NLLFDhLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:PRK13636 83 SVGMVFQDpdNQLFS-ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPK 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG--SSVFLKR 744
Cdd:PRK13636 162 VLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEK 233
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
543-732 |
4.76e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.67 E-value: 4.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNlyEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIsqhmdqvrnsLGLCP---------QQNLLFDHL 613
Cdd:COG3840 19 DLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL----------TALPPaerpvsmlfQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVSEHLYF----YCRIkGVPQKMYLEEtnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:COG3840 87 TVAQNIGLglrpGLKL-TAEQRAQVEQ---ALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46358378 690 ASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRGT 732
Cdd:COG3840 163 ALRQEMLDLVDELcrERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1328-1572 |
4.87e-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: 99.11 E-value: 4.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1328 GTSEDndVENERREILYQPEKFLNC----PVL-IKELTKIYF--KSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQ 1400
Cdd:TIGR03269 251 GTPDE--VVAVFMEGVSEVEKECEVevgePIIkVRNVSKRYIsvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1401 ILTGENIPTAGDVFI----DGISLTKNIVKVRSK----IGYCPQFDAL------LEYMT---GWEIMIMYARIWGISEHQ 1463
Cdd:TIGR03269 329 IIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRGRakryIGILHQEYDLyphrtvLDNLTeaiGLELPDELARMKAVITLK 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1464 IQPYVKKYlnsldLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRES-GKAIII 1542
Cdd:TIGR03269 409 MVGFDEEK-----AEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFII 483
|
250 260 270
....*....|....*....|....*....|
gi 46358378 1543 TSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:TIGR03269 484 VSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1360-1548 |
5.06e-21 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 93.58 E-value: 5.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1360 TKIYFKSPLILavKNISLAIQEracfG----LLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIVKVRSKI 1431
Cdd:COG2884 8 SKRYPGGREAL--SDVSLEIEK----GefvfLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQfDA-LLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:COG2884 82 GVVFQ-DFrLLPDRTVYE-NVALPlRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSME 1548
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1354-1569 |
5.78e-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: 93.09 E-value: 5.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSkIGY 1433
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1514 PSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1356-1613 |
5.91e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 96.30 E-value: 5.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY-FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRSK 1430
Cdd:COG1135 4 LENLSKTFpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTalseRELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1431 IGYCPQFDALLEYMTGWEiMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAE-NVALPlEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1510 FLDEPSTGMDPRARR----LLWDtvikI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLtclgspqylknkfgniyil 1584
Cdd:COG1135 163 LCDEATSALDPETTRsildLLKD----InRELGLTIVLITHEMDVVRRICDRVAVLENGRI------------------- 219
|
250 260
....*....|....*....|....*....
gi 46358378 1585 kakVKSGETLDEFKNfitltfPGSELQQE 1613
Cdd:COG1135 220 ---VEQGPVLDVFAN------PQSELTRR 239
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
522-749 |
7.41e-21 |
|
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: 92.20 E-value: 7.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGL--YPPTSGEAYVHGEDISqHM---DQV 596
Cdd:cd03217 1 LEIKDLHVSVGG----KEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT-DLppeERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQQNLlfdhltvsehlyfycRIKGVPQKMYLEETNnmlsafnlmekcdafsKSLSGGMKRKLAIIIALIGGSK 676
Cdd:cd03217 76 RLGIFLAFQYPP---------------EIPGVKNADFLRYVN----------------EGFSGGEKKRNEILQLLLLEPD 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEAD-VLGDRIAIMVRGTLRCCGSSVFLKRLYGVG 749
Cdd:cd03217 125 LAILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
544-713 |
1.08e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 91.65 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQvrnslglcPQQNLLF-DH-------LTV 615
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE--------PHENILYlGHlpglkpeLSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLYFYCRIKGVPQKMYLEetnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRST 695
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170
....*....|....*....
gi 46358378 696 WDILQTYKQNRTI-LLTTH 713
Cdd:TIGR01189 167 AGLLRAHLARGGIvLLTTH 185
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
522-733 |
1.11e-20 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 92.85 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI-SQHMD--QVRN 598
Cdd:PRK09493 2 IEFKNVSKHF---GPTQV-LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVnDPKVDerLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQNLLFDHLTVSEHLYF-YCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:PRK09493 78 EAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLaEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
539-733 |
1.57e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 93.60 E-value: 1.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS---QHMDQVRNSLGLCPQQ--NLLFDHl 613
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNpdDQLFAP- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRR 693
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 694 STWDILqtYKQNR---TILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK13639 175 QIMKLL--YDLNKegiTIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1356-1569 |
1.66e-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: 90.57 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK-IGYC 1434
Cdd:cd03214 2 VENLSVGYGGRTVL---DDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARkIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQfdaLLEYMtgweimimyariwgisehQIQPYVKKYLNSLdleshanslistySEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:cd03214 79 PQ---ALELL------------------GLAHLADRPFNEL-------------SGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1515 STGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1371-1564 |
2.05e-20 |
|
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: 91.73 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK--NIVKVRSKIGYCPQFDALLEYMTGWE 1448
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpPHERARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIMYARIWGISEHQIQ--------PYVKKYLNSLdleshANSListySEGNKRRLSTAIATMGKPSVIFLDEPSTGMDP 1520
Cdd:cd03224 95 NLLLGAYARRRAKRKARlervyelfPRLKERRKQL-----AGTL----SGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 1521 RARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1369-1565 |
2.06e-20 |
|
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: 91.50 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALLEYMT-- 1445
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQ-DVTLFYGTlr 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1446 ---------GWEIMIMYA-RIWGISEhqiqpYVKKYLNSLDLE--SHANSListySEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:cd03245 96 dnitlgaplADDERILRAaELAGVTD-----FVNKHPNGLDLQigERGRGL----SGGQRQAVALARALLNDPPILLLDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1514 PSTGMDPRARRLLwdtVIKIRE--SGKAIIITSH--SMEEceaLCTRLSIMVRGRL 1565
Cdd:cd03245 167 PTSAMDMNSEERL---KERLRQllGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
537-713 |
2.41e-20 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 96.97 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 537 TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHlTV 615
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLYFYCR------IKGVPQKMYLEETNNMLSAfNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:TIGR02857 413 AENIRLARPdasdaeIREALERAGLDEFVAALPQ-GLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180
....*....|....*....|....
gi 46358378 690 ASRRSTWDILQTYKQNRTILLTTH 713
Cdd:TIGR02857 492 ETEAEVLEALRALAQGRTVLLVTH 515
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1356-1585 |
2.69e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.83 E-value: 2.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPL-ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT---KNIVKVRSKI 1431
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQ------FDALLEYMTGWEIMIMyariwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTA-IATMg 1504
Cdd:PRK13639 81 GIVFQnpddqlFAPTVEEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAgILAM- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1505 KPSVIFLDEPSTGMDPRA----RRLLWDtvikIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPqylKNKFGN 1580
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGasqiMKLLYD----LNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP---KEVFSD 227
|
....*
gi 46358378 1581 IYILK 1585
Cdd:PRK13639 228 IETIR 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1354-1583 |
3.09e-20 |
|
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: 91.63 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRsKIGY 1433
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER-NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMI----MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAfglrVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1510 FLDEPSTGMDPRARRLL--WdtvikIRESGKAIIITS----HSMEECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYI 1583
Cdd:cd03296 159 LLDEPFGALDAKVRKELrrW-----LRRLHDELHVTTvfvtHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
515-713 |
3.73e-20 |
|
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: 90.99 E-value: 3.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 515 PTDLTAGIQIKHLHKVFQKNNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD 594
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 Q-VRNSLGLCPQQNLLFDHlTVSEHLYFycRIKGVPQKMYLE--ETNNMLSAFNLMEK---CDAFSKS--LSGGMKRKLA 666
Cdd:cd03248 84 KyLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKEaaQKAHAHSFISELASgydTEVGEKGsqLSGGQKQRVA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 667 IIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAH 207
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1365-1545 |
3.79e-20 |
|
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: 91.18 E-value: 3.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1365 KSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTG--ENIPTA-GDVFIDGISLTKNivKVRSKIGYCPQFDALL 1441
Cdd:cd03234 18 KYARIL--NDVSLHVESGQVMAILGSSGSGKTTLLDAISGrvEGGGTTsGQILFNGQPRKPD--QFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1442 EYMTGWEiMIMYARIWGISEHQIQPYVKK-----YLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:cd03234 94 PGLTVRE-TLTYTAILRLPRKSSDAIRKKrvedvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172
|
170 180
....*....|....*....|....*....
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSH 1545
Cdd:cd03234 173 GLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1357-1565 |
4.58e-20 |
|
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: 90.54 E-value: 4.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1357 KELTKIYfkSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRSKIG 1432
Cdd:cd03292 4 INVTKTY--PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
539-719 |
5.49e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 97.12 E-value: 5.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ--HMDQVrnslglCPQ-----QNL--- 608
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarHRRAV------CPRiaympQGLgkn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLmekcDAF-----SKsLSGGMKRKLAIIIALIGGSKVAILDEP 683
Cdd:NF033858 89 LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFadrpaGK-LSGGMKQKLGLCCALIHDPDLLILDEP 163
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 684 TSGMDPASRRSTWDILQTYKQNR---TILLTTHYMDEAD 719
Cdd:NF033858 164 TTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1371-1582 |
5.73e-20 |
|
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: 91.09 E-value: 5.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRSKIGYCPQFDALLEYMTG 1446
Cdd:cd03256 16 ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLRRQIGMIFQQFNLIERLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEiMIMYAR------IWGI----SEHQIQpYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:cd03256 96 LE-NVLSGRlgrrstWRSLfglfPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1517 GMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNK-FGNIY 1582
Cdd:cd03256 174 SLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEvLDEIY 241
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
538-733 |
8.27e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 91.81 E-value: 8.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI-----SQHMDQVRNSLGLCPQ--QNLLF 610
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVFQfpEAQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 DHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:PRK13641 100 EN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSE--DLISKSpfeLSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 688 DPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
522-731 |
9.73e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 92.84 E-value: 9.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNsLG 601
Cdd:PRK10851 3 IEIANIKKSF---GRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYCRI---KGVPQKMYL-EETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAFGLTVlprRERPNAAAIkAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 678 AILDEPTSGMDPASRRS--TWdILQTYKQNR-TILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK10851 158 LLLDEPFGALDAQVRKElrRW-LRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQG 213
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
541-751 |
1.18e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 90.56 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH----MDQVRnslGLCPQQNLL-FDhLTV 615
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWspweLARRR---AVLPQHSSLaFP-FTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SE--------HLYFYCRIKGVPQKmYLEETNnmlsafnlmekCDAFSK----SLSGGMKRK--LAIIIALI-----GGSK 676
Cdd:COG4559 93 EEvvalgrapHGSSAAQDRQIVRE-ALALVG-----------LAHLAGrsyqTLSGGEQQRvqLARVLAQLwepvdGGPR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYKQNR----TIL----LTTHYmdeadvlGDRIAIMVRGTLRCCGS--SVF----L 742
Cdd:COG4559 161 WLFLDEPTSALDLAHQHAVLRLARQLARRGggvvAVLhdlnLAAQY-------ADRILLLHQGRLVAQGTpeEVLtdelL 233
|
250
....*....|...
gi 46358378 743 KRLYG----VGSH 751
Cdd:COG4559 234 ERVYGadlrVLAH 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
544-713 |
1.45e-19 |
|
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: 88.70 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEHLYFYC 623
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 624 RIKGVPQkmyLEETnnmLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS-RRSTWDILQTY 702
Cdd:cd03231 99 ADHSDEQ---VEEA---LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGvARFAEAMAGHC 172
|
170
....*....|.
gi 46358378 703 KQNRTILLTTH 713
Cdd:cd03231 173 ARGGMVVLTTH 183
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
522-741 |
1.76e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 90.95 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNT-TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTS-----GEAYVHGEDISQHMDQ 595
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEgkvtvGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 VRNSLGLCPQ--QNLLFDHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIA 670
Cdd:PRK13643 82 VRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAD--EFWEKSpfeLSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 671 LIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQN-RTILLTTHYMDEADVLGDRIAIMVRGTLRCCG--SSVF 741
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVF 232
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1371-1587 |
1.83e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-----KNIVKVRSKIGYCPQF-DALLEYM 1444
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVFQFpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYARIWGISEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTA-IATMgKPSVIFLDEPSTGMDPRA 1522
Cdd:PRK13649 102 TVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAgILAM-EPKILVLDEPTAGLDPKG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1523 RRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPqylKNKFGNIYILKAK 1587
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP---KDIFQDVDFLEEK 242
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
540-733 |
2.81e-19 |
|
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: 94.01 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSLGLCPQQNLLFDHlTVSEH 618
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYtLASLRRQVALVSQDVVLFND-TIANN 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYfYCRIKGVPQkmylEETNNMLSAFNLMEKCDAFSKS-----------LSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:TIGR02203 426 IA-YGRTEQADR----AEIERALAAAYAQDFVDKLPLGldtpigengvlLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 688 DPASRRSTWDILQTYKQNRTILLTTHYMDEADVlGDRIAIMVRGTL 733
Cdd:TIGR02203 501 DNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
518-713 |
3.06e-19 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.02 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 518 LTAGIQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQV 596
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 ----RNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALI 672
Cdd:PRK10535 81 aqlrREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 673 GGSKVAILDEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTH 713
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILhQLRDRGHTVIIVTH 202
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
522-728 |
3.39e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.50 E-value: 3.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP---TSGEAYVHGEDISQ----HMD 594
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 QVR------------NSLglcpqqNLLFdhlTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKCDAFSK---SLS 658
Cdd:COG0444 82 KIRgreiqmifqdpmTSL------NPVM---TVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLDRyphELS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 659 GGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIM 728
Cdd:COG0444 153 GGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELglAILFITHDLGVVAEIADRVAVM 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1371-1577 |
4.38e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 89.41 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIGYCPQF-DALLEYMTGWE 1448
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWD 1528
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 1529 TVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
512-733 |
4.38e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.81 E-value: 4.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 512 EAEPTDLtagIQIKHLHKVFqknnTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ 591
Cdd:PRK15439 5 DTTAPPL---LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 HMDQVRNSLG--LCPQQNLLFDHLTVSEHLYFycrikGVPQKMYLEE-TNNMLSAFNLMEKCDAFSKSLSGGMKRKLAII 668
Cdd:PRK15439 78 LTPAKAHQLGiyLVPQEPLLFPNLSVKENILF-----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 669 IALIGGSKVAILDEPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1356-1547 |
4.41e-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: 87.59 E-value: 4.41e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKiYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT---KNIVKVRSKIG 1432
Cdd:cd03262 3 IKNLHK-SFGDFHVL--KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEiMIMYARIW--GISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:cd03262 80 MVFQQFNLFPHLTVLE-NITLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSM 1547
Cdd:cd03262 159 FDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
539-713 |
4.71e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 92.81 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHlTVSE 617
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYFYCriKGVPQkmylEETNNMLSAFNLMEKCDAF-----------SKSLSGGMKRKLAIIIALIGGSKVAILDEPTSG 686
Cdd:TIGR02868 428 NLRLAR--PDATD----EELWAALERVGLADWLRALpdgldtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEH 501
|
170 180
....*....|....*....|....*..
gi 46358378 687 MDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:TIGR02868 502 LDAETADELLEDLLAALSGRTVVLITH 528
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
533-733 |
4.74e-19 |
|
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: 86.33 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 533 KNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI---SQHmDQVRNSLGLCP---QQ 606
Cdd:cd03215 8 RGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrrSPR-DAIRAGIAYVPedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 607 NLLFDHLTVSEhlyfycrikgvpqkmyleetnNMlsafnlmekcdAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSG 686
Cdd:cd03215 87 EGLVLDLSVAE---------------------NI-----------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 687 MDPASRRSTWD-ILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:cd03215 135 VDVGAKAEIYRlIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
522-748 |
6.06e-19 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 88.22 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSL 600
Cdd:COG4604 2 IEIKNVSKRYG----GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHLTVSEHLYF----YCriKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGmKRKLAII-IALIGGS 675
Cdd:COG4604 78 AILRQENHINSRLTVRELVAFgrfpYS--KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFIaMVLAQDT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 676 KVAILDEPTSGMDPASRRSTWDILQ--TYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS------SVFLKRLYG 747
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRrlADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTpeeiitPEVLSDIYD 234
|
.
gi 46358378 748 V 748
Cdd:COG4604 235 T 235
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
540-733 |
8.17e-19 |
|
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: 92.17 E-value: 8.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVH-GEDISQHMD-------QVRNSLGLCPQQNLLFD 611
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKpgpdgrgRAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 612 HLTVSEHLYFYCRIKgVPQKMYLEETNNMLSAFNLMEK-----CDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSG 686
Cdd:TIGR03269 379 HRTVLDNLTEAIGLE-LPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 687 MDPASRRSTWD-ILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:TIGR03269 458 MDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1371-1565 |
8.40e-19 |
|
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: 87.24 E-value: 8.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTG-----ENIPTAGDVFIDG---ISLTKNIVKVRSKIGYCPQFDALLE 1442
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiYDLDVDVLELRRRVGMVFQKPNPFP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 yMTGWEIMIMYARIWGISEH-QIQPYVKKYLNSLDL------ESHANSListySEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03260 95 -GSIYDNVAYGLRLHGIKLKeELDERVEEALRKAALwdevkdRLHALGL----SGGQQQRLCLARALANEPEVLLLDEPT 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESgKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03260 170 SALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1358-1590 |
1.60e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 87.35 E-value: 1.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKIYFKSPLI--LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYC 1434
Cdd:PRK13632 9 KVENVSFSYPNSenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKeNLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 ---P--QFDAL---------LEymtgwEIMIMYARIWGIsehqIQPYVKK--YLNSLDLESHanSListySEGNKRRLST 1498
Cdd:PRK13632 89 fqnPdnQFIGAtveddiafgLE-----NKKVPPKKMKDI----IDDLAKKvgMEDYLDKEPQ--NL----SGGQKQRVAI 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1499 AIATMGKPSVIFLDEpSTGM-DPRARRLLWDTVIKIRESG-KAIIITSHSMEECeALCTRLSIMVRGRLTCLGSPQ-YLK 1575
Cdd:PRK13632 154 ASVLALNPEIIIFDE-STSMlDPKGKREIKKIMVDLRKTRkKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKeILN 231
|
250
....*....|....*
gi 46358378 1576 NKfgNIyILKAKVKS 1590
Cdd:PRK13632 232 NK--EI-LEKAKIDS 243
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
537-770 |
1.66e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 86.99 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 537 TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD-QVRNSLGLCPQQNLLFDHLTV 615
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLPQHHLTPEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 --------SEHLYFYCRIKG-----VPQKMYLEETNnmlsafNLMEKCDAfskSLSGGMKRKLAIIIALIGGSKVAILDE 682
Cdd:PRK11231 94 relvaygrSPWLSLWGRLSAednarVNQAMEQTRIN------HLADRRLT---DLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 683 PTSGMDPASRRSTWDILQTYKQN-RTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSsvflkrlygvgSHLVMVKEPYCD 761
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELNTQgKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT-----------PEEVMTPGLLRT 233
|
....*....
gi 46358378 762 IAEISKLIH 770
Cdd:PRK11231 234 VFDVEAEIH 242
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
538-751 |
1.74e-18 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 87.13 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVRNSLglcPQQ-NLLFDh 612
Cdd:PRK13548 15 RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRRAVL---PQHsSLSFP- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 613 LTVSE--------HLYFYCRIKGVPQKmYLEETNnmlsafnlmekCDAFSK----SLSGGMK------RKLAIIIALIGG 674
Cdd:PRK13548 91 FTVEEvvamgrapHGLSRAEDDALVAA-ALAQVD-----------LAHLAGrdypQLSGGEQqrvqlaRVLAQLWEPDGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 675 SKVAILDEPTSGMDPASRRSTWDILQ--TYKQNRTIL-------LTTHYmdeadvlGDRIAIMVRGTLRCCGS--SVF-- 741
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARqlAHERGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGTpaEVLtp 231
|
250
....*....|....*.
gi 46358378 742 --LKRLYG----VGSH 751
Cdd:PRK13548 232 etLRRVYGadvlVQPH 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
541-721 |
2.07e-18 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 85.61 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP---TSGEAYVHGEDISQHMDQVRNsLGLCPQQNLLFDHLTVSE 617
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-IGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYFycrikGVPQKMYLEE----TNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRR 693
Cdd:COG4136 96 NLAF-----ALPPTIGRAQrrarVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
|
170 180 190
....*....|....*....|....*....|
gi 46358378 694 ST--WDILQTYKQNRTILLTTHymDEADVL 721
Cdd:COG4136 171 QFreFVFEQIRQRGIPALLVTH--DEEDAP 198
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
522-731 |
2.36e-18 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 86.34 E-value: 2.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNnttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVhGE---DISQHMDQ--- 595
Cdd:PRK11264 4 IEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDitiDTARSLSQqkg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 ----VRNSLGLCPQQNLLFDHLTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIA 670
Cdd:PRK11264 79 lirqLRQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 671 LIGGSKVAILDEPTSGMDPasrRSTWDILQTYKQ----NRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
543-738 |
2.87e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 88.63 E-value: 2.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE---DISQHMDQV--RNSLGLCPQQNLLFDHLTVSE 617
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRtlfDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HL-YFYCRIKGVPQKMYLEETNNMLSAFNLMEKcdaFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTW 696
Cdd:TIGR02142 95 NLrYGMKRARPSERRISFERVIELLGIGHLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 697 DILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:TIGR02142 172 PYLERLHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1369-1576 |
3.32e-18 |
|
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: 85.80 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIvkVRSKIGYCPQFDALLEYM 1444
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI--ARLGIGYVPEGRRIFPSL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWE--IMIMYARIWGISEHQIQPYV-------KKYLNSLdleshANSListySEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:COG0410 94 TVEEnlLLGAYARRDRAEVRADLERVyelfprlKERRRQR-----AGTL----SGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN 1576
Cdd:COG0410 165 LGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
530-733 |
3.45e-18 |
|
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: 83.80 E-value: 3.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 530 VFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNL 608
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LFDHlTVSEHLyfycrikgvpqkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:cd03246 87 LFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 689 PASRRSTWD-ILQTYKQNRTILLTTHYMdEADVLGDRIAIMVRGTL 733
Cdd:cd03246 129 VEGERALNQaIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1353-1572 |
4.31e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 88.35 E-value: 4.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTkNIVKVRSKI 1431
Cdd:PRK11607 18 PLLeIRNLTKSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFL 1511
Cdd:PRK11607 94 NMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKIRES-GKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK11607 174 DEPMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
522-713 |
5.18e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 5.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEaYVHGEDIsqhmdqvrnSLG 601
Cdd:COG0488 316 LELEGLSKSYGD----KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFD-HLTVSEHlyfycrIKGVPQKMYLEETNNMLSAFNLM-EKCDAFSKSLSGGMKRKLAIIIALIGGSKVAI 679
Cdd:COG0488 382 YFDQHQEELDpDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190
....*....|....*....|....*....|....
gi 46358378 680 LDEPTSGMDPASRRSTWDILQTYKQnrTILLTTH 713
Cdd:COG0488 456 LDEPTNHLDIETLEALEEALDDFPG--TVLLVSH 487
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1369-1576 |
5.98e-18 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.43 E-value: 5.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT---------KNIVK----VRskigycp 1435
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghqiarMGVVRtfqhVR------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 qfdaLLEYMTGWEIMIM-------------------YARiwgiSEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRL 1496
Cdd:PRK11300 91 ----LFREMTVIENLLVaqhqqlktglfsgllktpaFRR----AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1497 STAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLK 1575
Cdd:PRK11300 163 EIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIR 242
|
.
gi 46358378 1576 N 1576
Cdd:PRK11300 243 N 243
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1356-1565 |
6.08e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 87.16 E-value: 6.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY-FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRSK 1430
Cdd:PRK11153 4 LKNISKVFpQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1431 IGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
534-727 |
6.14e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.20 E-value: 6.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 534 NNTTKV-----AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEdiSQHMDQVRNSLG----LCP 604
Cdd:PRK11288 8 DGIGKTfpgvkALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--EMRFASTTAALAagvaIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 605 QQNLLFDHLTVSEHLY---FYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:PRK11288 86 QELHLVPEMTVAENLYlgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 682 EPTSGMdpaSRRSTwDIL-----QTYKQNRTILLTTHYMDEADVLGDRIAI 727
Cdd:PRK11288 166 EPTSSL---SAREI-EQLfrvirELRAEGRVILYVSHRMEEIFALCDAITV 212
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
522-722 |
6.86e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.87 E-value: 6.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD----QVR 597
Cdd:PRK11629 6 LQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 N-SLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:PRK11629 86 NqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQ--TYKQNRTILLTTHYMDEADVLG 722
Cdd:PRK11629 166 LVLADEPTGNLDARNADSIFQLLGelNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
543-713 |
8.67e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQvrnslglcPQQNLLF--------DHLT 614
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE--------YHQDLLYlghqpgikTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLYFYCRIKGVPQKmylEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS-RR 693
Cdd:PRK13538 91 ALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGvAR 167
|
170 180
....*....|....*....|
gi 46358378 694 STWDILQTYKQNRTILLTTH 713
Cdd:PRK13538 168 LEALLAQHAEQGGMVILTTH 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
507-713 |
1.11e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 88.95 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 507 ESKYFEAEPTDLTAGIQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP---TSGEAY 583
Cdd:TIGR00955 7 NSDVFGRVAQDGSWKQLVSRLRGCFCRERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 584 VHGEDISQHMDQVRNslGLCPQQNLLFDHLTVSEHLYFYCRIK---GVPQKMYLEETNNMLSAFNLMeKC-------DAF 653
Cdd:TIGR00955 87 LNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLR-KCantrigvPGR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 654 SKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQN-RTILLTTH 713
Cdd:TIGR00955 164 VKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKgKTIICTIH 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
541-713 |
1.16e-17 |
|
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: 84.13 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDhLTVSEHL 619
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFD-GTIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 YfYCRiKGVPQKMyLEETNNMLSAFNLMEK--------CDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS 691
Cdd:cd03249 98 R-YGK-PDATDEE-VEEAAKKANIHDFIMSlpdgydtlVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAES 174
|
170 180
....*....|....*....|..
gi 46358378 692 RRSTWDILQTYKQNRTILLTTH 713
Cdd:cd03249 175 EKLVQEALDRAMKGRTTIVIAH 196
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
515-753 |
1.48e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 89.01 E-value: 1.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 515 PTDLTAGIQIKHLHkvFQKNNTTKVAI-KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHM 593
Cdd:TIGR00958 472 PLNLEGLIEFQDVS--FSYPNRPDVPVlKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 594 DQ-VRNSLGLCPQQNLLFDHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEK-----CDAFSKSLSGGMKRKLAI 667
Cdd:TIGR00958 550 HHyLHRQVALVGQEPVLFSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNgydteVGEKGSQLSGGQKQRIAI 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 668 IIALIGGSKVAILDEPTSGMDPASRRStwdiLQTYK--QNRTILLTTHYMDEADVlGDRIAIMVRGTLRCCGSSVFLKRL 745
Cdd:TIGR00958 629 ARALVRKPRVLILDEATSALDAECEQL----LQESRsrASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED 703
|
....*...
gi 46358378 746 YGVGSHLV 753
Cdd:TIGR00958 704 QGCYKHLV 711
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
530-733 |
1.57e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.76 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 530 VFQKNNTTKV-AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-QHMDQVRNSLGLCPQQ- 606
Cdd:PRK13642 11 VFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 607 NLLFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAI--IIALigGSKVAILDEPT 684
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVagIIAL--RPEIIILDEST 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 685 SGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEAdVLGDRIAIMVRGTL 733
Cdd:PRK13642 169 SMLDPTGRQEIMRVIHEIKEkyQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
515-738 |
1.60e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 85.67 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 515 PTDLTAGI--QIKHLHKVF-QKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ 591
Cdd:PRK13631 13 PNPLSDDIilRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 HMDQVRNSLGLCPQQNLLFDHL--TVS------EHLYFYCRIK----------GVPQKMYLEETNNMLSAFNLmeKCDAF 653
Cdd:PRK13631 93 KKNNHELITNPYSKKIKNFKELrrRVSmvfqfpEYQLFKDTIEkdimfgpvalGVKKSEAKKLAKFYLNKMGL--DDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 654 SKS---LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWD-ILQTYKQNRTILLTTHYMDEADVLGDRIAIMV 729
Cdd:PRK13631 171 ERSpfgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQlILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
....*....
gi 46358378 730 RGTLRCCGS 738
Cdd:PRK13631 251 KGKILKTGT 259
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1371-1564 |
1.85e-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: 81.66 E-value: 1.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALLEYMTgwei 1449
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAYVPQ-DPFLFSGT---- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 mimyariwgISEhqiqpyvkkylNSLdleshanslistySEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDT 1529
Cdd:cd03228 92 ---------IRE-----------NIL-------------SGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEA 138
|
170 180 190
....*....|....*....|....*....|....*
gi 46358378 1530 VIKIREsGKAIIITSHSMEECEaLCTRLSIMVRGR 1564
Cdd:cd03228 139 LRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
522-738 |
2.11e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 2.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSL 600
Cdd:PRK11160 339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHlTVSEHLYFYC------RIKGVPQKMYLE---ETNNMLSAFnLMEKcdafSKSLSGGMKRKLAIIIAL 671
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNLLLAApnasdeALIEVLQQVGLEkllEDDKGLNAW-LGEG----GRQLSGGEQRRLGIARAL 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 672 IGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLgDRIAIMVRGTLRCCGS 738
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGT 556
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1371-1577 |
2.71e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.06 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-----KNIVKVRSKIGYCPQF--DALLEY 1443
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIGMVFQFpeSQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWEImIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLiSTY--SEGNKRRLS-TAIATMgKPSVIFLDEPSTGMDP 1520
Cdd:PRK13646 102 TVEREI-IFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQ-SPFqmSGGQMRKIAiVSILAM-NPDIIVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1521 RARRLLWDTVIKIR-ESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:PRK13646 179 QSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1374-1572 |
2.77e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 84.11 E-value: 2.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1374 NISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-----KNIVKVRSKIGYCPQF-DALLEYMTGW 1447
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKKLRKKVSLVFQFpEAQLFENTVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1448 EIMIMYARIWGISEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLL 1526
Cdd:PRK13641 105 KDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 1527 WDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13641 185 MQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
512-713 |
3.00e-17 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 87.53 E-value: 3.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 512 EAEPTDLTAGIQIKHLHkvFQKNNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ 591
Cdd:COG1132 330 AVPLPPVRGEIEFENVS--FSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 H-MDQVRNSLGLCPQQNLLFdHLTVSEHLYFycrikGVPQkMYLEETNNMLSAFNLMEKCDAFSK-----------SLSG 659
Cdd:COG1132 407 LtLESLRRQIGVVPQDTFLF-SGTIRENIRY-----GRPD-ATDEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSG 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 660 GMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAH 533
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1358-1584 |
3.05e-17 |
|
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: 87.97 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKIYFK----SPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIG 1432
Cdd:COG2274 475 ELENVSFRypgdSPPVL--DNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQ----FDA-LLEYMTGWEIMIMYARIWGISEH-QIQPYVKKYLNSLD--LESHANSListySEGNKRRLSTAIATMG 1504
Cdd:COG2274 553 VVLQdvflFSGtIRENITLGDPDATDEEIIEAARLaGLHDFIEALPMGYDtvVGEGGSNL----SGGQRQRLAIARALLR 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1505 KPSVIFLDEPSTGMDPRARRLLWDTVIKIREsGKAIIITSHSMeECEALCTRLSIMVRGRLTCLGSPQYLKNKFGNIYIL 1584
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1387-1545 |
3.13e-17 |
|
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: 81.52 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGENIP--TAGDVFIDGISLTKNIVKVrskIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQi 1464
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALLRGLSVEQ- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1465 qpyvkkylnsldleshanslistysegnKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITS 1544
Cdd:cd03232 114 ----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTI 165
|
.
gi 46358378 1545 H 1545
Cdd:cd03232 166 H 166
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
542-728 |
3.49e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 85.47 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 542 KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGedisQHMDQV---RNSLGLCPQQNLLFDHLTVSEH 618
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE----KRMNDVppaERGVGMVFQSYALYPHLSVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR---RSt 695
Cdd:PRK11000 96 MSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRvqmRI- 174
|
170 180 190
....*....|....*....|....*....|....
gi 46358378 696 wDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIM 728
Cdd:PRK11000 175 -EISRLHKRlGRTMIYVTHDQVEAMTLADKIVVL 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
522-738 |
3.50e-17 |
|
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: 82.16 E-value: 3.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLhkVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSL 600
Cdd:cd03244 3 IEFKNV--SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHlTVSEHLYFYCR-----IKGVPQKMYL-EETNNMLSAFNLMEKCDafSKSLSGGMKRKLAIIIALIGG 674
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDPFGEysdeeLWQALERVGLkEFVESLPGGLDTVVEEG--GENLSVGQRQLLCLARALLRK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 675 SKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDE-ADVlgDRIAIMVRGTLRCCGS 738
Cdd:cd03244 158 SKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDS 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1386-1565 |
3.93e-17 |
|
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: 81.96 E-value: 3.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1386 GLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKV-----RSKIGYCPQFDALLEYMTGWEIMIMYARIWGIS 1460
Cdd:cd03297 27 GIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKInlppqQRKIGLVFQQYALFPHLNVRENLAFGLKRKRNR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1461 EHQIQpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRES-GKA 1539
Cdd:cd03297 107 EDRIS--VDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNlNIP 184
|
170 180
....*....|....*....|....*.
gi 46358378 1540 IIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03297 185 VIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
526-717 |
4.89e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 82.07 E-value: 4.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 526 HLHKVFQKNNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHM-DQVRNSLGLCP 604
Cdd:PRK10247 9 QLQNVGYLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIYRQQVSYCA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 605 QQNLLFDHlTVSEHLYFYCRIKGV---PQKMYLEetnnmLSAFNLMEkcDAFSKS---LSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK10247 88 QTPTLFGD-TVYDNLIFPWQIRNQqpdPAIFLDD-----LERFALPD--TILTKNiaeLSGGEKQRISLIRNLQFMPKVL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDE 717
Cdd:PRK10247 160 LLDEITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1372-1574 |
5.95e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.24 E-value: 5.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIGYC---P--QF-DALLE-- 1442
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeENVWDIRHKIGMVfqnPdnQFvGATVEdd 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 YMTGWEIMimyariwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:PRK13650 103 VAFGLENK-------GIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1523 RRLLWDTVIKIRES-GKAIIITSHSMEECeALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK13650 176 RLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
540-738 |
7.62e-17 |
|
nickel import ATP-binding protein NikD; This family represents the NikD 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. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 81.65 E-value: 7.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP----TSGEAYVHGEDISQhmDQVRNSLGLCPQQNLL--FDHL 613
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLP--LSIRGRHIATIMQNPRtaFNPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 -TVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSK---SLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:TIGR02770 79 fTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKypfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 690 ASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:TIGR02770 159 VNQARVLKLLRELRQLFgtGILLITHDLGVVARIADEVAVMDDGRIVERGT 209
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1370-1586 |
8.26e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.83 E-value: 8.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGI--SLTKNIVKVRSKIGYCPQ------FDALL 1441
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLdtSDEENLWDIRNKAGMVFQnpdnqiVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1442 EymtgwEIMIMYARIWGISEHQIQPYVKKYLNSLDL---ESHANSLISTyseGNKRRLSTA-IATMgKPSVIFLDEPSTG 1517
Cdd:PRK13633 104 E-----EDVAFGPENLGIPPEEIRERVDESLKKVGMyeyRRHAPHLLSG---GQKQRVAIAgILAM-RPECIIFDEPTAM 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1518 MDPRARRLLWDTVIKI-RESGKAIIITSHSMEECeALCTRLSIMVRGRLTCLGSPqylKNKFGNIYILKA 1586
Cdd:PRK13633 175 LDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP---KEIFKEVEMMKK 240
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
528-738 |
8.50e-17 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 81.76 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 528 HKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQ 606
Cdd:cd03252 5 HVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 607 NLLFDHlTVSEHLYFycrIKGVPQKMYLEETNNMLSAFN-LMEKCDAFSK-------SLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03252 85 NVLFNR-SIRDNIAL---ADPGMSMERVIEAAKLAGAHDfISELPEGYDTivgeqgaGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMdEADVLGDRIAIMVRGTLRCCGS 738
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1353-1565 |
8.81e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.46 E-value: 8.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIYfksPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSK 1430
Cdd:COG1129 3 PLLeMRGISKSF---GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRfRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1431 -IGYCPQFDALLEYMTGWE-IMI--MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKP 1506
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAEnIFLgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1507 SVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
540-769 |
1.00e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 83.63 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAgksttlSILSGLYPptsgeAYVHGEDISQ----------HMDQVRNSLGLC-PQQNL 608
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GPDAGRrpwrf*twcaNRRALRRTIG*HrPVR*G 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:NF000106 97 RRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 689 PASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSSVFLKRlyGVGSHLVMVKEPYCdiAEISK 767
Cdd:NF000106 177 PRTRNEVWDEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT--KVGGRTLQIRPAHA--AELDR 252
|
..
gi 46358378 768 LI 769
Cdd:NF000106 253 MV 254
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
540-724 |
1.06e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 81.46 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ--VRNSLGLCPQQNLLFDHLTVSE 617
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HL----YFYCRikgvpqKMYLEETNNMLSAF-NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:PRK11614 100 NLamggFFAER------DQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190
....*....|....*....|....*....|...
gi 46358378 693 RSTWDILQTYKQN-RTILLTTHYMDEADVLGDR 724
Cdd:PRK11614 174 QQIFDTIEQLREQgMTIFLVEQNANQALKLADR 206
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1357-1572 |
1.18e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1357 KELTKIYFKSplILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCP 1435
Cdd:PRK13652 7 RDLCYSYSGS--KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIMYARI-WGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:PRK13652 85 QNPDDQIFSPTVEQDIAFGPInLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1515 STGMDPRARRLLWDTVIKIRES-GKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13652 165 TAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1372-1571 |
1.30e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.98 E-value: 1.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL---TKNIVKVRSKIGYCPQFDALLEYMTGWE 1448
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVFQDPEQQIFYTDID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIMYA-RIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLW 1527
Cdd:PRK13638 97 SDIAFSlRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 1528 DTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSP 1571
Cdd:PRK13638 177 AIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1356-1514 |
2.05e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.35 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDgisltKNIvkvrsKIGYCP 1435
Cdd:COG0488 1 LENLSKSFGGRPLL---DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGL-----RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIMIM----------------------------YARIWG----ISEHQIQPYVKKYLNSLDL-ESHAN 1482
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDgdaelraleaeleeleaklaepdedlerLAELQEefeaLGGWEAEARAEEILSGLGFpEEDLD 147
|
170 180 190
....*....|....*....|....*....|..
gi 46358378 1483 SLISTYSEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
522-732 |
2.30e-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: 80.17 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVF---QKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE----DISQHMD 594
Cdd:COG4778 5 LEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 QV-----RNSLGLCPQqnllfdHL----------TVSEHLyfycRIKGVPQKMYLEETNNMLSAFNLMEKC-DAFSKSLS 658
Cdd:COG4778 85 REilalrRRTIGYVSQ------FLrviprvsaldVVAEPL----LERGVDREEARARARELLARLNLPERLwDLPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 659 GGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLT-THYMDEADVLGDRIAIMVRGT 732
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRVVDVTPFS 229
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
535-713 |
2.60e-16 |
|
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: 79.96 E-value: 2.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 535 NTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHl 613
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVSEHL-YFYCRIKGvpqkmylEETNNMLSAFNLmekcDAF---------------SKSLSGGMKRKLAIIIALIGGSKV 677
Cdd:cd03254 92 TIMENIrLGRPNATD-------EEVIEAAKEAGA----HDFimklpngydtvlgenGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 46358378 678 AILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1351-1566 |
3.20e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.86 E-value: 3.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1351 NCPVLI-KELTKIYFKSPLILAV-KNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NI 1424
Cdd:PRK11629 2 NKILLQcDNLCKRYQEGSVQTDVlHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1425 VKVRS-KIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATM 1503
Cdd:PRK11629 82 AELRNqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1504 GKPSVIFLDEPSTGMDPRARrllwDTVIKI-----RESGKAIIITSHSMEeceaLCTRLSI---MVRGRLT 1566
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNA----DSIFQLlgelnRLQGTAFLVVTHDLQ----LAKRMSRqleMRDGRLT 224
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1371-1572 |
3.99e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.66 E-value: 3.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL---TKNIVKVRSKIGYCPQ------FDALL 1441
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQdpdnqlFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1442 EYMTGWEIMIMyariwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPR 1521
Cdd:PRK13636 101 YQDVSFGAVNL-----KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1522 ARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13636 176 GVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1372-1565 |
5.44e-16 |
|
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: 77.26 E-value: 5.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQFDALLEymtgweim 1450
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFS-------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 imyariwG-ISEhqiqpyvkkylNSLdleshanslistySEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDT 1529
Cdd:cd03246 90 -------GsIAE-----------NIL-------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138
|
170 180 190
....*....|....*....|....*....|....*.
gi 46358378 1530 VIKIRESGKAIIITSHSMEECEAlCTRLSIMVRGRL 1565
Cdd:cd03246 139 IAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1371-1586 |
6.04e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 80.16 E-value: 6.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPT-----AGDVFIDGISLTKNIVKVRSKIGYCPQF-DALLEYM 1444
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTegkvtVGDIVVSSTSKQKEIKPVRKKVGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHA-NSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRAR 1523
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1524 RLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQylkNKFGNIYILKA 1586
Cdd:PRK13643 181 IEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPS---DVFQEVDFLKA 240
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1006-1228 |
6.19e-16 |
|
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: 81.28 E-value: 6.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1006 NRVNLTVLFNNEAYHSPSLSLTVLDNIL-----FMSLSGSDASITVFNKPQPSPQRKEWPGSTDGKIVAFKIQLGMALLV 1080
Cdd:pfam12698 97 ESATVTVYINSSNLLVSKLILNALQSLLqqlnaSALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1081 SGFCILTVTERHNKTKHMQFLSGVSILVYWLSALVFDLIIFFISCCFLLVMFkyckFDIYVTDYHILDTMLILTLFGWSA 1160
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL----FGIGIPFGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1161 IPLTYLLSFLFSKSNSAYINLLVFCYLSGTLSLLMdtiiearistIMSNSTQTFLLNALLLFPMYNLG 1228
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGL----------FPLEDPPSFLQWIFSIIPFFSPI 310
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1358-1577 |
8.95e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.52 E-value: 8.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK--IGYCP 1435
Cdd:PRK09700 7 SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQlgIGIIY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEIM----IMYARIWGI-----SEHQIQPYVkkYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKP 1506
Cdd:PRK09700 87 QELSVIDELTVLENLyigrHLTKKVCGVniidwREMRVRAAM--MLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1507 SVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1356-1564 |
9.75e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 9.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFK-SPL-ILAVKNISLAIQEracfG----LLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRS 1429
Cdd:COG1101 4 LKNLSKTFNPgTVNeKRALDGLNLTIEE----GdfvtVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 K----------IGYCPQfdalleyMTGWEIMIM-YAR------IWGISEHQIQPYvKKYLNSLD--LESHANSLISTYSE 1490
Cdd:COG1101 80 KyigrvfqdpmMGTAPS-------MTIEENLALaYRRgkrrglRRGLTKKRRELF-RELLATLGlgLENRLDTKVGLLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1491 GNKRRLSTAIATMGKPSVIFLDEPSTGMDPR-ARRLLWDTVIKIRESG-KAIIITsHSMEECEALCTRLSIMVRGR 1564
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKtAALVLELTEKIVEENNlTTLMVT-HNMEQALDYGNRLIMMHEGR 226
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
531-713 |
1.06e-15 |
|
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: 78.43 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 531 FQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSLGLCPQQNLL 609
Cdd:cd03251 8 FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYtLASLRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 610 FDHlTVSEHLYFycrikGVPQKMyLEETNNMLSAFNLMEKCDAFSK-----------SLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03251 88 FND-TVAENIAY-----GRPGAT-REEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190
....*....|....*....|....*....|....*
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
535-713 |
1.11e-15 |
|
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: 78.43 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 535 NTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHl 613
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVsEHLYFYCRIKGVPQKMYL--------EETNNMLSAFN-------LMekcdafsksLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03253 90 TI-GYNIRYGRPDATDEEVIEaakaaqihDKIMRFPDGYDtivgergLK---------LSGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAH 194
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
536-738 |
1.42e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 79.08 E-value: 1.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 536 TTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQ--NLLFDH 612
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVFQNpdDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 613 lTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 693 RSTWDILQTYKQN--RTILLTTHYMDEADVLGDRIAIMVRGtlRCCGS 738
Cdd:PRK13652 174 KELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKG--RIVAY 219
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
541-733 |
1.55e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 78.42 E-value: 1.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILS---GLYPP--TSGEAYVHGEDISQhMD--QVRNSLGLC-----PQQNL 608
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNrliELYPEarVSGEVYLDGQDIFK-MDviELRRRVQMVfqipnPIPNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 -LFDHLTVSEHL--------YFYCRIKGVPQKMYL-EETNNMLsafnlmekcDAFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK14247 98 sIFENVALGLKLnrlvkskkELQERVRWALEKAQLwDEVKDRL---------DAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
545-731 |
1.76e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 545 SLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDiSQHMDQVRNSLGLCPQQNLLFDHLTVSEHL----- 619
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQNIglgln 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 -------YFYCRIKGVPQKMYLEetnnmlsafNLMEKcdaFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:PRK10771 98 pglklnaAQREKLHAIARQMGIE---------DLLAR---LPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46358378 693 RSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1356-1548 |
1.91e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 78.97 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY-FKSPLIL-AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDV---FIDG------------- 1417
Cdd:PRK13651 5 VKNIVKIFnKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEknkkktkekekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1418 ----ISLT-----KNIVKVRSKIGYCPQFdalLEYM----TGWEIMIMYARIWGISEHQIQPYVKKYLNSLDL-ESHANS 1483
Cdd:PRK13651 85 eklvIQKTrfkkiKKIKEIRRRVGVVFQF---AEYQlfeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1484 LISTYSEGNKRRLSTA-IATMgKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSME 1548
Cdd:PRK13651 162 SPFELSGGQKRRVALAgILAM-EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
538-739 |
2.25e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.78 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP------PTSGEAYVHGEDISQhMD--QVRNSLGLCPQQNLL 609
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ-IDaiKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 610 FDHLTVSEHLYFYCRIKGVPQKM----YLEETNNMLSAFN-LMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPT 684
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKReikkIVEECLRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 685 SGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSS 739
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1356-1572 |
2.25e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 78.52 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLI--LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIG 1432
Cdd:PRK13635 5 IIRVEHISFRYPDAatYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSeETVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YC---P--QF------DAL---LEYMtgweimimyariwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLst 1498
Cdd:PRK13635 85 MVfqnPdnQFvgatvqDDVafgLENI-------------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV-- 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1499 AIATM--GKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13635 150 AIAGVlaLQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPE 225
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
527-731 |
2.54e-15 |
|
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: 76.53 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 527 LHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPT---SGEAYVHGEDISQHMDQVRNSLGLC 603
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 PQQNLLFDHLTVSEHLYFYCRIKGvpqkmyleetnnmlsafnlmekcDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEP 683
Cdd:cd03233 89 SEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 684 TSGMDPAsrrSTWDILQTYKQNRTILLTTHYM------DEADVLGDRIAIMVRG 731
Cdd:cd03233 146 TRGLDSS---TALEILKCIRTMADVLKTTTFVslyqasDEIYDLFDKVLVLYEG 196
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1354-1596 |
2.57e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 79.61 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTkNIVKVRSKIGY 1433
Cdd:PRK09452 15 VELRGISKSFDGKEVI---SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1514 PSTGMDPRARRLLwDTVIKI--RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL----KNKF-----GNIY 1582
Cdd:PRK09452 171 SLSALDYKLRKQM-QNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLFvarfiGEIN 249
|
250
....*....|....
gi 46358378 1583 ILKAKVKsgETLDE 1596
Cdd:PRK09452 250 IFDATVI--ERLDE 261
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
540-715 |
2.64e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.84 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ----VRNSLGLCPQQNLLFDHLTV 615
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpfLRRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRst 695
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSE-- 174
|
170 180
....*....|....*....|....
gi 46358378 696 wDILQTYKQ-NR---TILLTTHYM 715
Cdd:PRK10908 175 -GILRLFEEfNRvgvTVLMATHDI 197
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1371-1565 |
2.83e-15 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 75.55 E-value: 2.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK--VRSKIGYCP---QFDALLEYMT 1445
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPedrKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1446 GWEimimyariwgisehqiqpyvkkylnsldleshaNSLISTY-SEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARR 1524
Cdd:cd03215 95 VAE---------------------------------NIALSSLlSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 46358378 1525 LLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:cd03215 142 EIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
522-719 |
3.47e-15 |
|
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: 76.70 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQhMDQ-----V 596
Cdd:COG4181 9 IELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFA-LDEdararL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RN-SLGLCPQQNLLFDHLTVSEHLyfycrikGVPqkmyLEETNN---------MLSAFNLMEKCDAFSKSLSGGMKRKLA 666
Cdd:COG4181 88 RArHVGFVFQSFQLLPTLTALENV-------MLP----LELAGRrdarararaLLERVGLGHRLDHYPAQLSGGEQQRVA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 667 IIIALIGGSKVAILDEPTSGMDPASRRSTWDILqtYKQNR----TILLTTHymDEAD 719
Cdd:COG4181 157 LARAFATEPAILFADEPTGNLDAATGEQIIDLL--FELNRergtTLVLVTH--DPAL 209
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1367-1565 |
3.47e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1367 PLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGI---------SLTKNIVKVRSKIGYCPQf 1437
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVAIIYQELHLVPE- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1438 dalleyMTGWE-IMI--MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:PRK11288 94 ------MTVAEnLYLgqLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1515 STGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
541-738 |
4.76e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 77.35 E-value: 4.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE--DISQH----MDQVRNSLGLCPQQNLLFDhlT 614
Cdd:PRK13638 17 LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRgllaLRQQVATVFQDPEQQIFYT--D 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRS 694
Cdd:PRK13638 95 IDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 46358378 695 TWDILQ-TYKQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:PRK13638 175 MIAIIRrIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1353-1566 |
5.05e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.07 E-value: 5.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIYfksPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltkNIVKVRS-- 1429
Cdd:COG3845 4 PALeLRGITKRF---GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG-----KPVRIRSpr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 -----KIGYCPQ-FdALLEYMTGWE-IMIMYARIWGIS------EHQIQPYVKKYlnSLDLESHAnsLISTYSEGNKRRL 1496
Cdd:COG3845 76 daialGIGMVHQhF-MLVPNLTVAEnIVLGLEPTKGGRldrkaaRARIRELSERY--GLDVDPDA--KVEDLSVGEQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1497 STAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
522-718 |
6.32e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 76.66 E-value: 6.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHG---EDISQHMDQVRN 598
Cdd:PRK11248 2 LQISHLYADYGG----KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGkpvEGPGAERGVVFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQNLLfdhltvsEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK11248 78 NEGLLPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQT--YKQNRTILLTTHYMDEA 718
Cdd:PRK11248 151 LLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEA 192
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
522-739 |
7.88e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.59 E-value: 7.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNttkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP----PTS-----GEAYVHGEDISQH 592
Cdd:PRK09984 5 IRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 593 MDQVRNSLGLCPQQNLLFDHLTVSEH----------LYFYCRIKGVPQKMylEETNNMLSAFNLMEKCDAFSKSLSGGMK 662
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENvligalgstpFWRTCFSWFTREQK--QRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 663 RKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCGSS 739
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1357-1574 |
9.02e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.90 E-value: 9.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1357 KELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQ-ILTGENIpTAGDVFIDGISLTKNIVKV---RSKIG 1432
Cdd:PRK09493 5 KNVSKHFGPTQVL---HNIDLNIDQGEVVVIIGPSGSGKSTLLRcINKLEEI-TSGDLIVDGLKVNDPKVDErliRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWE-IMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFL 1511
Cdd:PRK09493 81 MVFQQFYLFPHLTALEnVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
536-733 |
1.05e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 78.91 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 536 TTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH--MDQVRNSLGLCP---QQNLLF 610
Cdd:COG1129 263 SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRspRDAIRAGIAYVPedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 DHLTVSEHLYF-----YCRIKGVPQKMYLEETNNMLSAFNLmeKC---DAFSKSLSGGMKRKlaIIIA--LIGGSKVAIL 680
Cdd:COG1129 343 LDLSIRENITLasldrLSRGGLLDRRRERALAEEYIKRLRI--KTpspEQPVGNLSGGNQQK--VVLAkwLATDPKVLIL 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 681 DEPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEadVLG--DRIAIMVRGTL 733
Cdd:COG1129 419 DEPTRGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
539-726 |
1.19e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.97 E-value: 1.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSI---LSGLYPP--TSGEAYVHGEDI-SQHMD--QVRNSLGLCPQQNLLF 610
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyAPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 DHlTVSEHLYFYCRIKGVPQKM-YLEETNNMLSAF--NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGDMdELVERSLRQAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSAL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 688 DPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIA 726
Cdd:PRK14243 183 DPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
540-732 |
1.32e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 78.91 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSLGLCPQQNLLFDHlTVSEH 618
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYtLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYFYCriKGVPQKMYLEETNNMLSAFNLMEKCD--------AFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA 690
Cdd:PRK11176 437 IAYAR--TEQYSREQIEEAARMAYAMDFINKMDngldtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTE 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 691 SRRSTWDILQTYKQNRTILLTTHYM---DEAD--VLGDRIAIMVRGT 732
Cdd:PRK11176 515 SERAIQAALDELQKNRTSLVIAHRLstiEKADeiLVVEDGEIVERGT 561
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
144-464 |
1.39e-14 |
|
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: 77.04 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 144 SSDPLPKKVKYYLRFSDIKKNINSGAYYQGDTWLTKFLFHSLRLVGPRNPYEADGgSPGYITEGFLAVQHALDKAIMLHH 223
Cdd:pfam12698 53 EASPTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGESATVTVYINS-SNLLVSKLILNALQSLLQQLNASA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 224 GGADAAALFNDISLFIQRFPYPAYYHDYFYLFattfIPLTVACTFFFNHYVLVWSIVWEKENRLKEYQLMIGLRNWMFWV 303
Cdd:pfam12698 132 LVLLLEALSTSAPIPVESTPLFNPQSGYAYYL----VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 304 AYFFTFLCLYFINIIVMCMVLFvkiepAPIFQYNDPTLVFIFLLFYAISSIFFSFMVSTLFNKVSLAMSLGSFLFFLTYF 383
Cdd:pfam12698 208 GKILGDFLVGLLQLLIILLLLF-----GIGIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 384 PAVAMhQSFERMPSKQKLIWSFDFNVGMAFGFRFLVNtdakktGMKWSNIFLStdsdsflfayvLGMLLADAFIYGLVAW 463
Cdd:pfam12698 283 FFGGL-FPLEDPPSFLQWIFSIIPFFSPIDGLLRLIY------GDSLWEIAPS-----------LIILLLFAVVLLLLAL 344
|
.
gi 46358378 464 Y 464
Cdd:pfam12698 345 L 345
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
524-734 |
1.50e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 524 IKHLHKVFQknntTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGedisqhmdQVRnsLGLC 603
Cdd:COG0488 1 LENLSKSFG----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK--------GLR--IGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 PQQNLLFDHLTVSEHLY--------FYCRIKGVPQKM--YLEETNNMLSAFNLMEKCDAFS------------------- 654
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgdaelraLEAELEELEAKLaePDEDLERLAELQEEFEALGGWEaearaeeilsglgfpeedl 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 655 ----KSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRstW--DILQTYKqnRTILLTTHymDEA--DVLGDRIA 726
Cdd:COG0488 147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP--GTVLVVSH--DRYflDRVATRIL 220
|
....*...
gi 46358378 727 IMVRGTLR 734
Cdd:COG0488 221 ELDRGKLT 228
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
522-713 |
1.64e-14 |
|
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: 72.10 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEaYVHGEDIsqhmdqvrnslg 601
Cdd:cd03221 1 IELENLSKTYGG----KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTV------------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 lcpqqnllfdhltvsEHLYFycrikgvPQkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILD 681
Cdd:cd03221 64 ---------------KIGYF-------EQ--------------------------LSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|..
gi 46358378 682 EPTSGMDPASRRSTWDILQTYKqnRTILLTTH 713
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYP--GTVILVSH 125
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1354-1578 |
1.77e-14 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 77.04 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRsKIGY 1433
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR-NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1434 CPQFDALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRR--LSTAIATmgKPSVIFL 1511
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRvaLGRALVR--EPKVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1512 DEPSTGMDPRARrllWDTVIKI----RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL----KNKF 1578
Cdd:COG3839 158 DEPLSNLDAKLR---VEMRAEIkrlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELydrpANLF 229
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
512-733 |
2.29e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 75.07 E-value: 2.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 512 EAEPTDLTAGIQIKHLHkVFQKNnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSG---LYPP--TSGEAYVHG 586
Cdd:COG1117 2 TAPASTLEPKIEVRNLN-VYYGD---KQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmndLIPGarVEGEILLDG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 587 EDI-SQHMD--QVRNSLGLCPQQ-NLL----FDHLTvsehlyFYCRIKGVPQKMYLEEtnnmlsafnLMEKC-------- 650
Cdd:COG1117 78 EDIyDPDVDvvELRRRVGMVFQKpNPFpksiYDNVA------YGLRLHGIKSKSELDE---------IVEESlrkaalwd 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 651 ---DAFSKS---LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDR 724
Cdd:COG1117 143 evkDRLKKSalgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDY 222
|
....*....
gi 46358378 725 IAIMVRGTL 733
Cdd:COG1117 223 TAFFYLGEL 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1369-1571 |
5.03e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 75.27 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL-----------------TKNIVKVRSKI 1431
Cdd:PRK13631 39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnhelitnpyskkIKNFKELRRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQFDALLEYMTGWEIMIMYARI-WGISEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:PRK13631 119 SMVFQFPEYQLFKDTIEKDIMFGPVaLGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEIL 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSP 1571
Cdd:PRK13631 199 IFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTP 260
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
541-713 |
5.11e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 5.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQQNLLFDHLTVSEHLY 620
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 621 FycRIKGVPQKMYLEEtnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQ 700
Cdd:PRK13540 97 Y--DIHFSPGAVGITE---LCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQ 171
|
170
....*....|....
gi 46358378 701 TY-KQNRTILLTTH 713
Cdd:PRK13540 172 EHrAKGGAVLLTSH 185
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1371-1582 |
5.17e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.89 E-value: 5.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQ----ILTGENIPTA-----GDVFIDGISLTKNIVKVRSKIGYCPQFDALL 1441
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1442 EYMTGWEIMIMYA----RIWGISEHQIQPYVKKY----LNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:PRK09984 99 NRLSVLENVLIGAlgstPFWRTCFSWFTREQKQRalqaLTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1514 PSTGMDPRARRLLWDTVIKIRES-GKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN-KFGNIY 1582
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNeRFDHLY 249
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
540-738 |
5.82e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 5.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQV------RNSLGLC---PQQNLLF 610
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 DhlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSK-SLSGGMKRKLAI--IIALIGgsKVAILDEPTSGM 687
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALagIIAMDG--NTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 688 DPASRRSTWDILQTYKQN--RTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEykKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
522-733 |
7.03e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 73.34 E-value: 7.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTtkvaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLY-----PPTSGEAYVHGEDI-SQHMD- 594
Cdd:PRK14267 5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIySPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 -QVRNSLGLCPQQNLLFDHLTVSEHLYFYCRIKGV--PQKMYLEETNNMLSAFNLME----KCDAFSKSLSGGMKRKLAI 667
Cdd:PRK14267 81 iEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 668 IIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1371-1574 |
7.47e-14 |
|
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: 76.34 E-value: 7.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQ----FDA-LLEym 1444
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAVVPQrphlFDTtLRE-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 tgweiMIMYARIwGISEHQIQ---------PYVKKYLNSLD--LESHANSListySEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:COG4987 428 -----NLRLARP-DATDEELWaalervglgDWLAALPDGLDtwLGEGGRRL----SGGERRRLALARALLRDAPILLLDE 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1514 PSTGMDPRARRLLWDTVIKIREsGKAIIITSHSMEECEAlCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:COG4987 498 PTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEEL 556
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1356-1572 |
8.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 73.90 E-value: 8.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY-FKSPLI-LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-----KNIVKVR 1428
Cdd:PRK13634 5 FQKVEHRYqYKTPFErRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKPLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1429 SKIGYCPQF--DALLEYMTgwEIMIMYARI-WGISEHQIQPYVKK--YLNSLDLESHANSLIStYSEGNKRRLstAIA-- 1501
Cdd:PRK13634 85 KKVGIVFQFpeHQLFEETV--EKDICFGPMnFGVSEEDAKQKAREmiELVGLPEELLARSPFE-LSGGQMRRV--AIAgv 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1502 -TMgKPSVIFLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13634 160 lAM-EPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPR 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1372-1571 |
8.11e-14 |
|
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: 71.79 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTG--ENIPTAGDVFIDGISLTKNIVKVRSKIGycpqfdalleymtgweI 1449
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLG----------------I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMY---ARIWGISehqiqpyVKKYLNSLDLeshanslisTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLL 1526
Cdd:cd03217 80 FLAFqypPEIPGVK-------NADFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLV 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 1527 WDTVIKIRESGKAIIITSHSMEECEAL-CTRLSIMVRGRLTCLGSP 1571
Cdd:cd03217 144 AEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1365-1584 |
8.59e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 8.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1365 KSPL-ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFID------GISLTKNIVKVRSKIGYCPQF 1437
Cdd:PRK13645 19 KTPFeFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1438 DALLEYMTGWEIMIMYARIwGISEHQIQPYvKKYLNSLDL----ESHANSLISTYSEGNKRRLSTA--IATMGKPSVifL 1511
Cdd:PRK13645 99 PEYQLFQETIEKDIAFGPV-NLGENKQEAY-KKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAgiIAMDGNTLV--L 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLknkFGNIYIL 1584
Cdd:PRK13645 175 DEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEI---FSNQELL 245
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
536-741 |
9.17e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 9.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 536 TTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP----TSGEAYVHGEDIsqHMDQVRNSLGLCPQQN--LL 609
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPV--APCALRGRKIATIMQNprSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 610 FDHL-TVSEHLYFYCRIKGVP----------QKMYLEETNNMLSAFnlmekcdAFskSLSGGMKRKLAIIIALIGGSKVA 678
Cdd:PRK10418 92 FNPLhTMHTHARETCLALGKPaddatltaalEAVGLENAARVLKLY-------PF--EMSGGMLQRMMIALALLCEAPFI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 679 ILDEPTSGMDPASRRSTWDILQTYKQNRT--ILLTTHYMDEADVLGDRIAIMVRGTLRCCGS--SVF 741
Cdd:PRK10418 163 IADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1373-1574 |
9.50e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.24 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1373 KNISLAIQERACFGLLGFNGAGKTTTFQILTGENIP---TAGDVFIDGISLTKNIVKVRSkiGYCPQFDALLEYMTGWEI 1449
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKEMRAIS--AYVQQDDLFIPTLTVREH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARIW---GISEHQIQPYVKKYLNSLDLESHANSLIST------YSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDP 1520
Cdd:TIGR00955 120 LMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1521 RARRLLWDTVIKIRESGKAIIITSH--SMEECEaLCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:TIGR00955 200 FMAYSVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQA 254
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
540-738 |
1.00e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 73.48 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS--QHMDQVRNSLGLCPQQ-NLLFDHLTVS 616
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTW 696
Cdd:PRK13644 97 EDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 697 D-ILQTYKQNRTILLTTHYMDEADVlGDRIAIMVRGTLRCCGS 738
Cdd:PRK13644 177 ErIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
540-728 |
1.36e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqhMDQVRNS----LGLCPQQNLLFDHLTV 615
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT--FNGPKSSqeagIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLY----FYCRIKGVP-QKMYlEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA 690
Cdd:PRK10762 97 AENIFlgreFVNRFGRIDwKKMY-AEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 691 SRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIM 728
Cdd:PRK10762 176 ETESLFRVIRELKsQGRGIVYISHRLKEIFEICDDVTVF 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1369-1565 |
1.38e-13 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 1.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT--KNIVKVRSKIGYCPQFDALLEYMTG 1446
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwQTAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIMIMYAriWGISEHQIQPYVKKYLNSLD-LESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRL 1525
Cdd:PRK11614 98 EENLAMGG--FFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 46358378 1526 LWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:PRK11614 176 IFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1370-1545 |
1.52e-13 |
|
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: 71.24 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGF-------------NGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQ 1436
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFtlnagealqvtgpNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1437 FDALLEYMTGWEIMIMYARIWGISehqiQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:TIGR01189 81 LPGLKPELSALENLHFWAAIHGGA----QRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
170 180
....*....|....*....|....*....
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSH 1545
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1371-1570 |
1.68e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 72.61 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKvrSKIGYCPQ-------FDALLE- 1442
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--NLVAYVPQseevdwsFPVLVEd 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 -YMTGWEIMIMYARIWGISEHQIqpyVKKYLNSLDLESHANSLISTYSEGNKRR--LSTAIATMGkpSVIFLDEPSTGMD 1519
Cdd:PRK15056 100 vVMMGRYGHMGWLRRAKKRDRQI---VTAALARVDMVEFRHRQIGELSGGQKKRvfLARAIAQQG--QVILLDEPFTGVD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1520 PRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTrLSIMVRGrlTCLGS 1570
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG--TVLAS 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
540-732 |
1.90e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 72.33 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLCPQ-QNL-LFDHLTVSE 617
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTfQHVrLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYfycrikgVPQKMYLEetNNMLS------AF------------------NLMEKCDAFSKSLSGGMKRKLAIIIALIG 673
Cdd:PRK11300 100 NLL-------VAQHQQLK--TGLFSgllktpAFrraesealdraatwlervGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 674 GSKVAILDEPTSGMDPasrRSTWDILQTYKQNR-----TILLTTHYMDEADVLGDRIAIMVRGT 732
Cdd:PRK11300 171 QPEILMLDEPAAGLNP---KETKELDELIAELRnehnvTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1371-1574 |
2.37e-13 |
|
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: 71.10 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALLEYMTgweI 1449
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ-DTFLFSGT---I 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 M--IMYAR--------IWGISEHQIQPYVKKYLNslDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:cd03254 94 MenIRLGRpnatdeevIEAAKEAGAHDFIMKLPN--GYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNID 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1520 PRARRLLWDTVIKIREsGKAIIITSHsmeecealctRLS-------IMV--RGRLTCLGSPQYL 1574
Cdd:cd03254 172 TETEKLIQEALEKLMK-GRTSIIIAH----------RLStiknadkILVldDGKIIEEGTHDEL 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
543-689 |
4.54e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 71.33 E-value: 4.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI----SQHMDQVRNSLGLCPQQNLLFDHLTVSEH 618
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 619 LYFYCRIKGVPQKMYLEETNNM-LSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
534-733 |
5.43e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 5.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 534 NNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH--MDQVRNS------------ 599
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspQDGLANGivyisedrkrdg 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 --LGLCPQQNLlfdHLTVSEHL-YFYCRIKGVPQKMyleETNNMLSAFNL-MEKCDAFSKSLSGGMKRKLAIIIALIGGS 675
Cdd:PRK10762 341 lvLGMSVKENM---SLTALRYFsRAGGSLKHADEQQ---AVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRP 414
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 676 KVAILDEPTSGMDPASRRSTWDILQTYKQN-RTILLTTHYMDEadVLG--DRIAIMVRGTL 733
Cdd:PRK10762 415 KVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
533-734 |
6.12e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 71.00 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 533 KNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEdisqhMDQVRNSLGLCPQqnllfdh 612
Cdd:PRK13546 32 HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----VSVIAISAGLSGQ------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 613 LTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:PRK13546 100 LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFA 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 46358378 693 RSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGTLR 734
Cdd:PRK13546 180 QKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1356-1545 |
6.21e-13 |
|
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: 67.86 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVfidgisltknIVKVRSKIGYCP 1435
Cdd:cd03221 3 LENLSKTYGGKLLL---KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------TWGSTVKIGYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFdalleymtgweimimyariwgisehqiqpyvkkylnsldleshanslistySEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03221 70 QL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|
gi 46358378 1516 TGMDPRARRLLWDTvikIRESGKAIIITSH 1545
Cdd:cd03221 99 NHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1387-1545 |
7.66e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 73.99 E-value: 7.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGE---NIPTAGDVFIDGISLTKNIVkvRSkIGYCPQFDALLEYMTGWEIMIMYARIW---GIS 1460
Cdd:TIGR00956 794 LMGASGAGKTTLLNVLAERvttGVITGGDRLVNGRPLDSSFQ--RS-IGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVS 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1461 EHQIQPYVKKYLNSLDLESHANSLISTYSEG----NKRRLSTAIATMGKP-SVIFLDEPSTGMDPRARRLLWDTVIKIRE 1535
Cdd:TIGR00956 871 KSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPkLLLFLDEPTSGLDSQTAWSICKLMRKLAD 950
|
170
....*....|
gi 46358378 1536 SGKAIIITSH 1545
Cdd:TIGR00956 951 HGQAILCTIH 960
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
540-713 |
7.71e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.46 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHlTVSEH 618
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR-SIEDN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LyfycRIkGVP----QKMYLEETNNMLSAFnLMEKCDAFS-------KSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:PRK13657 429 I----RV-GRPdatdEEMRAAAERAQAHDF-IERKPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
170 180
....*....|....*....|....*.
gi 46358378 688 DPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:PRK13657 503 DVETEAKVKAALDELMKGRTTFIIAH 528
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1372-1572 |
8.18e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.19 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT----KNIVKVRskiGYCPQ-----FDALLE 1442
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAdwspAELARRR---AVLPQhsslsFPFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 ymtgwEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTA------IATMGKPSVIFLDEPST 1516
Cdd:PRK13548 95 -----EVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvlaqlWEPDGPPRWLLLDEPTS 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1517 GMDPR--------ARRLlwdtvikIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13548 170 ALDLAhqhhvlrlARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1371-1556 |
9.17e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 73.00 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGislTKNIVKVRSkigycpqfdALLEYMTGWEIM 1450
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---SAALIAISS---------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTV 1530
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180
....*....|....*....|....*.
gi 46358378 1531 IKIRESGKAIIITSHSMEECEALCTR 1556
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTK 212
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1356-1580 |
1.54e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 69.61 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSKIGYCP 1435
Cdd:PRK10619 8 VIDLHKRYGEHEVL---KGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNG----QTINLVRDKDGQLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDA------------------LLEYMTGWE-IMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTY-SEGNKRR 1495
Cdd:PRK10619 81 VADKnqlrllrtrltmvfqhfnLWSHMTVLEnVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHlSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1496 LSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLk 1575
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL- 239
|
....*
gi 46358378 1576 nkFGN 1580
Cdd:PRK10619 240 --FGN 242
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1371-1566 |
1.57e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVK-VRSKIGYCP---QFDALLEYMT 1445
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDaIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1446 GWEIMIM-----YARIWGISEHQIQPYVKKYLNSLDLE-SHANSLISTYSEGNKRR--LSTAIATmgKPSVIFLDEPSTG 1517
Cdd:COG1129 347 IRENITLasldrLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKvvLAKWLAT--DPKVLILDEPTRG 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 1518 MDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:COG1129 425 IDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
540-731 |
1.62e-12 |
|
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: 72.46 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHlTVSEH 618
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYFYCRiKGVPQKMYLE---------ETNNMLSAFNLMEKCDAFSksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:TIGR01193 568 LLLGAK-ENVSQDEIWAaceiaeikdDIENMPLGYQTELSEEGSS--ISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 690 ASRRSTWDILqTYKQNRTILLTTHYMDEADvLGDRIAIMVRG 731
Cdd:TIGR01193 645 ITEKKIVNNL-LNLQDKTIIFVAHRLSVAK-QSDKIIVLDHG 684
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
522-718 |
2.00e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKV-AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGE-----------------AY 583
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 584 VHGEDISQ--------HMDQVRNSLGLCPQ--QNLLFDHlTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFNLMEkcDAF 653
Cdd:PRK13651 83 VLEKLVIQktrfkkikKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDE--SYL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 654 SKS---LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQT-YKQNRTILLTTHYMDEA 718
Cdd:PRK13651 160 QRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNV 228
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
543-733 |
2.41e-12 |
|
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: 69.06 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVRNSLGLC---------PQQNLl 609
Cdd:TIGR02769 29 NVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrkQRRAFRRDVQLVfqdspsavnPRMTV- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 610 fdHLTVSEHLYFYCRIKGVPQKmylEETNNMLSAFNL-MEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:TIGR02769 108 --RQIIGEPLRHLTSLDESEQK---ARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 689 PASRRSTWDILQTYKQNRTI--LLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
538-702 |
2.64e-12 |
|
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: 66.41 E-value: 2.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGeayvhgedisqhmdqvrnSLGLCPQQNLLFdhltvse 617
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG------------------RIGMPEGEDLLF------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 hlyfycrikgVPQKMYleetnnmLSAFNLMEK-CDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTW 696
Cdd:cd03223 69 ----------LPQRPY-------LPLGTLREQlIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
....*.
gi 46358378 697 DILQTY 702
Cdd:cd03223 132 QLLKEL 137
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
539-731 |
3.28e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 68.32 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH----MDQ------VRNSLGLCPQQNL 608
Cdd:TIGR02323 17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqLSEaerrrlMRTEWGFVHQNPR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 609 LFDHLTVSEHLYFYCRIKGVPQKMY---LEETNNMLSAFNL-MEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPT 684
Cdd:TIGR02323 97 DGLRMRVSAGANIGERLMAIGARHYgniRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPT 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 685 SGMDPASRRSTWDILQTYKQNRTI--LLTTHYMDEADVLGDRIAIMVRG 731
Cdd:TIGR02323 177 GGLDVSVQARLLDLLRGLVRDLGLavIIVTHDLGVARLLAQRLLVMQQG 225
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1354-1577 |
3.96e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 68.67 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELTKIYFKSPlILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGD---VFIDGISLT-KNIVKVRS 1429
Cdd:PRK13640 6 VEFKHVSFTYPDSK-KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTaKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 KIGYCPQF-DALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSV 1508
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1509 IFLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEaLCTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
522-718 |
3.99e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.46 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTtkvaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQ------ 595
Cdd:PRK10619 6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 596 --------VRNSLGLCPQQNLLFDHLTVSEH-LYFYCRIKGVPQKMYLEETNNMLSAFNLMEKC-DAFSKSLSGGMKRKL 665
Cdd:PRK10619 82 adknqlrlLRTRLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 666 AIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEA 718
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFA 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1353-1557 |
4.00e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.86 E-value: 4.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIYFKSPLIlavKNISLAIQ--ERAcfGLLGFNGAGKTTTFQILTGENIPTAGDVFIdGISLtknivkvrs 1429
Cdd:COG0488 314 KVLeLEGLSKSYGDKTLL---DDLSLRIDrgDRI--GLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV--------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1430 KIGYCPQ-FDALLEYMTGWEIMimyariWGISEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIATMGKPS 1507
Cdd:COG0488 379 KIGYFDQhQEELDPDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1508 VIFLDEPSTGMDPRARRLL------WDtvikiresGkAIIITSHSMEECEALCTRL 1557
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALeealddFP--------G-TVLLVSHDRYFLDRVATRI 499
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1371-1572 |
4.09e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.48 E-value: 4.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT--KNIVKVRSKIGYCPQfDALLEYM--TG 1446
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQ-NPETQFVgrTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTA-IATMgKPSVIFLDEPSTGMDPRARRL 1525
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAgILTM-EPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 1526 LWDTVIKIRESGKAIIITSHSMEECEAlCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPE 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1370-1566 |
5.44e-12 |
|
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: 66.18 E-value: 5.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQfdalleymtgwei 1449
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 mimyariwgisehqiQPYVkkYLNSLdleshANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDT 1529
Cdd:cd03247 83 ---------------RPYL--FDTTL-----RNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 1530 VIKIREsGKAIIITSHSMEECEALcTRLSIMVRGRLT 1566
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKII 175
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
538-688 |
5.48e-12 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 68.09 E-value: 5.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMD-QVRNSLGLCPQQNLLFDHLTVS 616
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 E--------HLYFYCRIKgvpqKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:PRK10253 100 ElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
551-713 |
6.92e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.11 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 551 GQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSL-----GLCPQQNLLFDHLTVSEHLYFYCRI 625
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 626 KGVPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILqtYKQN 705
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLL--FSLN 193
|
170
....*....|..
gi 46358378 706 R----TILLTTH 713
Cdd:PRK10584 194 RehgtTLILVTH 205
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
522-731 |
7.35e-12 |
|
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: 69.85 E-value: 7.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP--PTSGEAYVHGEDI-SQHM-DQVR 597
Cdd:TIGR02633 2 LEMKGIVKTF---GGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkASNIrDTER 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 598 NSLGLCPQQNLLFDHLTVSEHLYFYCRIKGVPQKMYLEETnnMLSAFNLME--KCDAFSKS-----LSGGMKRKLAIIIA 670
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAM--YLRAKNLLRelQLDADNVTrpvgdYGGGQQQLVEIAKA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 671 LIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:TIGR02633 156 LNKQARLLILDEPSSSLTEKETEILLDIIRDLKAhGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1372-1566 |
7.91e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 69.81 E-value: 7.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT--------KN----IVKVRSKIGYCPQFD- 1438
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprspldavKKgmayITESRRDNGFFPNFSi 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1439 ----ALLEYMTgweiMIMYARIWGI-SEHQIQPYVKKYLNSLDLESHA-NSLISTYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:PRK09700 359 aqnmAISRSLK----DGGYKGAMGLfHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLT 488
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1371-1572 |
8.16e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 8.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL-------TKNIVKVRSKIGYCPQFDALLEY 1443
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWEIMIMY-ARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:PRK11124 97 LTVQQNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1523 RRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL------TCLGSPQ 1572
Cdd:PRK11124 177 TAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIveqgdaSCFTQPQ 232
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
516-726 |
1.21e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.98 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 516 TDLTAGIQIKHLHKVFqknNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLyPPTSGEAYVHG--EDISQ-- 591
Cdd:PRK14258 2 SKLIPAIKVNNLSFYY---DTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrvEFFNQni 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 592 -----HMDQVRNSLGLC-PQQNLLfdHLTVSEHLYFYCRIKGVPQKMYLEE-TNNMLSAFNLMEKC-DAFSKS---LSGG 660
Cdd:PRK14258 77 yerrvNLNRLRRQVSMVhPKPNLF--PMSVYDNVAYGVKIVGWRPKLEIDDiVESALKDADLWDEIkHKIHKSaldLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 661 MKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIA 726
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1371-1570 |
1.21e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 66.68 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQE---RAcfgLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIvkVRSKIGYCPQFDALLEY 1443
Cdd:COG4674 25 ALNDLSLYVDPgelRV---IIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGldehEI--ARLGIGRKFQKPTVFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWE-IMIMYAR---IWGISEHQIQPYVKKYLNSL----DLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:COG4674 100 LTVFEnLELALKGdrgVFASLFARLTAEERDRIEEVletiGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESgKAIIITSHSMEECEALCTRLSIMVRGRLTCLGS 1570
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGK-HSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
515-725 |
1.45e-11 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 66.62 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 515 PTDLTAGIQ--IKHLHKVFQKNNTtkvaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH 592
Cdd:PRK11247 4 TARLNQGTPllLNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 593 MDQVRnslgLCPQQNLLFDHLTVSEHLYFycRIKGVPQKMYLEetnnMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALI 672
Cdd:PRK11247 80 REDTR----LMFQDARLLPWKKVIDNVGL--GLKGQWRDAALQ----ALAAVGLADRANEWPAALSGGQKQRVALARALI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 673 GGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRI 725
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHgfTVLLVTHDVSEAVAMADRV 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
307-721 |
1.82e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 69.37 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 307 FTFLCLYFINIIVMCMVLFvKIEPAPIFQYndptLVFIFLLFYAISSIFFsfMVSTLFNKVSLAMSLGSFLFFltyfpAV 386
Cdd:TIGR00956 507 FKIIESVVFNIILYFMVNF-RRTAGRFFFY----LLILFICTLAMSHLFR--SIGAVTKTLSEAMTPAAILLL-----AL 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 387 AMHQSF----ERMPSKQKLIWSFDfnvGMAFGFRFLVNTDAKKTGMKWSNIFLSTD-----SDSFLFAYVLGMLLADAFI 457
Cdd:TIGR00956 575 SIYTGFaiprPSMLGWSKWIYYVN---PLAYAFESLMVNEFHGRRFECSQYVPSGGgydnlGVTNKVCTVVGAEPGQDYV 651
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 458 YGlvAWYIEAVFPGEY-----GVPKPWNF--FLMHSYW----FGEPPQQKLEITQFYERVESKYFEAEPT------DLTA 520
Cdd:TIGR00956 652 DG--DDYLKLSFQYYNshkwrNFGIIIGFtvFFFFVYIllteFNKGAKQKGEILVFRRGSLKRAKKAGETsasnknDIEA 729
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 521 GIQIKHL--------------------HKVFQ-KNNTTKVAIKDLSLNLYE--------GQVTVLLGHNGAGKSTTLSIL 571
Cdd:TIGR00956 730 GEVLGSTdltdesddvndekdmekesgEDIFHwRNLTYEVKIKKEKRVILNnvdgwvkpGTLTALMGASGAGKTTLLNVL 809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 572 SGLYPP---TSGEAYVHGEDISQHMDQvrnSLGLCPQQNLLFDHLTVSEHLYFYCRI---KGVP--QKM-YLEETNNMLS 642
Cdd:TIGR00956 810 AERVTTgviTGGDRLVNGRPLDSSFQR---SIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSksEKMeYVEEVIKLLE 886
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 643 afnlMEK-CDAF----SKSLSGGMKRKLAIIIALIGGSKVAI-LDEPTSGMDPasrRSTWDILQTYKQ----NRTILLTT 712
Cdd:TIGR00956 887 ----MESyADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDS---QTAWSICKLMRKladhGQAILCTI 959
|
490
....*....|....
gi 46358378 713 H-----YMDEADVL 721
Cdd:TIGR00956 960 HqpsaiLFEEFDRL 973
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
523-748 |
2.55e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.96 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHKVFQKNNTT-----KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQV 596
Cdd:PRK10575 4 YTNHSDTTFALRNVSfrvpgRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQQNLLFDHLTVSEhLYFYCRIK--------GVPQKMYLEETNNMLSAFNLMEKcdaFSKSLSGGMKRKLAII 668
Cdd:PRK10575 84 ARKVAYLPQQLPAAEGMTVRE-LVAIGRYPwhgalgrfGAADREKVEEAISLVGLKPLAHR---LVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 669 IALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMVRGTLRCCGS------SV 740
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTpaelmrGE 239
|
....*...
gi 46358378 741 FLKRLYGV 748
Cdd:PRK10575 240 TLEQIYGI 247
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
532-732 |
3.04e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 64.41 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 532 QKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGedisqhmdqvrnSLGLCPQQNLLFd 611
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQEPWIQ- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 612 HLTVSEHLYFycrikGVP--QKMYLEetnnMLSAFNLMEKCDAFSK-----------SLSGGMKRKLAIIIALIGGSKVA 678
Cdd:cd03250 79 NGTIRENILF-----GKPfdEERYEK----VIKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 679 ILDEPTSGMDPASRRSTWD--ILQTYKQNRTILLTTH---YMDEAdvlgDRIAIMVRGT 732
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1372-1572 |
3.25e-11 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 65.42 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK-IGYCPQFDALLEYMTGWEiM 1450
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARrLALLPQHHLTPEGITVRE-L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IMYAR-----IWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRL 1525
Cdd:PRK11231 97 VAYGRspwlsLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 46358378 1526 LWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK11231 177 LMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1371-1574 |
3.33e-11 |
|
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: 67.86 E-value: 3.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALLEYMTGWEI 1449
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQ-NPYLFAGTIREN 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARiwGISEHQIQP-----YVKKYLNSL------DLESHANSListySEGNKRRLSTAIATMGKPSVIFLDEPSTGM 1518
Cdd:COG4988 431 LRLGRP--DASDEELEAaleaaGLDEFVAALpdgldtPLGEGGRGL----SGGQAQRLALARALLRDAPLLLLDEPTAHL 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1519 DPRARRLLWDTVIKIREsGKAIIITSHSMEECeALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:COG4988 505 DAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEEL 558
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
542-733 |
3.58e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 3.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 542 KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQVRNSLGLC--P---QQNLLF------ 610
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPedrQSSGLYldapla 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 ---DHLTVSEHLYFycrIKGVPQKMYLEETNNMLSAfnlmeKC---DAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPT 684
Cdd:PRK15439 360 wnvCALTHNRRGFW---IKPARENAVLERYRRALNI-----KFnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 685 SGMDPASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK15439 432 RGVDVSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1372-1572 |
4.22e-11 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 66.79 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSK-IGYCPQFDALLEYMTGWEIM 1450
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRrVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IM-----YARIWGISEHQiQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD-PRARR 1524
Cdd:PRK09536 99 EMgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 1525 LLwDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
530-733 |
4.42e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.50 E-value: 4.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 530 VFQKNNTTKV---AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS--QHMDQVRNSLGLCP 604
Cdd:PRK09700 265 VFEVRNVTSRdrkKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 605 Q---QNLLFDHLTVSEHLYFYCRIK------------GVPQKMYLEETNNMLSAfnlmeKCDAFSKS---LSGGMKRKLA 666
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQNMAISRSLKdggykgamglfhEVDEQRTAENQRELLAL-----KCHSVNQNiteLSGGNQQKVL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 667 IIIALIGGSKVAILDEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK09700 420 ISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
551-713 |
5.33e-11 |
|
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: 63.42 E-value: 5.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 551 GQVTVLLGHNGAGKSTTLSILS-----GLyppTSGEAYVHGEDISQHMdqvRNSLGLCPQQNLLFDHLTVSEHLYFYCRI 625
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLAgrktaGV---ITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 626 KGvpqkmyleetnnmlsafnlmekcdafsksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPasrRSTWDILQTYK-- 703
Cdd:cd03232 107 RG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS---QAAYNIVRFLKkl 154
|
170
....*....|..
gi 46358378 704 --QNRTILLTTH 713
Cdd:cd03232 155 adSGQAILCTIH 166
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
518-731 |
5.47e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.44 E-value: 5.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 518 LTAG-IQIKHLHKVFQKNnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQV 596
Cdd:PRK10790 336 LQSGrIDIDNVSFAYRDD---NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 -RNSLGLCPQQ-----NLLFDHLT----VSEHLYFYCR--------IKGVPQKMY--LEETNNMLSAfnlmekcdafsks 656
Cdd:PRK10790 413 lRQGVAMVQQDpvvlaDTFLANVTlgrdISEEQVWQALetvqlaelARSLPDGLYtpLGEQGNNLSV------------- 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 657 lsgGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMDEAdVLGDRIAIMVRG 731
Cdd:PRK10790 480 ---GQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRG 550
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1373-1566 |
5.51e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.00 E-value: 5.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1373 KNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIG--YCP---QFDAL-LEYMTG 1446
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGlvYLPedrQSSGLyLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIM-IMYAR--IWgISEHQIQPYVKKYLNSLDLE-SHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:PRK15439 360 WNVCaLTHNRrgFW-IKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 1523 RRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEIS 482
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1375-1565 |
5.62e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.42 E-value: 5.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1375 ISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK----NIVKVRSK-IGYCPQFDALLEYMTGWEI 1449
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLRAKhVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDT 1529
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADL 188
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 1530 VIKI-RESGKAIIITSHSmEECEALCTRLSIMVRGRL 1565
Cdd:PRK10584 189 LFSLnREHGTTLILVTHD-LQLAARCDRRLRLVNGQL 224
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1387-1563 |
1.00e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 67.18 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGENIP--TAGDVFIDGisLTKNIVKVRSKIGYCPQFDALLEYMTGWEIMIMYARIW---GISE 1461
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISG--FPKKQETFARISGYCEQNDIHSPQVTVRESLIYSAFLRlpkEVSK 988
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1462 HQIQPYVKKYLNSLDLESHANSL-----ISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRES 1536
Cdd:PLN03140 989 EEKMMFVDEVMELVELDNLKDAIvglpgVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDT 1068
|
170 180
....*....|....*....|....*....
gi 46358378 1537 GKAIIITSH--SMEECEALcTRLSIMVRG 1563
Cdd:PLN03140 1069 GRTVVCTIHqpSIDIFEAF-DELLLMKRG 1096
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
538-733 |
1.06e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 64.35 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAY-----VHGEDISQHMD--QVRNSLGLCPQQNLLF 610
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 DhLTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKC-DAFSKS---LSGGMKRKLAIIIALIGGSKVAILDEPTS 685
Cdd:PRK14271 114 P-MSIMDNVLAGVRAhKLVPRKEFRGVAQARLTEVGLWDAVkDRLSDSpfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 686 GMDPASRRSTWDILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
530-727 |
1.09e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.11 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 530 VFQKNNTTK-----VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP--PTSGEAYVHGEDISQH--MDQVRNSL 600
Cdd:PRK13549 5 LLEMKNITKtfggvKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQASniRDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GLCPQQNLLFDHLTVSEHLYFYCRI--KGVPQ--KMYLeETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSK 676
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEItpGGIMDydAMYL-RAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 677 VAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDRIAI 727
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIRDLKaHGIACIYISHKLNEVKAISDTICV 215
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
544-721 |
1.10e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.36 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNslglcpqqnlLF-----D-HLTvs 616
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADnREAYRQ----------LFsavfsDfHLF-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLYfycrikGVPQKMYLEETNNMLSAFNLMEKC----DAFSK-SLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS 691
Cdd:COG4615 419 DRLL------GLDGEADPARARELLERLELDHKVsvedGRFSTtDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEF 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 692 RRstW---DILQTYK-QNRTILLTTH---YMDEADVL 721
Cdd:COG4615 493 RR--VfytELLPELKaRGKTVIAISHddrYFDLADRV 527
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1358-1572 |
1.53e-10 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 64.72 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKI--YFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRsKIGYCP 1435
Cdd:PRK10851 4 EIANIkkSFGRTQVL--NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1436 QFDALLEYMTGWEI----MIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFL 1511
Cdd:PRK10851 81 QHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKIRESGK--AIIITsHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK10851 161 DEPFGALDAQVRKELRRWLRQLHEELKftSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
522-731 |
2.06e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPP---TSGEAYVHGEDI----SQHMD 594
Cdd:PRK09473 13 LDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 595 QVRNSlglcpQQNLLF-DHLTvseHLYFYCRI-----------KGVPQKMYLEETNNMLSAFNLME---KCDAFSKSLSG 659
Cdd:PRK09473 93 KLRAE-----QISMIFqDPMT---SLNPYMRVgeqlmevlmlhKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 660 GMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHymDEADVLG--DRIAIMVRG 731
Cdd:PRK09473 165 GMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITH--DLGVVAGicDKVLVMYAG 238
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
538-713 |
2.21e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.82 E-value: 2.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGeayvhgedISQHMDQVRnsLGLCPQQnLLFDH---LT 614
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKRNGKLR--IGYVPQK-LYLDTtlpLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLyfycRIKGVPQKMYLEETNNMLSAFNLMekcDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRS 694
Cdd:PRK09544 86 VNRFL----RLRPGTKKEDILPALKRVQAGHLI---DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|.
gi 46358378 695 TWDILQTYKQ--NRTILLTTH 713
Cdd:PRK09544 159 LYDLIDQLRRelDCAVLMVSH 179
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1370-1545 |
3.78e-10 |
|
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: 61.35 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGF-------------NGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSKIGYCPQ 1436
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFtlaagealqvtgpNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1437 FDALLEYMTGWEIMIMYARIWGISEhqiqpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:cd03231 81 APGIKTTLSVLENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180
....*....|....*....|....*....
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSH 1545
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
544-689 |
4.29e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.40 E-value: 4.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE-----DISQHMDQVRNSLGLCPQqnllfdhLTVSEH 618
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKtatrgDRSRFMAYLGHLPGLKAD-------LSTLEN 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 619 LYFYCRIKGV-PQKMyleeTNNMLSAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:PRK13543 103 LHFLCGLHGRrAKQM----PGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1371-1546 |
4.47e-10 |
|
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: 64.30 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIV-KVRSKIGYCPQ----FDA-LLEYM 1444
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQdahlFDTtVRENL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 -------TGWEIMIMYARIwgisehQIQPYVKKYLNSLD--LESHANSListySEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:TIGR02868 430 rlarpdaTDEELWAALERV------GLADWLRALPDGLDtvLGEGGARL----SGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 46358378 1516 TGMDPRARRLLWDTVIKIrESGKAIIITSHS 1546
Cdd:TIGR02868 500 EHLDAETADELLEDLLAA-LSGRTVVLITHH 529
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
544-757 |
4.60e-10 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.78 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPtSGEAYVHGEDISQ--HMDQVRNSLGLCPQQNLLFDhLTVSEHLYF 621
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDwsAAELARHRAYLSQQQSPPFA-MPVFQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 622 YCRIKGVPQkmYLEETNNML-SAFNLMEKCDAFSKSLSGG-MKR-KLAIII-----ALIGGSKVAILDEPTSGMDPASRR 693
Cdd:COG4138 93 HQPAGASSE--AVEQLLAQLaEALGLEDKLSRPLTQLSGGeWQRvRLAAVLlqvwpTINPEGQLLLLDEPMNSLDVAQQA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 694 STWDILQTYK-QNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGSS--VF----LKRLYGVGSHLVMVKE 757
Cdd:COG4138 171 ALDRLLRELCqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETaeVMtpenLSEVFGVKFRRLEVEG 241
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1370-1572 |
4.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 62.08 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIGYC---P--QFDALLey 1443
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVfqnPdnQFVGSI-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 mtgweimIMYARIWGISEHQIqPY------VKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTG 1517
Cdd:PRK13648 101 -------VKYDVAFGLENHAV-PYdemhrrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1518 MDPRARRLLWDTVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISiTHDLSEA-MEADHVIVMNKGTVYKEGTPT 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
522-735 |
5.73e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 5.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKS-TTLSILSGLYPP----TSGEAYVHGEDI----SQH 592
Cdd:PRK15134 6 LAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLlhasEQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 593 MDQVR-NSLGLCPQQ-----NLLfdHlTVSEHLYFYCRI-KGVPQKMYLEEtnnMLSAF------NLMEKCDAFSKSLSG 659
Cdd:PRK15134 86 LRGVRgNKIAMIFQEpmvslNPL--H-TLEKQLYEVLSLhRGMRREAARGE---ILNCLdrvgirQAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 660 GMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGtlRC 735
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNG--RC 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1387-1566 |
6.12e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 61.04 E-value: 6.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGENIPTAGDVFIDG--ISLTKN--IVKVRSKIGYCPQFDALLEYMTGWEIMIMYARIWGISEH 1462
Cdd:PRK10908 33 LTGHSGAGKSTLLKLICGIERPSAGKIWFSGhdITRLKNreVPFLRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1463 QIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRarrlLWDTVIKIRES----GK 1538
Cdd:PRK10908 113 DIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDA----LSEGILRLFEEfnrvGV 188
|
170 180
....*....|....*....|....*...
gi 46358378 1539 AIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK10908 189 TVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1335-1545 |
8.42e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 63.65 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1335 VENERREILYQPEKFLNcPVLIKELTKIYFKSPLILAvkNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDvf 1414
Cdd:PRK10636 294 VDNPFHFSFRAPESLPN-PLLKMEKVSAGYGDRIILD--SIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGE-- 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1415 idgISLTKNIvkvrsKIGYCPQFDalLEYMTGWEIMIMY-ARiwgISEHQIQPYVKKYLNSLDLESHANSLIST-YSEGN 1492
Cdd:PRK10636 369 ---IGLAKGI-----KLGYFAQHQ--LEFLRADESPLQHlAR---LAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1493 KRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIResgKAIIITSH 1545
Cdd:PRK10636 436 KARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFE---GALVVVSH 485
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1372-1584 |
9.51e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 61.22 E-value: 9.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILT------GENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQFDALLEYM 1444
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYARIWGISE-HQIQPYVKKYLNSLDL--ESH--ANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEkREIKKIVEECLRKVGLwkEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1520 PRARRLLWDTVIKIRESgKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL----KNKFGNIYIL 1584
Cdd:PRK14246 186 IVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1350-1599 |
9.57e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.37 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1350 LNCPVLIKELTKIY---------FKSPLI--------LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGD 1412
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrtnkerMKDALIpkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1413 VFIDGislTKNIVKVRSkigycpqfdALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGN 1492
Cdd:PRK13546 81 VDRNG---EVSVIAISA---------GLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1493 KRRLSTAIATMGKPSVIFLDEP-STGMDPRARRLLwDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGS- 1570
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-DKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEl 227
|
250 260 270
....*....|....*....|....*....|...
gi 46358378 1571 ----PQYlkNKFGNIYilkaKVKSGETLDEFKN 1599
Cdd:PRK13546 228 ddvlPKY--EAFLNDF----KKKSKAEQKEFRN 254
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
522-745 |
1.05e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.81 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFqknNTTKVaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSG--LYPPTSGEAYVHGEDISQHMDQVRNS 599
Cdd:CHL00131 8 LEIKNLHASV---NENEI-LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LG---------------------LCPQQNLLFDHLTVSEHLYFYCRIKgvpQKMYLEetnNMLSAF---NLMEkcdafsk 655
Cdd:CHL00131 84 LGiflafqypieipgvsnadflrLAYNSKRKFQGLPELDPLEFLEIIN---EKLKLV---GMDPSFlsrNVNE------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 656 SLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEAD-VLGDRIAIMVRGTL 733
Cdd:CHL00131 151 GFSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKI 230
|
250
....*....|..
gi 46358378 734 RCCGSSVFLKRL 745
Cdd:CHL00131 231 IKTGDAELAKEL 242
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1370-1566 |
1.16e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVR-SKIGYCP---QFDALLEYM 1444
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITgLSPRERRrLGVAYIPedrLGRGLVPDM 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMyariwgiSEHQIQPYVKKY-LNSLDLESHANSLISTY--------------SEGNKRRLSTAIATMGKPSVI 1509
Cdd:COG3845 352 SVAENLIL-------GRYRRPPFSRGGfLDRKAIRAFAEELIEEFdvrtpgpdtparslSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1356-1565 |
1.19e-09 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 60.92 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKiYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAG-----DVFIDG---ISLTKNIVK- 1426
Cdd:PRK11264 6 VKNLVK-KFHGQTVL--HGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTarsLSQQKGLIRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1427 VRSKIGYCPQFDALLEYMTGWEIMIMYARIW-GISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGK 1505
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVkGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1506 PSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1356-1578 |
1.23e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 62.90 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKiYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTG--ENIPTAGDVfIDGISLTKNI--VKVRSKI 1431
Cdd:TIGR03269 3 VKNLTK-KFDGKEVL--KNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRI-IYHVALCEKCgyVERPSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GY-CPQFDALLE--------------YMTGWEIMIMYARIWGISE------------HQI----QPYVKKYLNSLD---L 1477
Cdd:TIGR03269 79 GEpCPVCGGTLEpeevdfwnlsdklrRRIRKRIAIMLQRTFALYGddtvldnvlealEEIgyegKEAVGRAVDLIEmvqL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1478 ESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIK-IRESGKAIIITSHSMEECEALCTR 1556
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEaVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260
....*....|....*....|..
gi 46358378 1557 LSIMVRGRLTCLGSPQYLKNKF 1578
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVF 260
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1387-1569 |
1.27e-09 |
|
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: 59.81 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRSkIGYCPQFDALLEYMTgWEIMIMYARIWGIS-EHQIQ 1465
Cdd:cd03298 29 IVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLT-VEQNVGLGLSPGLKlTAEDR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1466 PYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKI-RESGKAIIITS 1544
Cdd:cd03298 107 QAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVT 186
|
170 180
....*....|....*....|....*
gi 46358378 1545 HSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:cd03298 187 HQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
527-731 |
2.15e-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: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 527 LHKVFQKNNTTKVAI-KDLSLNLYEGQVTVLLGHNGAGKSTTL-SILSGLYPPTSG-EAYVHGEDISQH--MDQVRNSLG 601
Cdd:TIGR00956 62 FRKLKKFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLkTIASNTDGFHIGvEGVITYDGITPEeiKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 602 LCPQQNLLFDHLTVSEHLYFYC-------RIKGVPQKMYLE-ETNNMLSAFNLMEKCDA-----FSKSLSGGMKRKLAII 668
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAArcktpqnRPDGVSREEYAKhIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 669 IALIGGSKVAILDEPTSGMDPAsrrSTWDILQTYKQNRTILLTTHYM------DEADVLGDRIAIMVRG 731
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSA---TALEFIRALKTSANILDTTPLVaiyqcsQDAYELFDKVIVLYEG 287
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
551-713 |
2.34e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.20 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 551 GQVTVLLGHNGAGKSTTLSILSGLYPPTS--GEAYVHGEDISQhmdQVRNSLGLCPQQNLLFDHLTVSEHLYFyCRIKGV 628
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVF-CSLLRL 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 629 PQKMYLEE----TNNMLSAFNLMeKC------DAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP-ASRRSTWD 697
Cdd:PLN03211 170 PKSLTKQEkilvAESVISELGLT-KCentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDAtAAYRLVLT 248
|
170
....*....|....*.
gi 46358378 698 ILQTYKQNRTILLTTH 713
Cdd:PLN03211 249 LGSLAQKGKTIVTSMH 264
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1371-1545 |
2.41e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSkigycpQFDA------LLEY 1443
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRK------LFSAvftdfhLFDQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWEimimyariwgisEHQIQP-YVKKYLNSLDLE---SHANSLIST--YSEGNKRRLSTAIATMGKPSVIFLDEPSTG 1517
Cdd:PRK10522 412 LLGPE------------GKPANPaLVEKWLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180
....*....|....*....|....*....
gi 46358378 1518 MDPRARRLLWDTVI-KIRESGKAIIITSH 1545
Cdd:PRK10522 480 QDPHFRREFYQVLLpLLQEMGKTIFAISH 508
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
540-734 |
2.50e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 2.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS-QHMDQVRNSLGLCPQQNLLFDHL----- 613
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAVFTDFHLFDQLlgpeg 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 -TVSEHLYF-YCRIKGVPQKmyLEETNNMLSafNLmekcdafskSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS 691
Cdd:PRK10522 418 kPANPALVEkWLERLKMAHK--LELEDGRIS--NL---------KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHF 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 692 RRSTWDIL--QTYKQNRTILLTTH---YMDEAdvlgDRIAIMVRGTLR 734
Cdd:PRK10522 485 RREFYQVLlpLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQLS 528
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1358-1560 |
2.63e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 59.71 E-value: 2.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISltknIVKVRSKIGYCPQF 1437
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP----VEGPGAERGVVFQN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1438 DALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTG 1517
Cdd:PRK11248 79 EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 1518 MDPRARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIM 1560
Cdd:PRK11248 159 LDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLL 202
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1371-1572 |
2.70e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 61.72 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALLEYMTgweI 1449
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTFLFSGT---I 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 M--IMYARIwGISEHQIQPYVKKylnsldleSHANSLI---------------STYSEGNKRRLSTAIATMGKPSVIFLD 1512
Cdd:COG1132 431 RenIRYGRP-DATDEEVEEAAKA--------AQAHEFIealpdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILD 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1513 EPSTGMDPRARRLLWDTVIKIREsGKAIIITSHsmeecealctRLS-------IMV--RGRLTCLGSPQ 1572
Cdd:COG1132 502 EATSALDTETEALIQEALERLMK-GRTTIVIAH----------RLStirnadrILVldDGRIVEQGTHE 559
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1379-1532 |
3.18e-09 |
|
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: 59.34 E-value: 3.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1379 IQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDgisltknivkvRSKIGYCPQfdalleYMTGWEIMIMYARIWG 1458
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIE-----------LDTVSYKPQ------YIKADYEGTVRDLLSS 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1459 ISE-HQIQPYVK-KYLNSLDLESHANSLISTYSEGNKRRLSTAiATMGKPSVIFL-DEPSTGMDPRaRRLLWDTVIK 1532
Cdd:cd03237 85 ITKdFYTHPYFKtEIAKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDADIYLlDEPSAYLDVE-QRLMASKVIR 159
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1372-1569 |
3.46e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 59.47 E-value: 3.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTT---TFQILT--GENIPTAGDVFIDGISLTK---NIVKVRSKIGYCPQFDALLEY 1443
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGWEIMIMYARIWGI--SEHQIQPYVKKYLNSLDL----ESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTG 1517
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1518 MDPRARRLLWDTVIKIRESgKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:PRK14267 180 IDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
524-731 |
4.24e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.41 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 524 IKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVH--------------GEDI 589
Cdd:PRK10261 15 VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrqvielSEQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 590 SQHMDQVRNS-LGLCPQQNL--LFDHLTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLMEKCDAFSK---SLSGGMK 662
Cdd:PRK10261 95 AAQMRHVRGAdMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMR 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 663 RKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRT--ILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK10261 175 QRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
522-688 |
4.47e-09 |
|
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: 61.10 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVhGE--DISqHMDQVRNS 599
Cdd:TIGR03719 323 IEAENLTKAFGD----KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GEtvKLA-YVDQSRDA 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGlcPQQNLL------FDHLTVSEHlyfycrikGVPQKMYleetnnmLSAFNLM----EKcdaFSKSLSGGMKRKLAIII 669
Cdd:TIGR03719 397 LD--PNKTVWeeisggLDIIKLGKR--------EIPSRAY-------VGRFNFKgsdqQK---KVGQLSGGERNRVHLAK 456
|
170
....*....|....*....
gi 46358378 670 ALIGGSKVAILDEPTSGMD 688
Cdd:TIGR03719 457 TLKSGGNVLLLDEPTNDLD 475
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1371-1564 |
5.60e-09 |
|
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: 60.61 E-value: 5.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTG--ENIPTAGDVFIDGISLT---------KNIVKVRSKIGYCPQFDA 1439
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKasnirdterAGIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1440 LLEYMTGWEIMI---------MYARiwgisehqiqpyVKKYLNSLDLESHANSL-ISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:TIGR02633 96 AENIFLGNEITLpggrmaynaMYLR------------AKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:TIGR02633 164 ILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1372-1572 |
7.10e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 7.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltknivkvRSKIGYCPQ---FDALLEyMTGWE 1448
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------KLRIGYVPQklyLDTTLP-LTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMIMYAriwGISEHQIQPYVKKYLNSLDLESHANSListySEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWD 1528
Cdd:PRK09544 89 FLRLRP---GTKKEDILPALKRVQAGHLIDAPMQKL----SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1529 TVIKIR-ESGKAIIITSHSM-----EECEALCtrlsimVRGRLTCLGSPQ 1572
Cdd:PRK09544 162 LIDQLRrELDCAVLMVSHDLhlvmaKTDEVLC------LNHHICCSGTPE 205
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
535-692 |
7.46e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.19 E-value: 7.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 535 NTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVRNSLGLCPQqnllf 610
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNiakpYCTYIGHNLGLKLE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 611 dhLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAFnLMEKCdafsKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA 690
Cdd:PRK13541 85 --MTVFENLKFWSEIYNSAETLYAAIHYFKLHDL-LDEKC----YSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
..
gi 46358378 691 SR 692
Cdd:PRK13541 158 NR 159
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1371-1548 |
7.49e-09 |
|
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: 60.38 E-value: 7.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKV-RSKIGYCPQFDALLEyMTGWEI 1449
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSwRDQIAWVPQHPFLFA-GTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARiwGISEHQIQPYVKK-YLNSL--DLESHANSLI----STYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:TIGR02857 416 IRLARP--DASDAEIREALERaGLDEFvaALPQGLDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180
....*....|....*....|....*.
gi 46358378 1523 RRLLWDTVIKIREsGKAIIITSHSME 1548
Cdd:TIGR02857 494 EAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
539-731 |
8.63e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 58.40 E-value: 8.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 539 VAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDisqhmDQVRNSLGLC-PQQNLL------FD 611
Cdd:PRK11701 20 KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD-----GQLRDLYALSeAERRRLlrtewgFV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 612 H--------LTVS------EhlyfycRIKGVPQKMY--LEETnnmlsAFNLMEKC-------DAFSKSLSGGMKRKLAII 668
Cdd:PRK11701 95 HqhprdglrMQVSaggnigE------RLMAVGARHYgdIRAT-----AGDWLERVeidaariDDLPTTFSGGMQQRLQIA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 669 IALIGGSKVAILDEPTSGMDPASRRSTWDILQTY--KQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK11701 164 RNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvrELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
540-731 |
1.13e-08 |
|
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: 57.04 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFDHlTVSEH 618
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSG-TIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYfycrikgvPQKMYLEEtnNMLSAFNLMEKCDafskSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDI 698
Cdd:cd03369 102 LD--------PFDEYSDE--EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190
....*....|....*....|....*....|....
gi 46358378 699 LQTYKQNRTILLTTHYMDE-ADVlgDRIAIMVRG 731
Cdd:cd03369 168 IREEFTNSTILTIAHRLRTiIDY--DKILVMDAG 199
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1374-1576 |
1.30e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.85 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1374 NISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDG---ISLTKN-IVKVRSKIGYCPQFDALLEYMTGWEI 1449
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGeniPAMSRSrLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MImyariWGISEHQ------IQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRAR 1523
Cdd:PRK11831 105 VA-----YPLREHTqlpaplLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1524 RLLwdtVIKIRESGKAI----IITSHSMEECEALCTRLSIMVRGRLTCLGSPQYLKN 1576
Cdd:PRK11831 180 GVL---VKLISELNSALgvtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
519-737 |
1.33e-08 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.97 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 519 TAGIQIKHLHKVFQKNNTtkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQvrN 598
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK--N 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 599 SLGLCPQQN--------LLFDHLTVSE--HLYFYCRikgvPQKMYLEETNNMLSAFNLMEKCDAFSKSLSGGMKRKLAII 668
Cdd:PRK15056 79 LVAYVPQSEevdwsfpvLVEDVVMMGRygHMGWLRR----AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 669 IALIGGSKVAILDEPTSGMDPASRRSTWDILQTYK-QNRTILLTTHYMDEADVLGDrIAIMVRGTLRCCG 737
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASG 223
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1371-1571 |
1.37e-08 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 56.65 E-value: 1.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQFDALLE--YMTGW 1447
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSgtIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1448 EIMIMYariwgiSEHQIqpyvkkyLNSLDLESHANSListySEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLW 1527
Cdd:cd03369 103 DPFDEY------SDEEI-------YGALRVSEGGLNL----SQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQ 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 1528 DTvikIRE--SGKAIIITSHSMEECeALCTRLSIMVRGRLTCLGSP 1571
Cdd:cd03369 166 KT---IREefTNSTILTIAHRLRTI-IDYDKILVMDAGEVKEYDHP 207
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1356-1574 |
1.41e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 57.80 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-KNIVKVRSKIGYC 1434
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQF-DALLEYMTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDE 1513
Cdd:PRK13642 87 FQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1514 PSTGMDPRARRLLWDTVIKIRESGKAIIIT-SHSMEECeALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK13642 167 STSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1353-1579 |
1.70e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.48 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1353 PVL-IKELTKIYFKSPlilAVKNISLAIQERACFGLLGFNGAGKTTTFQILT--GENIP---TAGDVFIDG---ISLTKN 1423
Cdd:PRK14239 4 PILqVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNGhniYSPRTD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1424 IVKVRSKIGYCPQ----FDalleyMTGWEIMIMYARIWGISEHQI-QPYVKKYL------NSLDLESHANSLisTYSEGN 1492
Cdd:PRK14239 81 TVDLRKEIGMVFQqpnpFP-----MSIYENVVYGLRLKGIKDKQVlDEAVEKSLkgasiwDEVKDRLHDSAL--GLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1493 KRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITsHSMEECEALCTRLSIMVRGRLTCLGS-- 1570
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYNDtk 232
|
250 260
....*....|....*....|
gi 46358378 1571 -----PQ------YLKNKFG 1579
Cdd:PRK14239 233 qmfmnPKhketedYISGKFG 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
520-731 |
2.16e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 520 AGIQIKHLHKVFQKNNTtkvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQhmdqvrns 599
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE-------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 lgLCPQ--------QNL-LFDHLTVSEHLYFYCRIKGVPQ---KMYLEETNNMLsafNLMEKCDAFSKSLSGGMKRKLAI 667
Cdd:PRK11650 71 --LEPAdrdiamvfQNYaLYPHMSVRENMAYGLKIRGMPKaeiEERVAEAARIL---ELEPLLDRKPRELSGGQRQRVAM 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 668 IIALIGGSKVAILDEPTSGMDPASR---RStwDILQTYKQ-NRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAKLRvqmRL--EIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
538-733 |
3.23e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 58.32 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGlYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFdHLTVS 616
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRElDPESWRKHLSWVGQNPQLP-HGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 617 EHLYFycrikGVPQkMYLEETNNMLSAFNLMEKCDAFSK-----------SLSGGMKRKLAIIIALIGGSKVAILDEPTS 685
Cdd:PRK11174 441 DNVLL-----GNPD-ASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTA 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 46358378 686 GMDPASRRSTWDILQTYKQNRTILLTTHYMDE-ADVlgDRIAIMVRGTL 733
Cdd:PRK11174 515 SLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
543-737 |
3.75e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 57.54 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 543 DLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI-SQHMDQVRNSLGLCPQQNLL---FDHLTVSE- 617
Cdd:PRK09536 21 GVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLsfeFDVRQVVEm 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 ----HLYFYCRI-----KGVPQKMYLEETnnmlSAFnlmekCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:PRK09536 101 grtpHRSRFDTWtetdrAAVERAMERTGV----AQF-----ADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 689 PASRRSTWDILQTY-KQNRTILLTTHYMDEADVLGDRIAIMVRGTLRCCG 737
Cdd:PRK09536 172 INHQVRTLELVRRLvDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1356-1565 |
3.89e-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: 57.91 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGEnIPT--AGDVFIDGISL-TKNIVK-VRSKI 1431
Cdd:TIGR02633 260 ARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGA-YPGkfEGNVFINGKPVdIRNPAQaIRAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQ---FDALLEYM-TGWEIMIM----YARIWGISEHQIQPYVKKYLNSLDLESHANSL-ISTYSEGNKRRLSTAIAT 1502
Cdd:TIGR02633 339 AMVPEdrkRHGIVPILgVGKNITLSvlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKML 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 1503 MGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:TIGR02633 419 LTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
522-731 |
3.95e-08 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 58.16 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKS-TTLSILsGLYPP----TSGEAYVHGEDISQ----H 592
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGlserE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 593 MDQVR-NSLGLCPQQ-----NLLFdhlTVSEHLYFYCRI-KGVPQKMYLEETNNMLSAFNLME---KCDAFSKSLSGGMK 662
Cdd:COG4172 86 LRRIRgNRIAMIFQEpmtslNPLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46358378 663 RKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHymDEADV--LGDRIAIMVRG 731
Cdd:COG4172 163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELgmALLLITH--DLGVVrrFADRVAVMRQG 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
545-731 |
4.04e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 4.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 545 SLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE--DISQHMDQVRNSLGLCPQ---QNLLFDHLTVSEHL 619
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 YFYCRIKGVPQKMYLE---ETNNmlsafnlmekCDAFSKS--------------LSGGMKRKlaIIIA--LIGGSKVAIL 680
Cdd:PRK11288 353 NISARRHHLRAGCLINnrwEAEN----------ADRFIRSlniktpsreqlimnLSGGNQQK--AILGrwLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 681 DEPTSGMDPASRRSTWDIL-QTYKQNRTILLTTHymDEADVLG--DRIAIMVRG 731
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSS--DLPEVLGvaDRIVVMREG 472
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1345-1519 |
4.44e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 4.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1345 QPEKFLNCPVLIKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVfidgiSLTKNi 1424
Cdd:PRK15064 311 QDKKLHRNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----KWSEN- 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1425 vkvrSKIGYCPQ-----FD---ALLEYMTGWeimimyaRIWGISEHQIQPYVKKYLNSLDlesHANSLISTYSEGNKRRL 1496
Cdd:PRK15064 382 ----ANIGYYAQdhaydFEndlTLFDWMSQW-------RQEGDDEQAVRGTLGRLLFSQD---DIKKSVKVLSGGEKGRM 447
|
170 180
....*....|....*....|...
gi 46358378 1497 STAIATMGKPSVIFLDEPSTGMD 1519
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
542-713 |
4.68e-08 |
|
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: 57.91 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 542 KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDI---SQHmdQVRNSLGLCPQQNLLFDhltvsEH 618
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIrdvTQA--SLRAAIGIVPQDTVLFN-----DT 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 619 LYF---YCRIkGVPQkmylEETNNMLSAFNLmekcDAFSKS---------------LSGGMKRKLAIIIALIGGSKVAIL 680
Cdd:COG5265 448 IAYniaYGRP-DASE----EEVEAAARAAQI----HDFIESlpdgydtrvgerglkLSGGEKQRVAIARTLLKNPPILIF 518
|
170 180 190
....*....|....*....|....*....|...
gi 46358378 681 DEPTSGMDPASRRSTWDILQTYKQNRTILLTTH 713
Cdd:COG5265 519 DEATSALDSRTERAIQAALREVARGRTTLVIAH 551
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
522-724 |
5.14e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 5.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHkvFQKNNTTKVAI-KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHG----EDISqhMDQV 596
Cdd:PTZ00265 383 IQFKNVR--FHYDTRKDVEIyKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDIN--LKWW 458
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 RNSLGLCPQQNLLFDH------------LTVSEHLYFY-----------------CRIKG------VPQKMYLEETNNML 641
Cdd:PTZ00265 459 RSKIGVVSQDPLLFSNsiknnikyslysLKDLEALSNYynedgndsqenknkrnsCRAKCagdlndMSNTTDSNELIEMR 538
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 642 SAFNLMEKCDAFSKS--------------------------LSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRST 695
Cdd:PTZ00265 539 KNYQTIKDSEVVDVSkkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
250 260 270
....*....|....*....|....*....|....*..
gi 46358378 696 WDILQTYK--QNRTILLTTH------YMDEADVLGDR 724
Cdd:PTZ00265 619 QKTINNLKgnENRITIIIAHrlstirYANTIFVLSNR 655
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1386-1574 |
5.48e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 55.95 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1386 GLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVKVRS-KIGYCPQFDALLEYMTGWEIMIMYARIW------- 1457
Cdd:PRK10575 41 GLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFArKVAYLPQQLPAAEGMTVRELVAIGRYPWhgalgrf 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1458 GISEHQiqpYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKI-RES 1536
Cdd:PRK10575 121 GAADRE---KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQER 197
|
170 180 190
....*....|....*....|....*....|....*...
gi 46358378 1537 GKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK10575 198 GLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
523-733 |
6.50e-08 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 57.34 E-value: 6.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 523 QIKHLHkvfQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISqHMD--QV---- 596
Cdd:COG3845 259 EVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDIT-GLSprERrrlg 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 597 -------RNSLGLCP----QQNLLFDHLTVSEhlyfYCRiKGVPQKMYLEE-TNNMLSAFNLmeKC---DAFSKSLSGGM 661
Cdd:COG3845 335 vayipedRLGRGLVPdmsvAENLILGRYRRPP----FSR-GGFLDRKAIRAfAEELIEEFDV--RTpgpDTPARSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 662 KRKLaiIIA--LIGGSKVAILDEPTSGMDPASRRSTWD-ILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRGTL 733
Cdd:COG3845 408 QQKV--ILAreLSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
508-733 |
6.91e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.41 E-value: 6.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 508 SKYFEAEPTDLTAGIqikhlhKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE 587
Cdd:PRK10789 304 SEPVPEGRGELDVNI------RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 588 DISQ-HMDQVRNSLGLCPQQNLLFDHlTVSEHLYFYC------------RIKGV-------PQKMYLE--ETNNMlsafn 645
Cdd:PRK10789 378 PLTKlQLDSWRSRLAVVSQTPFLFSD-TVANNIALGRpdatqqeiehvaRLASVhddilrlPQGYDTEvgERGVM----- 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 646 lmekcdafsksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNRTILLTTHYMdEADVLGDRI 725
Cdd:PRK10789 452 -----------LSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEI 519
|
....*...
gi 46358378 726 AIMVRGTL 733
Cdd:PRK10789 520 LVMQHGHI 527
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1372-1566 |
7.73e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSK------IGYCPQ---FDALLE 1442
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG----HEVVTRSPQdglangIVYISEdrkRDGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 YMTGWEIMIMYA-----RIWGISEHQI-QPYVKKYLNSLDLES-HANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:PRK10762 344 GMSVKENMSLTAlryfsRAGGSLKHADeQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1516 TGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK10762 424 RGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRIS 474
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1371-1564 |
7.80e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 56.86 E-value: 7.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGEnIPTA---GDVFIDGISLTKNIVK--VRSKIGYCPQFDALLEYMT 1445
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNIRdtERAGIAIIHQELALVKELS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1446 -------GWEIM--------IMYARiwgisehqiqpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:PRK13549 99 vleniflGNEITpggimdydAMYLR------------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:PRK13549 167 LDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
540-731 |
9.67e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDIS----------------QHMDQVRNS---- 599
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealengismvhQELNLVLQRsvmd 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 ---LGLCPQQNLLFDHltvsehlyfycrikgvpQKMYlEETNNMLSAFNLmeKCDAFSK--SLSGGMKRKLAIIIALIGG 674
Cdd:PRK10982 93 nmwLGRYPTKGMFVDQ-----------------DKMY-RDTKAIFDELDI--DIDPRAKvaTLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 675 SKVAILDEPTSGMDPASRRSTWDILQTYKQNRT-ILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1370-1571 |
1.20e-07 |
|
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: 54.42 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1370 LAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQ----F------- 1437
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQdpvlFsgtirsn 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1438 -DALLEYmTGWEImimyariWGISEH-QIQPYVKKYLNSLDLESHANSliSTYSEGNKRRLSTAIATMGKPSVIFLDEPS 1515
Cdd:cd03244 98 lDPFGEY-SDEEL-------WQALERvGLKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1516 TGMDPRARRLLWDTvikIRE--SGKAIIITSHsmeecealctRLS-------IMV--RGRLTCLGSP 1571
Cdd:cd03244 168 ASVDPETDALIQKT---IREafKDCTVLTIAH----------RLDtiidsdrILVldKGRVVEFDSP 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1358-1587 |
1.23e-07 |
|
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: 54.41 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1358 ELTKIYFK----SPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL-TKNIVKVRSKIG 1432
Cdd:cd03252 2 TFEHVRFRykpdGPVIL--DNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1433 YCPQFDALLEYMTGWEIMIMYAriwGISEHQIQpYVKKYLNS----LDLESHANSLI----STYSEGNKRRLSTAIATMG 1504
Cdd:cd03252 80 VVLQENVLFNRSIRDNIALADP---GMSMERVI-EAAKLAGAhdfiSELPEGYDTIVgeqgAGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1505 KPSVIFLDEPSTGMDPRARRLLWDTVIKIReSGKAIIITSHSMEECEAlCTRLSIMVRGRLTCLGSPQYLKNKFGNIYIL 1584
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
...
gi 46358378 1585 KAK 1587
Cdd:cd03252 234 YQL 236
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
550-728 |
1.23e-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: 56.33 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 550 EGQVTVLLGHNGAGKSTTLSILSGLYPPTSGE-----------AYVHGEDISQHMDQVRN---SLGLCPQQ-NLLFDHL- 613
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevlKRFRGTELQDYFKKLANgeiKVAHKPQYvDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 -TVSEHLyfycriKGVPQKMYLEETNNMLSAFNLMEKcDAfsKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASR 692
Cdd:COG1245 178 gTVRELL------EKVDERGKLDELAEKLGLENILDR-DI--SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR 248
|
170 180 190
....*....|....*....|....*....|....*....
gi 46358378 693 RSTWDILQTY-KQNRTILLTTHymDEA--DVLGDRIAIM 728
Cdd:COG1245 249 LNVARLIRELaEEGKYVLVVEH--DLAilDYLADYVHIL 285
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
553-738 |
1.28e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 55.65 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 553 VTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQHMDQV------RNsLGLCPQQNLLFDHLTVSEHLYFYCRIK 626
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppekRR-IGYVFQDARLFPHYKVRGNLRYGMAKS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 627 GVPQKMYLEEtnnMLSAFNLMekcDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ-- 704
Cdd:PRK11144 105 MVAQFDKIVA---LLGIEPLL---DRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARei 178
|
170 180 190
....*....|....*....|....*....|....
gi 46358378 705 NRTILLTTHYMDEADVLGDRIAIMVRGTLRCCGS 738
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
522-767 |
1.38e-07 |
|
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: 56.35 E-value: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGL--YPPTSGEAYVH-------------- 585
Cdd:TIGR03269 1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 586 ----------GEDISQHMD----------QVRNSLGLCPQQNL-LFDHLTVSEHLYFYCRIKGVPQKMYLEETNNMLSAF 644
Cdd:TIGR03269 77 kvgepcpvcgGTLEPEEVDfwnlsdklrrRIRKRIAIMLQRTFaLYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 645 NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQ--TYKQNRTILLTTHYMDEADVLG 722
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeaVKASGISMVLTSHWPEVIEDLS 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 723 DRIAIMVRGTLRCCG-----SSVFLKRLYGV-GSHLVMVKEPYCDIAEISK 767
Cdd:TIGR03269 237 DKAIWLENGEIKEEGtpdevVAVFMEGVSEVeKECEVEVGEPIIKVRNVSK 287
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
537-729 |
1.50e-07 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 53.81 E-value: 1.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 537 TKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP--PTSGEAYVHGEDISQhmdqvrnslglcpqqnllfdHLT 614
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQFGR--------------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VSEHLYfycRIKGVPQKMYLeetnnmLSAFNLmekCDAFS-----KSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP 689
Cdd:COG2401 102 LIDAIG---RKGDFKDAVEL------LNAVGL---SDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDR 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 46358378 690 ASRRSTWDILQ--TYKQNRTILLTTHYMDEADVLGDRIAIMV 729
Cdd:COG2401 170 QTAKRVARNLQklARRAGITLVVATHHYDVIDDLQPDLLIFV 211
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
524-713 |
1.68e-07 |
|
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: 56.10 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 524 IKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVhGEDIsqhmdqvrnSLGLC 603
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-QPGI---------KVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 PQQNLLFDHLTVSEHLYFYCR-IKGVPQKM------YLEETNNM----------------LSAFNL-------ME--KC- 650
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEGVAeIKDALDRFneisakYAEPDADFdklaaeqaelqeiidaADAWDLdsqleiaMDalRCp 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 651 --DAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASrrSTW--DILQTYKQnrTILLTTH 713
Cdd:TIGR03719 154 pwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES--VAWleRHLQEYPG--TVVAVTH 216
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1354-1569 |
2.09e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 54.15 E-value: 2.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1354 VLIKELtKIYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTG--ENIPTA---GDVFIDGISLTK-NIVKV 1427
Cdd:PRK14247 4 IEIRDL-KVSFGQVEVL--DGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEArvsGEVYLDGQDIFKmDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1428 RSKIGYCPQFDALLEYMTGWEIMIMYARIWGI--SEHQIQPYVKKYLNSLDL----ESHANSLISTYSEGNKRRLSTAIA 1501
Cdd:PRK14247 81 RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1502 TMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESgKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
531-688 |
2.11e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 54.71 E-value: 2.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 531 FQKNNTTKvAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVRNSLGLCPQQ 606
Cdd:PRK15079 28 WQPPKTLK-AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddEWRAVRSDIQMIFQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 607 NL--LFDHLTVSEhlyfycrIKGVPQKMY---------LEETNNMLSAFNLMEK-CDAFSKSLSGGMKRKLAIIIALIGG 674
Cdd:PRK15079 107 PLasLNPRMTIGE-------IIAEPLRTYhpklsrqevKDRVKAMMLKVGLLPNlINRYPHEFSGGQCQRIGIARALILE 179
|
170
....*....|....
gi 46358378 675 SKVAILDEPTSGMD 688
Cdd:PRK15079 180 PKLIICDEPVSALD 193
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
540-694 |
2.37e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 2.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGE-----DISQHMDQVR-----NSLGLCPQQNll 609
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIRmifqdPSTSLNPRQR-- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 610 fdhltVSEHLYFYCRIKGVPQKMYLEE-TNNMLSAFNLM-EKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:PRK15112 106 -----ISQILDFPLRLNTDLEPEQREKqIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASL 180
|
....*..
gi 46358378 688 DpASRRS 694
Cdd:PRK15112 181 D-MSMRS 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
544-690 |
2.74e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.78 E-value: 2.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYpPTSGEAYVHGEDISQ--HMDQVRNSLGLCPQQNLLFDhLTVSEHLYF 621
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsAAELARHRAYLSQQQTPPFA-MPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 622 YcrikgVPQKMYLEETNNMLS----AFNLMEKCDAFSKSLSGG--MKRKLAIII-----ALIGGSKVAILDEPTSGMDPA 690
Cdd:PRK03695 93 H-----QPDKTRTEAVASALNevaeALGLDDKLGRSVNQLSGGewQRVRLAAVVlqvwpDINPAGQLLLLDEPMNSLDVA 167
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1372-1574 |
2.88e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 53.95 E-value: 2.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAG-----DVFIDGISL--TKNIVKVRSKIGycpqfdALLEYM 1444
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRRVG------MLFQRP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYARIWGISEHQIQP------YVKKYLNSLDLESHANSLIST----YSEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:PRK14271 111 NPFPMSIMDNVLAGVRAHKLVPrkefrgVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEP 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1515 STGMDPRARRLLWDTVIKIRESGKAIIITsHSMEECEALCTRLSIMVRGRLTCLGSPQYL 1574
Cdd:PRK14271 191 TSALDPTTTEKIEEFIRSLADRLTVIIVT-HNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
538-713 |
3.35e-07 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 53.54 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ----HMDQVRNSLGLCPQqnllfDHL 613
Cdd:PRK10419 25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMVFQ-----DSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 614 TVSEHLYFYCRIKGVPQKMYL--------EETNNMLSAFNL-MEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPT 684
Cdd:PRK10419 100 SAVNPRKTVREIIREPLRHLLsldkaerlARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|.
gi 46358378 685 SGMDPASRRSTWDILQTYKQNRTI--LLTTH 713
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTacLFITH 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1373-1545 |
3.42e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.12 E-value: 3.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1373 KNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKV---------RSKIGYCPQFDALLEY 1443
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAG----QDVATLdadalaqlrREHFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MTGW---EIMIMYAriwGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDP 1520
Cdd:PRK10535 101 LTAAqnvEVPAVYA---GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDS 177
|
170 180
....*....|....*....|....*
gi 46358378 1521 RARRLLWDTVIKIRESGKAIIITSH 1545
Cdd:PRK10535 178 HSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1356-1545 |
3.67e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIY------FKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLT-------- 1421
Cdd:PRK15112 7 VRNLSKTFryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysyrs 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1422 ----------KNIVKVRSKIGYCpqFDALLEYMTGWEIMIMYARIwgisehqIQPYVKKYLnsldLESHANSLISTYSEG 1491
Cdd:PRK15112 87 qrirmifqdpSTSLNPRQRISQI--LDFPLRLNTDLEPEQREKQI-------IETLRQVGL----LPDHASYYPHMLAPG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 46358378 1492 NKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRES-GKAII-ITSH 1545
Cdd:PRK15112 154 QKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIyVTQH 209
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1372-1577 |
4.47e-07 |
|
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: 53.32 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTgENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQ--------FDALLE 1442
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFL-RLLNTEGDIQIDGVSWNSvPLQKWRKAFGVIPQkvfifsgtFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 YMTGWEimimYARIWGISEH-QIQPYVKKYLNSLDLESHANSLIstYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPR 1521
Cdd:cd03289 99 PYGKWS----DEEIWKVAEEvGLKSVIEQFPGQLDFVLVDGGCV--LSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPI 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 46358378 1522 ARRLLWDTvIKIRESGKAIIITSHSMeecEAL--CTRLSIMVRGRLTCLGSPQYLKNK 1577
Cdd:cd03289 173 TYQVIRKT-LKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
522-688 |
5.06e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.35 E-value: 5.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKnnttKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVhGE--DISqHMDQVRNS 599
Cdd:PRK11819 325 IEAENLSKSFGD----RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GEtvKLA-YVDQSRDA 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGlcPQQNLL------FDHLTVSEHlyfycrikGVPQKMYleetnnmLSAFNLM----EKcdaFSKSLSGGMKRKLAIII 669
Cdd:PRK11819 399 LD--PNKTVWeeisggLDIIKVGNR--------EIPSRAY-------VGRFNFKggdqQK---KVGVLSGGERNRLHLAK 458
|
170
....*....|....*....
gi 46358378 670 ALIGGSKVAILDEPTSGMD 688
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1363-1545 |
5.13e-07 |
|
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: 52.54 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1363 YFKSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQfDALL 1441
Cdd:cd03249 10 YPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQ-EPVL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1442 EYMTgweIM--IMYARIWGISEHQIQpyVKKYLNSLD----LESHANSLI----STYSEGNKRRLSTAIATMGKPSVIFL 1511
Cdd:cd03249 89 FDGT---IAenIRYGKPDATDEEVEE--AAKKANIHDfimsLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190
....*....|....*....|....*....|....
gi 46358378 1512 DEPSTGMDPRARRLLWDTVIKIREsGKAIIITSH 1545
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAMK-GRTTIVIAH 196
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1387-1546 |
5.19e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 52.18 E-value: 5.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTknIVKVRSKIGYCPQFDALLEYMTGWEIMIMYARIWGISEHQIQP 1466
Cdd:PRK13539 33 LTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGHRNAMKPALTVAENLEFWAAFLGGEELDIAA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1467 YvkkyLNSLDLeSHANSLISTY-SEGNKRRLSTA--IATmGKPsVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIIT 1543
Cdd:PRK13539 111 A----LEAVGL-APLAHLPFGYlSAGQKRRVALArlLVS-NRP-IWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183
|
...
gi 46358378 1544 SHS 1546
Cdd:PRK13539 184 THI 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1375-1566 |
5.46e-07 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 54.15 E-value: 5.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1375 ISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDG--ISLTKNIVKVRSKIGYCPQ---FDALLEYMTGWEI 1449
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYAR----IWG--ISEHQIQPYVKKYLNSLDLES-HANSLISTYSEGNK------RRLSTAIatmgkpSVIFLDEPST 1516
Cdd:PRK11288 352 INISARrhhlRAGclINNRWEAENADRFIRSLNIKTpSREQLIMNLSGGNQqkailgRWLSEDM------KVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1330-1545 |
6.22e-07 |
|
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: 54.17 E-value: 6.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1330 SEDNDVENERREILYQPEKFLNCPVL-IKELTKIYFKSPLIlavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIP 1408
Cdd:TIGR03719 298 SQEFQKRNETAEIYIPPGPRLGDKVIeAENLTKAFGDKLLI---DDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQP 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1409 TAGDVFIdGISLtknivkvrsKIGYCPQF-DALLEYMTGWEIMIMYARIWGISEHQIQPyvKKYLNSLDLE-SHANSLIS 1486
Cdd:TIGR03719 375 DSGTIEI-GETV---------KLAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPS--RAYVGRFNFKgSDQQKKVG 442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1487 TYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIreSGKAIIItSH 1545
Cdd:TIGR03719 443 QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVI-SH 498
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1387-1545 |
6.28e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.12 E-value: 6.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTG--ENIPTAGDVFIDGISLTKNIVKvrsKIGYCPQFDALLEYMTGWEIMIMYARIW---GISE 1461
Cdd:PLN03211 99 VLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILK---RTGFVTQDDILYPHLTVRETLVFCSLLRlpkSLTK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1462 HQIQPYVKKYLNSLDLESH-----ANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRES 1536
Cdd:PLN03211 176 QEKILVAESVISELGLTKCentiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK 255
|
....*....
gi 46358378 1537 GKAIIITSH 1545
Cdd:PLN03211 256 GKTIVTSMH 264
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
550-728 |
6.73e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 6.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 550 EGQVTVLLGHNGAGKSTTLSILSGLYPPTSG------------------EAYVHGEDIS----------QHMDQVRNSL- 600
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGdyeeepswdevlkrfrgtELQNYFKKLYngeikvvhkpQYVDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 601 GlcpqqnllfdhlTVSEHLyfycriKGVPQKMYLEETNNMLSAFNLMEKcDAfsKSLSGGMKRKLAIIIALIGGSKVAIL 680
Cdd:PRK13409 178 G------------KVRELL------KKVDERGKLDEVVERLGLENILDR-DI--SELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 681 DEPTSGMDPASRRSTWDILQTYKQNRTILLTTHymDEA--DVLGDRIAIM 728
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGKYVLVVEH--DLAvlDYLADNVHIA 284
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
498-734 |
2.46e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 498 EITQFYERveskyfeaEPTDLTAGI-QIKHLhKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP 576
Cdd:PRK13549 243 ELTALYPR--------EPHTIGEVIlEVRNL-TAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 577 -PTSGEAYVHGE--DISQHMDQVRNSLGLCP--------------QQNLLfdhLTVSEHLYFYCRI-KGVPQKMYLEETN 638
Cdd:PRK13549 314 gRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmgvGKNIT---LAALDRFTGGSRIdDAAELKTILESIQ 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 639 NM-LSAFNLMEKCdafsKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWD-ILQTYKQNRTILLTTHYMD 716
Cdd:PRK13549 391 RLkVKTASPELAI----ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKlINQLVQQGVAIIVISSELP 466
|
250 260
....*....|....*....|
gi 46358378 717 EadVLG--DRIAIMVRGTLR 734
Cdd:PRK13549 467 E--VLGlsDRVLVMHEGKLK 484
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1373-1572 |
2.70e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1373 KNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTKNIVK-VRSKIGYCPQfdallEYMTGWEIMI 1451
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQ-----NATTPGDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1452 MYARIWGISEHQI---------QPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:PRK10253 99 QELVARGRYPHQPlftrwrkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISH 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1523 RRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSPQ 1572
Cdd:PRK10253 179 QIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPK 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1374-1545 |
4.11e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1374 NISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltKNIVKVRSK-------IGYCPQFDALLeymTG 1446
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG----EPIRRQRDEyhqdllyLGHQPGIKTEL---TA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 WEIMIMYARIWG-ISEHQIQpyvkKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRL 1525
Cdd:PRK13538 92 LENLRFYQRLHGpGDDEALW----EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180
....*....|....*....|
gi 46358378 1526 LWDTVIKIRESGKAIIITSH 1545
Cdd:PRK13538 168 LEALLAQHAEQGGMVILTTH 187
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1485-1548 |
4.61e-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: 4.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1485 ISTYSEGNKR--RLSTAIA-TMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSME 1548
Cdd:pfam13304 234 AFELSDGTKRllALLAALLsALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
524-713 |
5.28e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.27 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 524 IKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAyVHGEDIsqhmdqvrnSLGLC 603
Cdd:PRK11819 6 IYTMNRVSKVVPPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA-RPAPGI---------KVGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 604 PQQNLLFDHLTVSEHLyfycrIKGVPQKMY----LEETNNMLSA----FN-LMEK------------------------- 649
Cdd:PRK11819 76 PQEPQLDPEKTVRENV-----EEGVAEVKAaldrFNEIYAAYAEpdadFDaLAAEqgelqeiidaadawdldsqleiamd 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 650 ---C---DAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASrrSTW--DILQTYKQnrTILLTTH 713
Cdd:PRK11819 151 alrCppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES--VAWleQFLHDYPG--TVVAVTH 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1371-1542 |
6.05e-06 |
|
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: 49.54 E-value: 6.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISL-TKNIVKVRSKIGYCPQfDALLEYMTGWEi 1449
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrDYTLASLRRQIGLVSQ-DVFLFNDTVAE- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1450 MIMYARIwGISEHQIQPYVKKylnsldleSHANSLI---------------STYSEGNKRRLSTAIATMGKPSVIFLDEP 1514
Cdd:cd03251 95 NIAYGRP-GATREEVEEAARA--------ANAHEFImelpegydtvigergVKLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180
....*....|....*....|....*...
gi 46358378 1515 STGMDPRARRLLWDTVIKIRESGKAIII 1542
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNRTTFVI 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
541-713 |
9.04e-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: 50.68 E-value: 9.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYpPTSGEAYVHGEDI-SQHMDQVRNSLGLCPQQNLLFDHlTVSEHL 619
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWnSVTLQTWRKAFGVIPQKVFIFSG-TFRKNL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 YFYCR---------IKGVPQKMYLEETNNMLSaFNLMEKcdafSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPA 690
Cdd:TIGR01271 1313 DPYEQwsdeeiwkvAEEVGLKSVIEQFPDKLD-FVLVDG----GYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180
....*....|....*....|....*..
gi 46358378 691 srrsTWDIL-QTYKQ---NRTILLTTH 713
Cdd:TIGR01271 1388 ----TLQIIrKTLKQsfsNCTVILSEH 1410
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1372-1566 |
1.03e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGEnIPTA--GDVFIDGISLTKN---------IVKV---RSKIGYCPQF 1437
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGA-YPGRweGEIFIDGKPVKIRnpqqaiaqgIAMVpedRKRDGIVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1438 D-------ALLEYMTGWEImimyariwgISEHQIQPYVKKYLNSLDLE-SHANSLISTYSEGNKRRLSTAIATMGKPSVI 1509
Cdd:PRK13549 357 GvgknitlAALDRFTGGSR---------IDDAAELKTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1510 FLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK13549 428 ILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1372-1551 |
1.23e-05 |
|
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: 50.29 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTgENIPTAGDVFIDGISLTK-NIVKVRSKIGYCPQ--------FDALLE 1442
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSvTLQTWRKAFGVIPQkvfifsgtFRKNLD 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1443 YMTGWEimimYARIWGISEH-QIQPYVKKYLNSLDLESHANSLIstYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPR 1521
Cdd:TIGR01271 1314 PYEQWS----DEEIWKVAEEvGLKSVIEQFPDKLDFVLVDGGYV--LSNGHKQLMCLARSILSKAKILLLDEPSAHLDPV 1387
|
170 180 190
....*....|....*....|....*....|...
gi 46358378 1522 ARRLLWDTvIKIRESGKAIIITSHSME---ECE 1551
Cdd:TIGR01271 1388 TLQIIRKT-LKQSFSNCTVILSEHRVEallECQ 1419
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
652-740 |
1.43e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 652 AFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQNR--TILLTTHYMDEADVLGDRIAIMV 729
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQWADKINVLY 233
|
90
....*....|.
gi 46358378 730 rgtlrcCGSSV 740
Cdd:PRK15093 234 ------CGQTV 238
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1374-1566 |
1.50e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 1.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1374 NISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVfidgiSLTKNIvkvrsKIGYC--PQFdALLEY------MT 1445
Cdd:PRK15064 19 NISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV-----SLDPNE-----RLGKLrqDQF-AFEEFtvldtvIM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1446 G----WEIMIMYARIWGISEHQIQPYVK------KY--LNSLDLESHA--------------NSLISTYSEGNKRRLSTA 1499
Cdd:PRK15064 88 GhtelWEVKQERDRIYALPEMSEEDGMKvadlevKFaeMDGYTAEARAgelllgvgipeeqhYGLMSEVAPGWKLRVLLA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1500 IATMGKPSVIFLDEPSTGMDPRARRLLWDtVIKIRESgkAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDINTIRWLED-VLNERNS--TMIIISHDRHFLNSVCTHMADLDYGELR 231
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
538-739 |
1.59e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYvhgedisqhmdqVRNSLGLCPQQNLLFDhLTVSE 617
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW------------AERSIAYVPQQAWIMN-ATVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 618 HLYFY-----CRIKGVPQKMYLEETNNMLSAfNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDP-AS 691
Cdd:PTZ00243 740 NILFFdeedaARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVG 818
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 46358378 692 RRSTWDILQTYKQNRTILLTTHYMDEADvLGDRIAIMVRGTLRCCGSS 739
Cdd:PTZ00243 819 ERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS 865
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1365-1565 |
1.86e-05 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 48.14 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1365 KSPLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGISLTK-------------NIVKVRSKI 1431
Cdd:PRK10419 21 KHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiQMVFQDSIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1432 GYCPQFDalleymTGWEIMIMYARIWGISEHQIQPYVKKYLNSLDL-ESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:PRK10419 101 AVNPRKT------VREIIREPLRHLLSLDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1511 LDEPSTGMDprarRLLWDTVIKI-----RESGKAIIITSHSMEECEALCTRLSIMVRGRL 1565
Cdd:PRK10419 175 LDEAVSNLD----LVLQAGVIRLlkklqQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
540-731 |
2.17e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH--MDQVRNSLGLCPQQNL---LFDHLT 614
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaNEAINHGFALVTEERRstgIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 615 VsEHLYFYCRIKGVPQKMYLEETNNMLS----AFNLME-KCDAFSK---SLSGGMKRKLAIIIALIGGSKVAILDEPTSG 686
Cdd:PRK10982 343 I-GFNSLISNIRNYKNKVGLLDNSRMKSdtqwVIDSMRvKTPGHRTqigSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 46358378 687 MDPASRRSTWD-ILQTYKQNRTILLTTHYMDEADVLGDRIAIMVRG 731
Cdd:PRK10982 422 IDVGAKFEIYQlIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
541-719 |
2.27e-05 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 47.33 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAY-----VHGEDISQHMDQVRNSLGLCPQQNLLFDhLTV 615
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnknESEPSFEATRSRNRYSVAYAAQKPWLLN-ATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLYFYC-----RIKGVPQKMYLEETNNMLSaFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM--- 687
Cdd:cd03290 96 EENITFGSpfnkqRYKAVTDACSLQPDIDLLP-FGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALdih 174
|
170 180 190
....*....|....*....|....*....|....*..
gi 46358378 688 --DPASRRSTWDILQTYKqnRTILLTTH---YMDEAD 719
Cdd:cd03290 175 lsDHLMQEGILKFLQDDK--RTLVLVTHklqYLPHAD 209
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1367-1564 |
2.41e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.96 E-value: 2.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1367 PLILAVKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFIDGisltknivkvrSKIGYCPQFDALLE--YM 1444
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG-----------KEIDFKSSKEALENgiSM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1445 TGWEIMIMYAR-----IW-------GISEHQIQPY--VKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIF 1510
Cdd:PRK10982 78 VHQELNLVLQRsvmdnMWlgryptkGMFVDQDKMYrdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLSIMVRGR 1564
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
551-779 |
3.02e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 3.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 551 GQVTVLLGHNGAGKSTTLSILSGlyPPTSGeaYVHGE-DIS---QHMDQVRNSLGLCPQQNLLFDHLTVSEHLYF----- 621
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEGDiRISgfpKKQETFARISGYCEQNDIHSPQVTVRESLIYsaflr 981
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 622 -------YCRIKGVPQKMYLEETNNMLSAFNLMEKCDAfsksLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPasrRS 694
Cdd:PLN03140 982 lpkevskEEKMMFVDEVMELVELDNLKDAIVGLPGVTG----LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA---RA 1054
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 695 TWDILQTYKQN----RTILLTTHyMDEADVLG--DRIAIMVRGtlrccGSSVFLKRLyGVGSHLVMvkEPYCDIAEISKL 768
Cdd:PLN03140 1055 AAIVMRTVRNTvdtgRTVVCTIH-QPSIDIFEafDELLLMKRG-----GQVIYSGPL-GRNSHKII--EYFEAIPGVPKI 1125
|
250
....*....|..
gi 46358378 769 IHSYVP-TATLE 779
Cdd:PLN03140 1126 KEKYNPaTWMLE 1137
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
536-734 |
3.65e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 3.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 536 TTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVhgedisqhmdqVRNSLGLCPQQNLLFDhLTV 615
Cdd:PLN03232 628 TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFN-ATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 616 SEHLYFYCRIKgvPQKMY-------LEETNNMLSAFNLMEKCDAfSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:PLN03232 696 RENILFGSDFE--SERYWraidvtaLQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 689 PASRRSTWD-ILQTYKQNRTILLTT---HYMDeadvLGDRIAIMVRGTLR 734
Cdd:PLN03232 773 AHVAHQVFDsCMKDELKGKTRVLVTnqlHFLP----LMDRIILVSEGMIK 818
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
526-753 |
5.08e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 5.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 526 HLHkVFQKNNttkVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPT--------SGEAYVHGEDISQ----HM 593
Cdd:PRK13547 6 HLH-VARRHR---AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAidapRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 594 DQVRNSLGLCPQQNLLF--DHLtVSEHLYFYCRIKGVPQKmyleETNNMLSAFNLMEKCDAFSK----SLSGG------M 661
Cdd:PRK13547 82 ARLRAVLPQAAQPAFAFsaREI-VLLGRYPHARRAGALTH----RDGEIAWQALALAGATALVGrdvtTLSGGelarvqF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 662 KRKLAIII---ALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ--NRTILLTTHYMDEADVLGDRIAIMVRGTLRCC 736
Cdd:PRK13547 157 ARVLAQLWpphDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250 260
....*....|....*....|...
gi 46358378 737 GS------SVFLKRLYGVGSHLV 753
Cdd:PRK13547 237 GApadvltPAHIARCYGFAVRLV 259
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
542-713 |
5.92e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 5.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 542 KDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYP--------------------------------------------- 576
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 577 ---------PTSGEAYVHGEDISQH-MDQVRNSLGLCPQQNLLFDhLTVSEHLYF------------YCRIKGVPQkmYL 634
Cdd:PTZ00265 1265 gsgedstvfKNSGKILLDGVDICDYnLKDLRNLFSIVSQEPMLFN-MSIYENIKFgkedatredvkrACKFAAIDE--FI 1341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 635 EETNNMLSAfnlmeKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPAS----RRSTWDILQtyKQNRTILL 710
Cdd:PTZ00265 1342 ESLPNKYDT-----NVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSekliEKTIVDIKD--KADKTIIT 1414
|
...
gi 46358378 711 TTH 713
Cdd:PTZ00265 1415 IAH 1417
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1356-1519 |
8.07e-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: 47.24 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1356 IKELTKIYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFI-DGIsltknivkvrsKIGYC 1434
Cdd:TIGR03719 7 MNRVSKVVPPKKEIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPqPGI-----------KVGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1435 PQ-----------------------------------------FDALLEYMTGWEIMIMYARIWGIsEHQiqpyvkkyln 1473
Cdd:TIGR03719 74 PQepqldptktvrenveegvaeikdaldrfneisakyaepdadFDKLAAEQAELQEIIDAADAWDL-DSQ---------- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1474 sldLESHANSL--------ISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:TIGR03719 143 ---LEIAMDALrcppwdadVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1372-1558 |
8.45e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.18 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGEN-----IPTAGDVFIDGISLTK---NIVKVRSKIGYC---PQFDAL 1440
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYErrvNLNRLRRQVSMVhpkPNLFPM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1441 LEY--------MTGW----------EIMIMYARIWGISEHQIQPyvkkylNSLDLeshanslistySEGNKRRLSTAIAT 1502
Cdd:PRK14258 103 SVYdnvaygvkIVGWrpkleiddivESALKDADLWDEIKHKIHK------SALDL-----------SGGQQQRLCIARAL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 1503 MGKPSVIFLDEPSTGMDPRARRLLWDTVIKIR-ESGKAIIITSHSMEEcealCTRLS 1558
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQ----VSRLS 218
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
653-723 |
9.76e-05 |
|
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: 44.66 E-value: 9.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 653 FSKSLSGGMKRK--LAIIIAL--IGGSKVAILDEPTSGMDPASRRS-TWDILQTYKQNRTILLTTHY---MDEADVLGD 723
Cdd:cd03227 74 TRLQLSGGEKELsaLALILALasLKPRPLYILDEIDRGLDPRDGQAlAEAILEHLVKGAQVIVITHLpelAELADKLIH 152
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
251-383 |
1.00e-04 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 45.19 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 251 YFYLFATTFIPLTVACTFFFNhyvLVWSIVWEKENRLKEYQLMIGLRNWMFWVAYFFTFLCLYFINIIVM--CMVLFVKI 328
Cdd:COG0842 1 YLAFLVPGLLAMSLLFTALML---TALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVllVALLFFGV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 329 EPAPIfqynDPTLVFIFLLFYAISSIFFSFMVSTLFNKVSLAMSLGSFLFFLTYF 383
Cdd:COG0842 78 PLRGL----SLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTF 128
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
540-587 |
1.01e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 46358378 540 AIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTS--GEAYVHGE 587
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGE 65
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
553-717 |
1.56e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.52 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 553 VTVLLGHNGAGKSTTLS----ILSGLYPPTS------------GE--AYVH-------GED--ISQHMDQVRNSLgLCPQ 605
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEalkyALTGELPPNSkggahdpklireGEvrAQVKlafenanGKKytITRSLAILENVI-FCHQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 606 ---QNLLFDHLtvsehlyfycrikgvpqkmyleetnnmlsafnlmekcdafsKSLSGGMKRKLAIIIAL------IGGSK 676
Cdd:cd03240 103 gesNWPLLDMR-----------------------------------------GRCSGGEKVLASLIIRLalaetfGSNCG 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 46358378 677 VAILDEPTSGMDPASRR-STWDILQTYKQ--NRTILLTTHymDE 717
Cdd:cd03240 142 ILALDEPTTNLDEENIEeSLAEIIEERKSqkNFQLIVITH--DE 183
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1479-1566 |
1.69e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.26 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1479 SHaNSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHSMEECEALCTRLS 1558
Cdd:PRK10982 384 GH-RTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRIL 462
|
....*...
gi 46358378 1559 IMVRGRLT 1566
Cdd:PRK10982 463 VMSNGLVA 470
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1371-1546 |
1.76e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTtfqiLTGENIPTAGDvfidgisltKNIVKVRSKIGYCPQfdalleymtgweIM 1450
Cdd:cd03238 10 NLQNLDVSIPLNVLVVVTGVSGSGKST----LVNEGLYASGK---------ARLISFLPKFSRNKL------------IF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 ImyariwgiseHQIQPYVKKYLNSLDLESHANSListySEGNKRRLSTA--IATMGKPSVIFLDEPSTGMDPRARRLLWD 1528
Cdd:cd03238 65 I----------DQLQFLIDVGLGYLTLGQKLSTL----SGGELQRVKLAseLFSEPPGTLFILDEPSTGLHQQDINQLLE 130
|
170
....*....|....*...
gi 46358378 1529 TVIKIRESGKAIIITSHS 1546
Cdd:cd03238 131 VIKGLIDLGNTVILIEHN 148
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1387-1519 |
2.12e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.26 E-value: 2.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1387 LLGFNGAGKTTTFQILTGE----NIPTAGDVFIDGISLTKNIVKVRSKIGYCPQFDALLEYMTGWEIMIMYA-------R 1455
Cdd:TIGR00956 92 VLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAArcktpqnR 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 1456 IWGISEhqiQPYVKK----YLNSLDLeSH------ANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMD 1519
Cdd:TIGR00956 172 PDGVSR---EEYAKHiadvYMATYGL-SHtrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1386-1545 |
2.47e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.57 E-value: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1386 GLLGFNGAGKTTTFQILTGENIPTAGDVF----IDGI--------------SLTKNIVKVRSKIGYcpqFDALLEYMTG- 1446
Cdd:PRK13409 103 GILGPNGIGKTTAVKILSGELIPNLGDYEeepsWDEVlkrfrgtelqnyfkKLYNGEIKVVHKPQY---VDLIPKVFKGk 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1447 -WEIMImyariwGISEHQIQPYVKKYLNsldLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRl 1525
Cdd:PRK13409 180 vRELLK------KVDERGKLDEVVERLG---LENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRL- 249
|
170 180
....*....|....*....|...
gi 46358378 1526 lwdTVIK-IRE--SGKAIIITSH 1545
Cdd:PRK13409 250 ---NVARlIRElaEGKYVLVVEH 269
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
541-738 |
2.69e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.09 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQ-HMDQVRNSLGLCPQQNLLFdhltvSEHL 619
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDPVLF-----SGSL 1376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 620 yfycRIKGVPQKMYLEET----------NNMLSAF--NLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGM 687
Cdd:TIGR00957 1377 ----RMNLDPFSQYSDEEvwwalelahlKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 688 DPASRRSTWDILQTYKQNRTILLTTH----YMDEAdvlgdRIAIMVRGTLRCCGS 738
Cdd:TIGR00957 1453 DLETDNLIQSTIRTQFEDCTVLTIAHrlntIMDYT-----RVIVLDKGEVAEFGA 1502
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1373-1578 |
2.83e-04 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 45.02 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1373 KNISLAIQERACFGLLGFNGAGKTTTFQILTG-ENIpTAGDVFIDGISLTKNIVKVRSkIGYCPQFDALLEYMTGWEIMI 1451
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGlEDI-TSGDLFIGEKRMNDVPPAERG-VGMVFQSYALYPHLSVAENMS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1452 MYARIWGISEHQIQPYVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWDTVI 1531
Cdd:PRK11000 98 FGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEIS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1532 KI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLGSP----QYLKNKF 1578
Cdd:PRK11000 178 RLhKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPlelyHYPANRF 229
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
538-688 |
3.11e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 538 KVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGE-AYVHGedisqhmdqVRnsLGLCPQQNLLFDHLTVS 616
Cdd:PRK10636 325 RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKG---------IK--LGYFAQHQLEFLRADES 393
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 46358378 617 --EHLyfyCRIkgVPQKMYlEETNNMLSAFNLM-EKCDAFSKSLSGGMKRKLaiIIALIGGSK--VAILDEPTSGMD 688
Cdd:PRK10636 394 plQHL---ARL--APQELE-QKLRDYLGGFGFQgDKVTEETRRFSGGEKARL--VLALIVWQRpnLLLLDEPTNHLD 462
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1386-1545 |
3.45e-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: 45.16 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1386 GLLGFNGAGKTTTFQILTGENIPTAGDV-----------FIDGISLTKNIVKVRS---KIGYCPQF-DALLEYMTG--WE 1448
Cdd:COG1245 103 GILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQDYFKKLANgeiKVAHKPQYvDLIPKVFKGtvRE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1449 IMImyariwGISEHQIqpyVKKYLNSLDLESHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRARRLLWD 1528
Cdd:COG1245 183 LLE------KVDERGK---LDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVAR 253
|
170
....*....|....*..
gi 46358378 1529 TVIKIRESGKAIIITSH 1545
Cdd:COG1245 254 LIRELAEEGKYVLVVEH 270
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
522-714 |
4.30e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.01 E-value: 4.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 522 IQIKHLHKVFQKNNTtkvaIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGL--YPPTSGEAYVHGEDIsqhmdqvrns 599
Cdd:PRK09580 2 LSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL---------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 600 LGLCPQQNllfdhltVSEHLY----FYCRIKGVPQKMYLEETNNMLSAFNLMEKCDAF--------------------SK 655
Cdd:PRK09580 68 LELSPEDR-------AGEGIFmafqYPVEIPGVSNQFFLQTALNAVRSYRGQEPLDRFdfqdlmeekiallkmpedllTR 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46358378 656 SL----SGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDILQTYKQ-NRTILLTTHY 714
Cdd:PRK09580 141 SVnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDgKRSFIIVTHY 204
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1369-1546 |
5.82e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 42.94 E-value: 5.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1369 ILAVKNISLAIQERACFGLL------------GFNGAGKTTTFQILTGENIPTAGDVFIDGISlTKNIVKvrSKIGYCPQ 1436
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLFDLSitflpsaityikGANGCGKSSLLRMIAGIMQPSSGNIYYKNCN-INNIAK--PYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1437 FDALLEYMTGWEIMIMYARIWGISEhqIQPYVKKYLNSLDLESHAnslISTYSEGNKRRLSTAIATMGKPSVIFLDEPST 1516
Cdd:PRK13541 78 NLGLKLEMTVFENLKFWSEIYNSAE--TLYAAIHYFKLHDLLDEK---CYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180 190
....*....|....*....|....*....|
gi 46358378 1517 GMDPRARRLLWDTVIKIRESGKAIIITSHS 1546
Cdd:PRK13541 153 NLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1371-1569 |
6.83e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.46 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1371 AVKNISLAIQERACFGLLGFNGAGKTTTFQIL-----TGENIPTAGDVFIDGISLTKnIVKVRSKIGYCPQ--FDALLEY 1443
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALlrlveSQGGEIIFNGQRIDTLSPGK-LQALRRDIQFIFQdpYASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1444 MT-GWEIMiMYARIWGISE-HQIQPYVKKYLNSLDLE-SHANSLISTYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDP 1520
Cdd:PRK10261 418 QTvGDSIM-EPLRVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 46358378 1521 RARRLLWDTVIKI-RESGKAIIITSHSMEECEALCTRLSIMVRGRLTCLG 1569
Cdd:PRK10261 497 SIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1511-1579 |
1.08e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46358378 1511 LDEPSTGMDPRARRLLWDTVIKIRES--GKAIIITSHSMEECEAlCTRLSIMVRGRLTCLGSPQYLKNKFG 1579
Cdd:NF033858 160 LDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
544-688 |
2.47e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 42.66 E-value: 2.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 544 LSLNLYEGQVTVLLGHNGAGKSTTLSILSGLYPPTSGEAYVHGEDISQH-MDQVRNSLGLCPQQNLLFDHlTV------- 615
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFgLTDLRRVLSIIPQSPVLFSG-TVrfnidpf 1333
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 46358378 616 SEHlyfycRIKGVPQKMYLEETNNML--SAFNLMEKCDAFSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMD 688
Cdd:PLN03232 1334 SEH-----NDADLWEALERAHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
541-741 |
2.51e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 41.91 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 541 IKDLSLNLyEGQVTVLLGHNGAGKSTTLSILSGLYPPTSG---------------------------------EAYVHGE 587
Cdd:COG3593 14 IKDLSIEL-SDDLTVLVGENNSGKSSILEALRLLLGPSSSrkfdeedfylgddpdlpeieieltfgsllsrllRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 588 D---ISQHMDQVRNSLglcpqqNLLFDHLT--VSEHLYFYCRIKGVPQKMYLEETNNMLSAFNL-MEKCDAFS-KSLSGG 660
Cdd:COG3593 93 DkeeLEEALEELNEEL------KEALKALNelLSEYLKELLDGLDLELELSLDELEDLLKSLSLrIEDGKELPlDRLGSG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 661 MKRklAIIIALI---------GGSKVAILDEPTSGMDPASRRSTWDILQTY-KQNRTILLTTH--YM-DEADVlgDRIAI 727
Cdd:COG3593 167 FQR--LILLALLsalaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELsEKPNQVIITTHspHLlSEVPL--ENIRR 242
|
250
....*....|....
gi 46358378 728 MVRGTLRCCGSSVF 741
Cdd:COG3593 243 LRRDSGGTTSTKLI 256
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1451-1545 |
2.84e-03 |
|
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: 40.42 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1451 IMYARIWGISEHQIQPYVKKY----LNSLDLESHANSLISTYSEGNKRRLSTA----IATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:cd03227 37 ILDAIGLALGGAQSATRRRSGvkagCIVAAVSAELIFTRLQLSGGEKELSALAlilaLASLKPRPLYILDEIDRGLDPRD 116
|
90 100
....*....|....*....|...
gi 46358378 1523 RRLLWDTVIKIRESGKAIIITSH 1545
Cdd:cd03227 117 GQALAEAILEHLVKGAQVIVITH 139
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1372-1544 |
4.28e-03 |
|
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: 41.00 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1372 VKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGdvfidgisltknIVKVRSKIGYCPQFDALleyMTGweiMI 1451
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG------------KIKHSGRISFSSQFSWI---MPG---TI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1452 MYARIWGIS--EHQIQPYVKKYLNSLDLESHA---NSLIS----TYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRA 1522
Cdd:cd03291 115 KENIIFGVSydEYRYKSVVKACQLEEDITKFPekdNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180
....*....|....*....|...
gi 46358378 1523 RRLLWDT-VIKIRESGKAIIITS 1544
Cdd:cd03291 195 EKEIFEScVCKLMANKTRILVTS 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1359-1436 |
5.15e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 5.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 46358378 1359 LTKIYFKSPLILavKNISLAIQERACFGLLGFNGAGKTTTFQILTGENIPTAGDVFI-DGIsltknivkvrsKIGYCPQ 1436
Cdd:PRK11819 12 VSKVVPPKKQIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI-----------KVGYLPQ 77
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
495-738 |
5.31e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 41.85 E-value: 5.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 495 QKLEITQFYERVESKYFEAEPTDLTAGIQIKHLHKVFQKNNTTKVAIKDLSLNLYEGQVTVLLGHNGAGKSTTLSILSGL 574
Cdd:TIGR00957 608 KRLRIFLSHEELEPDSIERRTIKPGEGNSITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAE 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 575 YPPTSGEAYVHGedisqhmdqvrnSLGLCPQQNLLfDHLTVSEHLYFYC-----RIKGVPQKMYLEETNNMLSAFNLMEK 649
Cdd:TIGR00957 688 MDKVEGHVHMKG------------SVAYVPQQAWI-QNDSLRENILFGKalnekYYQQVLEACALLPDLEILPSGDRTEI 754
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 650 CDAfSKSLSGGMKRKLAIIIALIGGSKVAILDEPTSGMDPASRRSTWDIL---QTYKQNRTILLTTH---YMDEADVlgd 723
Cdd:TIGR00957 755 GEK-GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHgisYLPQVDV--- 830
|
250
....*....|....*
gi 46358378 724 rIAIMVRGTLRCCGS 738
Cdd:TIGR00957 831 -IIVMSGGKISEMGS 844
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
540-571 |
6.37e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 40.68 E-value: 6.37e-03
10 20 30
....*....|....*....|....*....|..
gi 46358378 540 AIKDLSLNLyeGQVTVLLGHNGAGKSTTLSIL 571
Cdd:COG4637 12 SLRDLELPL--GPLTVLIGANGSGKSNLLDAL 41
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1506-1566 |
7.38e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.93 E-value: 7.38e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 46358378 1506 PSVIFLDEPSTGMDPRARRLLWdTVI-KIRESGKAIIITSHSMEECEALCTRLSIMVRGRLT 1566
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIY-TIInELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1486-1564 |
7.77e-03 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 39.91 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1486 STYSEGNKRRLSTAIATMGKPSVIFLDEPSTGMDPRAR-RLLwDTVIK-IRESGKAIIITSHSMEECEALCTRLSIMVRG 1563
Cdd:PRK11701 150 TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQaRLL-DLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
.
gi 46358378 1564 R 1564
Cdd:PRK11701 229 R 229
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
1474-1548 |
7.81e-03 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 40.37 E-value: 7.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46358378 1474 SLDLESHANSLISTYSEGNKRRLSTAIATM-------GKPSVIFLDEPSTGMDPRARRLLWDTVIKIRESGKAIIITSHS 1546
Cdd:COG3593 149 SLRIEDGKELPLDRLGSGFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHS 228
|
..
gi 46358378 1547 ME 1548
Cdd:COG3593 229 PH 230
|
|
| |
