|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-1520 |
3.16e-116 |
|
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: 406.71 E-value: 3.16e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 37 GVIFSDTFSY------RLKFNWGYRIPVIKEHSEYTEHCW-----AMHGEIFCYLakyWlKGFVAFQAAINAAIievtTN 105
Cdd:TIGR01257 550 GVVFPDMYPWtsslppHVKYKIRMDIDVVEKTNKIKDRYWdsgprADPVEDFRYI---W-GGFAYLQDMVEQGI----TR 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 106 HSVMEELTsvIGI---NMKIPPFISKGE--IMNEWFHFTCLVSFssfIYFASLNVA----RERGKFKKLMTVMGLRESAF 176
Cdd:TIGR01257 622 SQMQAEPP--VGIylqQMPYPCFVDDSFmiILNRCFPIFMVLAW---IYSVSMTVKsivlEKELRLKETLKNQGVSNAVI 696
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 177 WLSWGLTYICfIFIMSIFM-ALVITSIPIVFHTGFMVIFTLYSLYGLSLIALAFLMSVLIRKPMLAGLAGflftvfwGCL 255
Cdd:TIGR01257 697 WCTWFLDSFS-IMSMSIFLlTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACS-------GVI 768
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 256 GFTvLYRQLPLSLGW----------VLSLLSPFAFTAGMAQITHLDNYLSGV----IFPDP-SGDSYKMIATFFILAFDT 320
Cdd:TIGR01257 769 YFT-LYLPHILCFAWqdrmtadlktAVSLLSPVAFGFGTEYLVRFEEQGLGLqwsnIGNSPlEGDEFSFLLSMKMMLLDA 847
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 321 LFYLIFTLYFERVLPDKDGhgdSPL---FFLKSSFWSKHQ--NTHHE--------IFENEINPEHS---SDDSFEPVSPE 384
Cdd:TIGR01257 848 ALYGLLAWYLDQVFPGDYG---TPLpwyFLLQESYWLGGEgcSTREEralektepLTEEMEDPEHPegiNDSFFERELPG 924
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 385 FhgKEAIRIRNVIK--EYNGKTGkVEALQGIFfdiYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeiT 462
Cdd:TIGR01257 925 L--VPGVCVKNLVKifEPSGRPA-VDRLNITF---YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--T 996
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 463 DMEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:TIGR01257 997 NLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLKRKWGIGYH 622
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFY 1156
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 623 LSLHR-----------------------NEMC---------------DTEKITSLIKQHIPDAKLTTESEEKLVYSLPLE 664
Cdd:TIGR01257 1157 LTLVRkmkniqsqrggcegtcsctskgfSTRCparvdeitpeqvldgDVNELMDLVYHHVPEAKLVECIGQELIFLLPNK 1236
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 665 --KTNKFPDLYSDLDKC-SDQGIRNYAVSVTSLNEVFLNLEgKSAIDEPDFDIGKQEK---------IHVTRNTGDESEM 732
Cdd:TIGR01257 1237 nfKQRAYASLFRELEETlADLGLSSFGISDTPLEEIFLKVT-EDADSGSLFAGGAQQKrenanlrhpCSGPTEKAGQTPQ 1315
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 733 EQVLCS------------LPETR----KAVSSAALWRRQIYAVATLRFLKLRRERRALLCLLLVLG-IAFIPIILEKIMY 795
Cdd:TIGR01257 1316 ASHTCSpgqpaahpegqpPPEPEdpgvPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPAtFVFLALMLSIIIP 1395
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 796 KVTR----ETHCWEFSPSMYFLSLEQIPKTPLTSL--LIVNNTG----------------------------SNIEDLVH 841
Cdd:TIGR01257 1396 PFGEypalTLHPWMYGQQYTFFSMDEPNSEHLEVLadVLLNKPGfgnrclkeewlpeypcgnstpwktpsvsPNITHLFQ 1475
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 842 -----------SLKC-------------------------QDIVLEIDDFRNRNGSD---------------------DP 864
Cdd:TIGR01257 1476 kqkwtaahpspSCRCstrekltmlpecpegagglpppqrtQRSTEILQDLTDRNISDflvktypalirsslkskfwvnEQ 1555
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 865 SYNG--------AIIVSGD-----------------------------------QKDYRFSVACNTKKLNCFPVLMGIVS 901
Cdd:TIGR01257 1556 RYGGisiggklpAIPITGEalvgflsdlgqmmnvsggpvtreaskempdflkhlETEDNIKVWFNNKGWHALVSFLNVAH 1635
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 902 NALM-------------GI------FNFT--ELIQMESTSFSRDDIV-----LDLGFIDGSIFLLLITNCVSPfigmssi 955
Cdd:TIGR01257 1636 NAILraslpkdrdpeeyGItvisqpLNLTkeQLSEITVLTTSVDAVVaicviFAMSFVPASFVLYLIQERVNK------- 1708
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 956 sdyKKNVQsqlWISGLWPSAYWCGQALVDIPLYFLilfSIHLIYYfIFLGFQ----LSWELMFVLVVCIIGCAVSLIFLT 1031
Cdd:TIGR01257 1709 ---AKHLQ---FISGVSPTTYWLTNFLWDIMNYAV---SAGLVVG-IFIGFQkkayTSPENLPALVALLMLYGWAVIPMM 1778
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1032 YVLSFIFRKWRKNNGFWSFGFFIILICVSTI-MVSTQYE------KLNLIL--CMIFIPSFTL-LGyvmlLIQLDFMRNL 1101
Cdd:TIGR01257 1779 YPASFLFDVPSTAYVALSCANLFIGINSSAItFVLELFEnnrtllRFNAMLrkLLIVFPHFCLgRG----LIDLALSQAV 1854
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1102 DSLDNRINEVNKT------ILLTTLIPYLQSVIFLFVIRCLEMKYgneimnkdpvFRISPRSREthPNPEEPEEEDEDVQ 1175
Cdd:TIGR01257 1855 TDVYAQFGEEHSAnpfqwdLIGKNLVAMAVEGVVYFLLTLLIQHH----------FFLSRWIAE--PAKEPIFDEDDDVA 1922
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1176 AER---VQAANALTAPNLEEepvitascLHKEYYETKKScfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMI 1252
Cdd:TIGR01257 1923 EERqriISGGNKTDILRLNE--------LTKVYSGTSSP---------AVDRLCVGVRPGECFGLLGVNGAGKTTTFKML 1985
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1253 TGCTKPTAGVVVLQGSR--ASVRQQHDNslkfLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQ 1330
Cdd:TIGR01257 1986 TGDTTVTSGDATVAGKSilTNISDVHQN----MGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLS 2061
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1331 EQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKnKERGTLLTTHYMSEAEAVCDRM 1410
Cdd:TIGR01257 2062 LYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRL 2140
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1411 AMMVSGTLRCIGSIQHLKNKFGRDYLLEIKMKEPT-----QVEALHTEILKLFPQAAWQERYSSLMAYKLPVEDvhpLSR 1485
Cdd:TIGR01257 2141 AIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSSSS---LAR 2217
|
1770 1780 1790
....*....|....*....|....*....|....*
gi 296439455 1486 AFFKLEAMKQTFNLEEYSLSQATLEQVFLELCKEQ 1520
Cdd:TIGR01257 2218 IFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQ 2252
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
391-614 |
2.55e-82 |
|
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: 269.37 E-value: 2.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeiTDMEEIRKN 470
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR--TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLK 614
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1216-1428 |
2.90e-80 |
|
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: 263.60 E-value: 2.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSLKFLGYCPQENSLWPK 1295
Cdd:cd03263 12 KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYING--YSIRTDRKAARQSLGYCPQFDALFDE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:cd03263 90 LTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1376 QQMWQILQATVKNkeRGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLK 1428
Cdd:cd03263 170 RAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
391-609 |
5.97e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 237.65 E-value: 5.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeiTDMEEIRKN 470
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA--RDPAEVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1196-1431 |
1.43e-70 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 236.50 E-value: 1.43e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEYyetkkscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQ 1275
Cdd:COG1131 1 IEVRGLTKRY-----------GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLG--EDVARD 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1276 HDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL 1355
Cdd:COG1131 68 PAEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQatvKNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKF 1431
Cdd:COG1131 148 HDPELLILDEPTSGLDPEARRELWELLR---ELAAEGKtvLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
391-609 |
1.56e-60 |
|
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: 207.79 E-value: 1.56e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmeEIRKN 470
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHK-VDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1195-1434 |
3.33e-56 |
|
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: 195.46 E-value: 3.33e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1195 VITASCLHKEYyetkkscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-----SR 1269
Cdd:COG4555 1 MIEVENLSKKY-----------GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGedvrkEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1270 ASVRQQhdnslkfLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLC 1349
Cdd:COG4555 70 REARRQ-------IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1350 FVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:COG4555 143 LARALVHDPKVLLLDEPTNGLDVMARRLLREILRA-LKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
....*
gi 296439455 1430 KFGRD 1434
Cdd:COG4555 222 EIGEE 226
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
391-604 |
2.52e-55 |
|
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: 190.30 E-value: 2.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitDMEEIRKN 470
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK--EPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLrvfakikgiqpkeveqevkriimeldmqsiqdiiakKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1217-1418 |
1.67e-52 |
|
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: 182.21 E-value: 1.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFLGYCPQENSLWPKL 1296
Cdd:cd03230 11 GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGK--DIKKEPEEVKRRIGYLPEEPSLYENL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELyaavkglgkedaalsisrlvealklqeqlkapvktlSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:cd03230 89 TVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTSGLDPESRR 132
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1377 QMWQILQAtvKNKERGT-LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03230 133 EFWELLRE--LKKEGKTiLLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1218-1521 |
2.93e-52 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 186.08 E-value: 2.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDnslkfLGYCPQENSLWPKLT 1297
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRR-----IGYLPEERGLYPKMK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 MKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQ 1377
Cdd:COG4152 88 VGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVEL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1378 MWQILQATvknKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRdYLLEIKMKEPtqvealhTEIL 1455
Cdd:COG4152 168 LKDVIREL---AAKGTtvIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGR-NTLRLEADGD-------AGWL 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1456 KLFPQAAWQERYSSLMAYKLP-VEDVHPLsraffkLEAMKQTFNLEEYSLSQATLEQVFLELCKEQE 1521
Cdd:COG4152 237 RALPGVTVVEEDGDGAELKLEdGADAQEL------LRALLARGPVREFEEVRPSLNEIFIEVVGEKA 297
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1221-1516 |
6.63e-52 |
|
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: 185.29 E-value: 6.63e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-----SRASVRQQhdnslkfLGYCPQENSLWPK 1295
Cdd:TIGR01188 8 AVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGydvvrEPRKVRRS-------IGIVPQYASVDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:TIGR01188 81 LTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1376 QQMWQILQATVKNKeRGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRDYlLEIKMKEPTQVEALHTEIL 1455
Cdd:TIGR01188 161 RAIWDYIRALKEEG-VTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEVSMLI 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1456 KLFPQAAWQERYSSLMA--YKLPVEDVHPLSRAFFKlEAMKQTFNLEEYSLSQATLEQVFLEL 1516
Cdd:TIGR01188 239 AELGETGLGLLAVTVDSdrIKILVPDGDETVPEIVE-AAIRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1221-1428 |
7.33e-52 |
|
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: 182.18 E-value: 7.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:cd03265 15 AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH--DVVREPREVRRRIGIVFQDLSVDDELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQ 1380
Cdd:cd03265 93 NLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1381 ILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLK 1428
Cdd:cd03265 173 YIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1219-1422 |
4.38e-51 |
|
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: 179.40 E-value: 4.38e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDnslkfLGYCPQENSLWPKLTM 1298
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQM 1378
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 1379 WQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03269 168 KDVIR-ELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
405-703 |
1.41e-49 |
|
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: 178.74 E-value: 1.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLseITDMEEIRKNIGFCPQFNFQFDFL 484
Cdd:TIGR01188 4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV--VREPRKVRRSIGIVPQYASVDEDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:TIGR01188 82 TGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 565 RVWSLLKEHK-VDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLKRKWGiGYHLSLHRNEMCDTEKITSLIKQH 643
Cdd:TIGR01188 162 AIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG-KDTLESRPRDIQSLKVEVSMLIAE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 644 IPD-----AKLTTESEEKLVYSLPLEKTnkFPDLYSDLDKcsdQGIRNYAVSVT--SLNEVFLNLEG 703
Cdd:TIGR01188 241 LGEtglglLAVTVDSDRIKILVPDGDET--VPEIVEAAIR---NGIRIRSISTErpSLDDVFLKLTG 302
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
391-609 |
1.23e-48 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 173.29 E-value: 1.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:COG1122 1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQF-NFQFDFLTVRENLrVFA-KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLtlgiAILG---- 544
Cdd:COG1122 77 VGLVFQNpDDQLFAPTVEEDV-AFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRV----AIAGvlam 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
391-605 |
1.50e-48 |
|
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: 172.38 E-value: 1.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkvEALQGIFFDIYEGqITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitDMEEIRKN 470
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQ-FNFqFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03264 74 IGYLPQeFGV-YPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLK 605
Cdd:cd03264 153 IVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1195-1480 |
5.64e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 174.51 E-value: 5.64e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1195 VITASCLHKEY--YETK-------KSCFSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGvvv 1264
Cdd:COG4586 1 IIEVENLSKTYrvYEKEpglkgalKGLFRREYREVeAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSG--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1265 lqgsrasvrqqhdnSLKFLGYCPQENS----------------LWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALK 1328
Cdd:COG4586 78 --------------EVRVLGYVPFKRRkefarrigvvfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1329 LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAV 1406
Cdd:COG4586 144 LGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEAL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1407 CDRMAMMVSGTLRCIGSIQHLKNKFGRDYLLEIKMKEPTQVEAL--HTEILKLFPQAAW-----QERYSSLMAY---KLP 1476
Cdd:COG4586 222 CDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELprGGEVIEREGNRVRlevdpRESLAEVLARllaRYP 301
|
....
gi 296439455 1477 VEDV 1480
Cdd:COG4586 302 VRDL 305
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
391-604 |
1.48e-47 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 169.59 E-value: 1.48e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNT---QLSEITDMEEI 467
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTdisKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQ 547
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 548 VLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADiLADRKVFLSNGKL 604
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
391-614 |
2.94e-47 |
|
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: 169.09 E-value: 2.94e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqLSEITDMEEIRKN 470
Cdd:cd03265 1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAG--HDVVREPREVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03265 75 IGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLF 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHK--VDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLK 614
Cdd:cd03265 155 LDEPTIGLDPQTRAHVWEYIEKLKeeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
391-608 |
5.67e-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: 159.46 E-value: 5.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeiTDMEEIRKN 470
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHK-VDRLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
392-603 |
6.47e-44 |
|
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: 158.78 E-value: 6.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKNI 471
Cdd:cd03225 1 ELKNLSFSYPD--GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQF-NFQFDFLTVRENLrVFA-KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03225 78 GLVFQNpDDQFFGPTVEEEV-AFGlENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
391-603 |
8.72e-43 |
|
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: 155.33 E-value: 8.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitDMEEIRKN 470
Cdd:COG4133 3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD--AREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEveQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQfmDEADILADRKVFLSNGK 603
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARVLDLGDFK 206
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
410-556 |
5.58e-42 |
|
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: 150.88 E-value: 5.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDFLTVREN 489
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 490 LRVFAKIKGIQPKEVEQEVKRIIMELDMQ----SIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTA 556
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
388-604 |
7.66e-42 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.66 E-value: 7.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME-- 465
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREla 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIR-KNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILG 544
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADIlADRKVFLSNGKL 604
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
391-604 |
3.85e-41 |
|
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: 150.83 E-value: 3.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqlSEITDMEEIRKN 470
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGF---CPQFnfqFDFLTVRENLRVFAKIKGIQpkevEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQ 547
Cdd:cd03268 74 IGAlieAPGF---YPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 548 VLLLDEPTAGLDPFSRHRVWSLLKEH-KVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1217-1419 |
6.42e-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: 150.42 E-value: 6.42e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGeVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFLGYCPQENSLWPKL 1296
Cdd:cd03264 11 GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ--DVLKQPQKLRRRIGYLPQEFGVYPNF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:cd03264 88 TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERI 167
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1377 QMWQILQATVKNkeRGTLLTTHYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:cd03264 168 RFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1196-1419 |
1.25e-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: 149.29 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEYyetkkscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAsvrQQ 1275
Cdd:cd03268 1 LKTNDLTKTY-----------GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY---QK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1276 HDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDaalsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL 1355
Cdd:cd03268 67 NIEALRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:cd03268 143 GNPDLLILDEPTNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
392-603 |
2.66e-40 |
|
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: 146.62 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNI 471
Cdd:cd00267 1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKL-PLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQfnfqfdfltvrenlrvfakikgiqpkeveqevkriimeldmqsiqdiiakkLSGGQKRKLTLGIAILGDPQVLLL 551
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 552 DEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1219-1516 |
3.01e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 151.88 E-value: 3.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLkfLGYCPQENSLWPKLTM 1298
Cdd:PRK13537 20 KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--VGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQM 1378
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1379 WQILQATVKnKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL-KNKFGRDyLLEIKMKEPtqvEALHTEilkL 1457
Cdd:PRK13537 178 WERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALiESEIGCD-VIEIYGPDP---VALRDE---L 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1458 FPQAAWQE-RYSSLMAYklpVEDVHPLSRaffkleAMKQTFNLeEYSLSQATLEQVFLEL 1516
Cdd:PRK13537 250 APLAERTEiSGETLFCY---VRDPEPLHA------RLKGRAGL-RYLHRPANLEDVFLRL 299
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1196-1422 |
5.07e-39 |
|
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: 145.20 E-value: 5.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEYYETKKSCfstrkkkIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrQQ 1275
Cdd:cd03266 2 ITADALTKRFRDVKKTV-------QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV--KE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1276 HDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL 1355
Cdd:cd03266 73 PAEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQATvknKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQL---RALGKciLFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1224-1525 |
6.05e-39 |
|
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: 159.79 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1224 NVSFcvKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFLGYCPQENSLWPKLTMKEHLE 1303
Cdd:TIGR01257 950 NITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK--DIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1304 LYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILq 1383
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL- 1104
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1384 atVKNKE-RGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRDYLLEI--KMKE----------------- 1443
Cdd:TIGR01257 1105 --LKYRSgRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKNiqsqrggcegtcsctsk 1182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1444 ------PTQVEALHTE-------------ILKLFPQAAWQERYSSLMAYKLPVEDVHPLSRA--FFKLEAMKQTFNLEEY 1502
Cdd:TIGR01257 1183 gfstrcPARVDEITPEqvldgdvnelmdlVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYAslFRELEETLADLGLSSF 1262
|
330 340
....*....|....*....|...
gi 296439455 1503 SLSQATLEQVFLELCKEQELGNV 1525
Cdd:TIGR01257 1263 GISDTPLEEIFLKVTEDADSGSL 1285
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1196-1418 |
7.27e-39 |
|
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: 145.17 E-value: 7.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEY---------YETKKSCFSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVL 1265
Cdd:cd03267 1 IEVSNLSKSYrvyskepglIGSLKSLFKRKYREVeALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1266 QGSRASVRQqhDNSLKFLGYC-PQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGI 1344
Cdd:cd03267 81 AGLVPWKRR--KKFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1345 KRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03267 159 RMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY--NRERGTtvLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
390-603 |
8.30e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 148.83 E-value: 8.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEeiRK 469
Cdd:PRK13536 41 AIDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA--RA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFlTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK13536 115 RIGVVPQFdNLDLEF-TVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 549 LLLDEPTAGLDPFSRHRVW----SLLKEHKVdrlILFSTQFMDEADILADRKVFLSNGK 603
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
391-603 |
1.20e-38 |
|
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: 142.14 E-value: 1.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:cd03228 1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL-DLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFlTVRENLrvfakikgiqpkeveqevkriimeldmqsiqdiiakkLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGK 603
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
391-604 |
1.27e-38 |
|
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: 144.25 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL-----SVSTEGSATIYNTQLSEI-TDM 464
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLdVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFCPQFNFQFDfLTVRENLRVFAKIKGIQPKE-----VEQEVKRiiMELDMQSIQDIIAKKLSGGQKRKLTLG 539
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEelderVEEALRK--AALWDEVKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
391-601 |
4.62e-38 |
|
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: 142.61 E-value: 4.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeitdmeEIRKN 470
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 551 LDEPTAGLDPFSRHRVWSLL----KEHKVDrlILFSTQFMDEADILADRKVFLSN 601
Cdd:cd03293 155 LDEPFSALDALTREQLQEELldiwRETGKT--VLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
391-609 |
7.43e-38 |
|
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: 143.34 E-value: 7.43e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN 470
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQfN--FQFDFLTVR-------ENLrvfakikGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKltlgIA 541
Cdd:TIGR04520 79 VGMVFQ-NpdNQFVGATVEddvafglENL-------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQR----VA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 542 ILG----DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRL-ILFSTQFMDEAdILADRKVFLSNGKLKCAGS 609
Cdd:TIGR04520 147 IAGvlamRPDIIILDEATSMLDPKGRKEVLETIRKlNKEEGItVISITHDMEEA-VLADRVIVMNKGKIVAEGT 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1223-1398 |
1.19e-36 |
|
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: 138.00 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSLKFLGYCPQENSLWPKLTMKEHL 1302
Cdd:COG4133 19 SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG--EPIRDAREDYRRRLAYLGHADGLKPELTVRENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1303 ELYAAVKGLGKEDAAlsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQIL 1382
Cdd:COG4133 97 RFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELI 174
|
170
....*....|....*.
gi 296439455 1383 QATVKNKeRGTLLTTH 1398
Cdd:COG4133 175 AAHLARG-GAVLLTTH 189
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
390-603 |
1.32e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 141.10 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitDMEEIRK 469
Cdd:PRK13537 7 PIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFlTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK13537 81 RVGVVPQFdNLDPDF-TVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 549 LLLDEPTAGLDPFSRHRVW----SLLKEHKVdrlILFSTQFMDEADILADRKVFLSNGK 603
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWerlrSLLARGKT---ILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1219-1416 |
5.07e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.35 E-value: 5.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSLKFLGYCPQENSLWPKLTM 1298
Cdd:PRK13536 54 KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLG--VPVPARARLARARIGVVPQFDNLDLEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQM 1378
Cdd:PRK13536 132 RENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLI 211
|
170 180 190
....*....|....*....|....*....|....*...
gi 296439455 1379 WQILQATVKnKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK13536 212 WERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
390-609 |
5.85e-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: 137.03 E-value: 5.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYN---TQLSEiTDMEE 466
Cdd:COG1127 5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGqdiTGLSE-KELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKNIGFCpqfnFQ----FDFLTVREN----LRVFAKIKgiqpkevEQEVKRIIME-LDMQSIQDIIAKK---LSGGQKR 534
Cdd:COG1127 80 LRRRIGML----FQggalFDSLTVFENvafpLREHTDLS-------EAEIRELVLEkLELVGLPGAADKMpseLSGGMRK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 535 KLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKvDRL---ILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELR-DELgltSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
390-602 |
1.18e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.76 E-value: 1.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLseitdmEEIRK 469
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------TGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCpqfnFQ----FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGD 545
Cdd:COG1116 81 DRGVV----FQepalLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAND 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 546 PQVLLLDEPTAGLDPFSRHRVWSLL----KEHKvdRLILFSTQFMDEADILADRKVFLSNG 602
Cdd:COG1116 157 PEVLLMDEPFGALDALTRERLQDELlrlwQETG--KTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
391-625 |
1.50e-35 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 137.20 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATI--YNTQLSEITDMEEI 467
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIdgRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCpqfnFQFD----F-LTVRE-------NLrvfakikGIQPKEVEQEVKRIIMELDM-QSIQDIIAKKLSGGQKR 534
Cdd:TIGR04521 81 RKKVGLV----FQFPehqlFeETVYKdiafgpkNL-------GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 535 KltlgIAILG----DPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:TIGR04521 150 R----VAIAGvlamEPEVLILDEPTAGLDPKGRKEILDLFKRlhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
250
....*....|....*....
gi 296439455 609 SS--LFLKRKWGIGYHLSL 625
Cdd:TIGR04521 226 TPreVFSDVDELEKIGLDV 244
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
391-608 |
1.61e-35 |
|
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: 134.72 E-value: 1.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitdmeEIRKN 470
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI-----AARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
391-604 |
3.69e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.79 E-value: 3.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGkveaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:COG4619 1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDfLTVRENLRVFAKIKGIQPKEveQEVKRIIMELDMQsiQDIIAKK---LSGGQKRKLTLGIAILGDPQ 547
Cdd:COG4619 76 VAYVPQEPALWG-GTVRDNLPFPFQLRERKFDR--ERALELLERLGLP--PDILDKPverLSGGERQRLALIRALLLQPD 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 548 VLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG4619 151 VLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
390-706 |
5.37e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 136.39 E-value: 5.37e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeitdmEEIRK 469
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCP-------QfnfqfdfLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:COG4152 72 RIGYLPeerglypK-------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKV-DRLILFSTQFMDEADILADRKVFLSNGKLKCAGS-----SLFLKRK 616
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAkGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSvdeirRQFGRNT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 617 WGIGYHLslhrnemcDTEKITSLikqhipdAKLTTESEEKLVYSLPLEKTNKFPDLysdLDKCSDQG-IRNYAVSVTSLN 695
Cdd:COG4152 225 LRLEADG--------DAGWLRAL-------PGVTVVEEDGDGAELKLEDGADAQEL---LRALLARGpVREFEEVRPSLN 286
|
330
....*....|.
gi 296439455 696 EVFLNLEGKSA 706
Cdd:COG4152 287 EIFIEVVGEKA 297
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
386-604 |
6.03e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 134.00 E-value: 6.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 386 HGKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqLSEI--TD 463
Cdd:cd03267 13 YSKEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV----AGLVpwKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIG--FCPQFNFQFDfLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIA 541
Cdd:cd03267 89 RKKFLRRIGvvFGQKTQLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR--LILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03267 168 LLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1217-1423 |
1.22e-34 |
|
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: 133.05 E-value: 1.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKL 1296
Cdd:cd03218 11 GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 1377 QmwqiLQATVKN-KER--GTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:cd03218 171 D----IQKIIKIlKDRgiGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
391-604 |
1.56e-34 |
|
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: 132.63 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME--EIR 468
Cdd:cd03261 1 IELRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNFQFDFLTVRENLRVFAKIKGiqpKEVEQEVKRIIME-LDMQSIQDIIAKK---LSGGQKRKLTLGIAILG 544
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHT---RLSEEEIREIVLEkLEAVGLRGAEDLYpaeLSGGMKKRVALARALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKEHKvDRLILFS---TQFMDEADILADRKVFLSNGKL 604
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLK-KELGLTSimvTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
391-604 |
1.64e-34 |
|
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: 132.70 E-value: 1.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI--TDMEEIR 468
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLsgKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQ-FNFqFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQ 547
Cdd:cd03258 82 RRIGMIFQhFNL-LSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 548 VLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
405-603 |
1.82e-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: 132.17 E-value: 1.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFDFL 484
Cdd:cd03224 11 GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGiqPKEVEQEVKRIimeLDM----QSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:cd03224 91 TVEENLLLGAYARR--RAKRKARLERV---YELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 561 FSRHRVWSLLKEHKVDRL-ILFSTQFMDEADILADRKVFLSNGK 603
Cdd:cd03224 166 KIVEEIFEAIRELRDEGVtILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
394-604 |
7.33e-34 |
|
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: 129.59 E-value: 7.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGKTGKVEA--LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL--SVSTEGSATIYNTQLseitDMEEIRK 469
Cdd:cd03213 7 RNLTVTVKSSPSKSGKqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPL----DKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDFLTVRENLRVFAKIKGIqpkeveqevkriimeldmqsiqdiiakklSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03213 83 IIGYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLL 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFST-QFMDEADILADRKVFLSNGKL 604
Cdd:cd03213 134 FLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIhQPSSEIFELFDKLLLLSQGRV 190
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
391-603 |
8.71e-34 |
|
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: 128.46 E-value: 8.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDM-EEIRK 469
Cdd:cd03229 1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQfNFQ-FDFLTVRENlrvfakikgiqpkeveqevkriimeldmqsiqdiIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:cd03229 77 RIGMVFQ-DFAlFPHLTVLEN----------------------------------IALGLSGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKEHKvDRL---ILFSTQFMDEADILADRKVFLSNGK 603
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQ-AQLgitVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
391-609 |
9.08e-34 |
|
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: 130.63 E-value: 9.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAtIYNTQlsEITDMEE---I 467
Cdd:cd03219 1 LEVRGLTKRF----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSV-LFDGE--DITGLPPheiA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFcpqfNFQ----FDFLTVRENLRVFAKIKGIQP----------KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQK 533
Cdd:cd03219 74 RLGIGR----TFQiprlFPELTVLENVMVAAQARTGSGlllararreeREARERAEELLERVGLADLADRPAGELSYGQQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 534 RKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK------------EHKVDrlILFStqfmdeadiLADRKVFLSN 601
Cdd:cd03219 150 RRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRelrergitvllvEHDMD--VVMS---------LADRVTVLDQ 218
|
....*...
gi 296439455 602 GKLKCAGS 609
Cdd:cd03219 219 GRVIAEGT 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
390-623 |
1.11e-33 |
|
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: 138.36 E-value: 1.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRK 469
Cdd:COG4987 333 SLELEDVSFRYPG--AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE-DDLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDfLTVRENLRVfAKikgiqPKEVEQEVKRIimeLDMQSIQDIIAK--------------KLSGGQKRK 535
Cdd:COG4987 410 RIAVVPQRPHLFD-TTLRENLRL-AR-----PDATDEELWAA---LERVGLGDWLAAlpdgldtwlgeggrRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGKLKCAGSSLFLKR 615
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLA 558
|
....*...
gi 296439455 616 KWGIGYHL 623
Cdd:COG4987 559 QNGRYRQL 566
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
391-604 |
1.63e-33 |
|
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: 129.18 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQlseITDMEEIRKN 470
Cdd:cd03259 1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRD---VTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLrVFA-KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENI-AFGlKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
390-609 |
1.65e-33 |
|
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: 130.55 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRK 469
Cdd:COG1120 1 MLEAENLSVGYGGRP----VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSR-RELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNfQFDF-LTVRENLRV--FAKIKGIQP--KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILG 544
Cdd:COG1120 76 RIAYVPQEP-PAPFgLTVRELVALgrYPHLGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
390-609 |
2.04e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlseitDMEEIRK 469
Cdd:COG1121 6 AIELENLTVSYGGRP----VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK------PPRRARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ-FNFQFDF-LTVRE--------NLRVFAKIKgiqpKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLG 539
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmgrygRRGLFRRPS----RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLsNGKLKCAGS 609
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGP 221
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
362-623 |
5.50e-33 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 138.04 E-value: 5.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 362 EIFENEinPEHSSDDSFEPVsPEFHGkeAIRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILS 441
Cdd:COG2274 450 DILDLP--PEREEGRSKLSL-PRLKG--DIELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 442 GLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFdFLTVRENLRVFAKikGIQPKEVEQ-----EVKRIIMELD 516
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQI-DPASLRRQIGVVLQDVFLF-SGTIRENITLGDP--DATDEEIIEaarlaGLHDFIEALP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 517 MQsIQDIIA---KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQfmDEADI-L 592
Cdd:COG2274 599 MG-YDTVVGeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrL 675
|
250 260 270
....*....|....*....|....*....|.
gi 296439455 593 ADRKVFLSNGKLKCAGSSLFLKRKWGIGYHL 623
Cdd:COG2274 676 ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1221-1429 |
5.88e-33 |
|
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: 127.94 E-value: 5.88e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVkgLGKEDAALSISRLVEAL-KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMW 1379
Cdd:cd03224 95 NLLLGAYA--RRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1380 QILQATvknKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:cd03224 173 EAIREL---RDEGVtiLLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
405-608 |
9.23e-33 |
|
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: 126.88 E-value: 9.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLseitdmEEIRKNIGFCPQ-FNFQFDF 483
Cdd:cd03235 10 GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVPQrRSIDRDF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 484 -LTVRE--NLRVFAKIKGIQPkeVEQEVKRIIME-LDMQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTA 556
Cdd:cd03235 84 pISVRDvvLMGLYGHKGLFRR--LSKADKAKVDEaLERVGLSELADRQigeLSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 557 GLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRkVFLSNGKLKCAG 608
Cdd:cd03235 162 GVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1212-1438 |
1.33e-32 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 127.06 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGY 1285
Cdd:COG1122 7 SFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGkditkkNLRELRRK-------VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1286 CPQ-------------------ENSlwpkltmkehlelyaavkGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKR 1346
Cdd:COG1122 80 VFQnpddqlfaptveedvafgpENL------------------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1347 KLCF--VLSIlgNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT-LLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG1122 142 RVAIagVLAM--EPEVLVLDEPTAGLDPRGRRELLELLKRL--NKEGKTvIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
250
....*....|....*
gi 296439455 1424 IQHLknkFGRDYLLE 1438
Cdd:COG1122 218 PREV---FSDYELLE 229
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1222-1368 |
1.34e-32 |
|
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: 124.30 E-value: 1.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsRASVRQQHDNSLKFLGYCPQENSLWPKLTMKEH 1301
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDG-QDLTDDERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1302 LELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPV----KTLSEGIKRKLCFVLSILGNPSVVLLDEPFT 1368
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
361-609 |
1.43e-32 |
|
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: 134.89 E-value: 1.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 361 HEIFENEINPEHSSDDSFEPVSPEfhgkeAIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNIL 440
Cdd:COG4988 312 FALLDAPEPAAPAGTAPLPAAGPP-----SIELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLL 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 441 SGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDfLTVRENLRvFAKiKGIQPKEVEQEVKR-----IIMEL 515
Cdd:COG4988 384 LGFLPPYSGSILINGVDLSDL-DPASWRRQIAWVPQNPYLFA-GTIRENLR-LGR-PDASDEELEAALEAagldeFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 516 DmQSIQDII---AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQfmDEADI- 591
Cdd:COG4988 460 P-DGLDTPLgegGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLa 536
|
250
....*....|....*...
gi 296439455 592 LADRKVFLSNGKLKCAGS 609
Cdd:COG4988 537 QADRILVLDDGRIVEQGT 554
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
405-610 |
1.50e-32 |
|
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: 127.02 E-value: 1.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATiYNTQlsEITDM--EEI-RKNIGFCPQFNFQF 481
Cdd:COG0410 14 GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIR-FDGE--DITGLppHRIaRLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 DFLTVRENLRVFAKIKGiQPKEVEQEVKRiIMEL--DMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:COG0410 91 PSLTVEENLLLGAYARR-DRAEVRADLER-VYELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 560 PFSRHRVWSLLKEHKVDRL-ILFSTQFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:COG0410 169 PLIVEEIFEIIRRLNREGVtILLVEQNARFALEIADRAYVLERGRIVLEGTA 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
390-604 |
1.37e-31 |
|
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: 123.85 E-value: 1.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKtgKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRK 469
Cdd:cd03245 2 RIEFRNVSFSYPNQ--EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQL-DPADLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFdFLTVRENLRVF------------AKIKGiqpkeVEQEVKRIIMELDMQsiqdiIAKK---LSGGQKR 534
Cdd:cd03245 79 NIGYVPQDVTLF-YGTLRDNITLGapladderilraAELAG-----VTDFVNKHPNGLDLQ-----IGERgrgLSGGQRQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 535 KLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGKL 604
Cdd:cd03245 148 AVALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
395-604 |
1.45e-31 |
|
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: 123.92 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 395 NVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVS---TEGSATIYNTQLSEitdmEEIRKNI 471
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP----DQFQKCV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQFNFQFDFLTVRENLRVFAKI-------KGIQPKEVEQEVKRiimELDMQSIQDIIAKKLSGGQKRKLTLGIAILG 544
Cdd:cd03234 84 AYVRQDDILLPGLTVRETLTYTAILrlprkssDAIRKKRVEDVLLR---DLALTRIGGNLVKGISGGERRRVSIAVQLLW 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKEH-KVDRLILFSTQfMDEADI--LADRKVFLSNGKL 604
Cdd:cd03234 161 DPKVLILDEPTSGLDSFTALNLVSTLSQLaRRNRIVILTIH-QPRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1207-1417 |
1.49e-31 |
|
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: 123.35 E-value: 1.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFS-TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSlKFLGY 1285
Cdd:cd03225 1 ELKNLSFSyPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR-RKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1286 CPQ--ENSLWpKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCfVLSIL-GNPSVVL 1362
Cdd:cd03225 80 VFQnpDDQFF-GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVA-IAGVLaMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1363 LDEPFTGMDPEGQQQMWQILqATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGT 1417
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
390-609 |
1.75e-31 |
|
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: 123.99 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqlSEITDMEEIRK 469
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG---EDATDVPVQER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMEL----DMQSIQDIIAKKLSGGQKRKLTLGIAILGD 545
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 546 PQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
392-605 |
2.30e-31 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 122.75 E-value: 2.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitdmEEIRKNI 471
Cdd:cd03226 1 RIENISFSYKKGT---EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQ-FNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRI-IMELDMQSIQDiiakkLSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLLGLKELDAGNEQAETVLKDLdLYALKERHPLS-----LSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKLK 605
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1193-1423 |
2.74e-31 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 123.60 E-value: 2.74e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1193 EPVITASCLHKEYyetkkscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SR 1269
Cdd:COG1137 1 MMTLEAENLVKSY-----------GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGediTH 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1270 ASVrqqHDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLC 1349
Cdd:COG1137 70 LPM---HKRARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1350 FVLSILGNPSVVLLDEPFTGMDPegqqqmwqI----LQATVKN-KER--GTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:COG1137 147 IARALATNPKFILLDEPFAGVDP--------IavadIQKIIRHlKERgiGVLITDHNVRETLGICDRAYIISEGKVLAEG 218
|
.
gi 296439455 1423 S 1423
Cdd:COG1137 219 T 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
391-604 |
5.32e-31 |
|
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: 122.79 E-value: 5.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:cd03295 1 IEFENVTKRYGGGK---KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQ-DPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRII--MELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLalVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLK--EHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
390-604 |
1.09e-30 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 122.09 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT--DMEEI 467
Cdd:COG3638 2 MLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQfnfQFDF---LTVREN--------LRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKL 536
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 537 tlGIA--ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRL-ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG3638 156 --AIAraLVQEPKLILADEPVASLDPKTARQVMDLLRRiAREDGItVVVNLHQVDLARRYADRIIGLRDGRV 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1215-1422 |
1.87e-30 |
|
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: 120.32 E-value: 1.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHdnslkfLGYCPQENS 1291
Cdd:cd03259 9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGrdvTGVPPERRN------IGMVFQDYA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMD 1371
Cdd:cd03259 83 LFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1372 PEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03259 163 AKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
392-608 |
2.04e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 119.08 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNI 471
Cdd:cd03214 1 EVENLSVGYGGRT----VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASL-SPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQfnfqfdfltvreNLRVFakikgiqpkEVEQEVKRIIMELdmqsiqdiiakklSGGQKRKLTLGIAILGDPQVLLL 551
Cdd:cd03214 76 AYVPQ------------ALELL---------GLAHLADRPFNEL-------------SGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 552 DEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
390-609 |
2.11e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNgkTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRK 469
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN-LKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKeveqEVKRIIMEL----DMQSIQDIIAKKLSGGQKRKLTLGIAILG 544
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPK----KMKDIIDDLakkvGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEAdILADRKVFLSNGKLKCAGS 609
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
390-604 |
2.43e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.03 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEIRK 469
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGR---DVTDLPPKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCpqfnFQ----FDFLTVRENLRvFA-KIKGIQPKEVEQEVKRIimeLDMQSIQDIIAKK---LSGGQKRKLTLGIA 541
Cdd:COG3839 76 NIAMV----FQsyalYPHMTVYENIA-FPlKLRKVPKAEIDRRVREA---AELLGLEDLLDRKpkqLSGGQRQRVALGRA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKvdRL---ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRlHR--RLgttTIYVTHDQVEAMTLADRIAVMNDGRI 212
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
392-604 |
2.63e-30 |
|
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: 121.30 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDM--EEI-- 467
Cdd:COG0411 6 EVRGLTKRF----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR---DITGLppHRIar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 ----RKnigfcpqfnFQ----FDFLTVRENLRV----------FAKIKGI-----QPKEVEQEVKRIIMELDMQSIQDII 524
Cdd:COG0411 79 lgiaRT---------FQnprlFPELTVLENVLVaaharlgrglLAALLRLprarrEEREARERAEELLERVGLADRADEP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 525 AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK-------------EHKVDrLIlfstqfMDeadi 591
Cdd:COG0411 150 AGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRrlrdergitilliEHDMD-LV------MG---- 218
|
250
....*....|...
gi 296439455 592 LADRKVFLSNGKL 604
Cdd:COG0411 219 LADRIVVLDFGRV 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
390-609 |
3.86e-30 |
|
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: 126.94 E-value: 3.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL---SVSTEGSATIYNTQLSEITDmEE 466
Cdd:COG1123 4 LLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKNIGFCPQ-FNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGD 545
Cdd:COG1123 81 RGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 546 PQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR--LILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
391-604 |
4.66e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.39 E-value: 4.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT--DMEEIR 468
Cdd:COG2884 2 IRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCpqfnFQfDF-----LTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGG-QKRkltLGI-- 540
Cdd:COG2884 79 RRIGVV----FQ-DFrllpdRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIar 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFST---QFMDEadiLADRKVFLSNGKL 604
Cdd:COG2884 151 ALVNRPELLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIAThdlELVDR---MPKRVLELEDGRL 215
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
391-604 |
5.89e-30 |
|
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: 119.53 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD--MEEIR 468
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQ-----FNFQFdflTVRENLRVFAKIKGIQPKEVEQevKRIIMELDMQSIQD-IIAKK----LSGGQKRKLTL 538
Cdd:cd03257 82 KEIQMVFQdpmssLNPRM---TIGEQIAEPLRIHGKLSKKEAR--KEAVLLLLVGVGLPeEVLNRypheLSGGQRQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 539 GIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKvDRL---ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQ-EELgltLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
405-609 |
6.56e-30 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 119.17 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFDFL 484
Cdd:TIGR03410 11 GQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEvkriIMEL-----DMQSIQdiiAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPDE----IYELfpvlkEMLGRR---GGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 560 PfsrhrvwSLLKE-HKVDRL--------ILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:TIGR03410 164 P-------SIIKDiGRVIRRlraeggmaILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
387-610 |
7.99e-30 |
|
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: 125.79 E-value: 7.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEYNGK-TGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT--D 463
Cdd:COG1123 257 AEPLLEVRNLSKRYPVRgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIGFCPQFNF-QFD-FLTVRENLRVFAKIKGIQPKEveqEVKRIIMELdMQSIQ---DIIAKK---LSGGQKRK 535
Cdd:COG1123 337 LRELRRRVQMVFQDPYsSLNpRMTVGDIIAEPLRLHGLLSRA---ERRERVAEL-LERVGlppDLADRYpheLSGGQRQR 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKvDRL---ILFSTQFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQ-RELgltYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
390-604 |
1.81e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 120.96 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEY------NGKTG-----------KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAT 452
Cdd:COG4586 1 IIEVENLSKTYrvyekePGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 453 I--YNTQLSEItdmeEIRKNIGFCpqfnF-Q-----FDfLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDII 524
Cdd:COG4586 81 VlgYVPFKRRK----EFARRIGVV----FgQrsqlwWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 525 AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR--LILFSTQFMDeaDI--LADRKVFLS 600
Cdd:COG4586 152 VRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERgtTILLTSHDMD--DIeaLCDRVIVID 229
|
....
gi 296439455 601 NGKL 604
Cdd:COG4586 230 HGRI 233
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1224-1422 |
1.97e-29 |
|
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: 117.40 E-value: 1.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1224 NVSFCVKkGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-----SRASV----RQQHdnslkfLGYCPQENSLWP 1294
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdSRKKInlppQQRK------IGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLElYAAVKGLGKEDAaLSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:cd03297 89 HLNVRENLA-FGLKRKRNREDR-ISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1375 QQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03297 167 RLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1221-1429 |
2.48e-29 |
|
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: 117.92 E-value: 2.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLEL---------YAAVKGLGKEDAALS-ISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:cd03219 95 NVMVaaqartgsgLLLARARREEREARErAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1371 DPEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:cd03219 175 NPEETEELAELIRE-LRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
391-572 |
3.43e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 120.57 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME--EIR 468
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQfnfQFDFL---TVREN----LrvfaKIKGIQPKEVEQEVKRIimeLDMQSIQDiiaKK------LSGGQKRK 535
Cdd:COG1135 82 RKIGMIFQ---HFNLLssrTVAENvalpL----EIAGVPKAEIRKRVAEL---LELVGLSD---KAdaypsqLSGGQKQR 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 296439455 536 ltLGIA--ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:COG1135 149 --VGIAraLANNPKVLLCDEATSALDPETTRSILDLLKD 185
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
391-610 |
5.69e-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: 116.49 E-value: 5.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDM---EEI 467
Cdd:cd03218 1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQ---DITKLpmhKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQ 547
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 548 VLLLDEPTAGLDPFSRHRVWSLLKEHKvDRLI--LFSTQFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIgvLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
389-608 |
5.85e-29 |
|
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: 117.11 E-value: 5.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEG-SATIYNTQLSEiTDMEEI 467
Cdd:COG1119 2 PLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGG-EDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFC-PQFNFQFdfltvRENLRV--------FAKIkGIQPK---EVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRK 535
Cdd:COG1119 77 RKRIGLVsPALQLRF-----PRDETVldvvlsgfFDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEadILA--DRKVFLSNGKLKCAG 608
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEE--IPPgiTHVLLLKDGRVVAAG 225
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1217-1417 |
5.97e-29 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 113.88 E-value: 5.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNsLKFLGYCPQenslwpkl 1296
Cdd:cd00267 10 GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 tmkehlelyaavkglgkedaalsisrlvealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:cd00267 81 -------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRE 117
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 296439455 1377 QMWQILQATVKnKERGTLLTTHYMSEAEAVCDRMAMMVSGT 1417
Cdd:cd00267 118 RLLELLRELAE-EGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
383-604 |
7.33e-29 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 124.98 E-value: 7.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 383 PEFHGKeaIRIRNVIKEYNGKTGKveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIt 462
Cdd:TIGR03375 458 PRLQGE--IEFRNVSFAYPGQETP--ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQI- 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 463 DMEEIRKNIGFCPQFNFQFdFLTVRENLRVFAkikgiqPKEVEQEVKRIIME-------------LDMQsiqdiIAKK-- 527
Cdd:TIGR03375 533 DPADLRRNIGYVPQDPRLF-YGTLRDNIALGA------PYADDEEILRAAELagvtefvrrhpdgLDMQ-----IGERgr 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 528 -LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFST---QFMDeadiLADRKVFLSNGK 603
Cdd:TIGR03375 601 sLSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVThrtSLLD----LVDRIIVMDNGR 676
|
.
gi 296439455 604 L 604
Cdd:TIGR03375 677 I 677
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
391-604 |
1.18e-28 |
|
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: 115.04 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqlSEITDMEEIRKN 470
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG---RDVTDLPPKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQfNFQ-FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:cd03301 74 IAMVFQ-NYAlYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03301 153 LMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
390-604 |
2.11e-28 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 118.28 E-value: 2.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEIRK 469
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR---DVTGLPPEKR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCpqfnFQ----FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIimeLDMQSIQDIIAKK---LSGGQKRKLTLGIAI 542
Cdd:COG3842 78 NVGMV----FQdyalFPHLTVAENVAFGLRMRGVPKAEIRARVAEL---LELVGLEGLADRYphqLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKvdRL---ILFST--QfmDEADILADRKVFLSNGKL 604
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRRlQR--ELgitFIYVThdQ--EEALALADRIAVMNDGRI 214
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
391-604 |
6.28e-28 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 116.78 E-value: 6.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATI----YNTQLSeitdmee 466
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLngrdLFTNLP------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRK-NIGFCpqfnFQ----FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIA 541
Cdd:COG1118 72 PRErRVGFV----FQhyalFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG1118 148 LAVEPEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
383-604 |
1.04e-27 |
|
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: 112.63 E-value: 1.04e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 383 PEFHGKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyNTQLSEIT 462
Cdd:cd03220 11 PTYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 463 DMeeirkNIGFCPQfnfqfdfLTVRENLRVFAKIKGIQPKEVEQEVKRIIM--ELDmQSIQDIIaKKLSGGQKRKLTLGI 540
Cdd:cd03220 90 GL-----GGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEfsELG-DFIDLPV-KTYSSGMKARLAFAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03220 156 ATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
391-609 |
1.22e-27 |
|
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: 112.72 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqlSEITDMEEIRKN 470
Cdd:cd03300 1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG---KDITNLPPHKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:cd03300 154 LDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1196-1418 |
1.34e-27 |
|
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: 112.20 E-value: 1.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEYYETKKscfstrkKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASV 1272
Cdd:cd03255 1 IELKNLSKTYGGGGE-------KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdiSKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1273 RQQHDNSLKFLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKR 1346
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGqqqrvaIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1347 klcfvlSILGNPSVVLLDEPfTG-MDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAvCDRMAMMVSGTL 1418
Cdd:cd03255 154 ------ALANDPKIILADEP-TGnLDSETGKEVMELLREL--NKEAGTtiVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1219-1413 |
1.59e-27 |
|
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: 111.86 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrqqhdNSLKFLGYCPQ-ENSLW--Pk 1295
Cdd:cd03235 12 HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVPQrRSIDRdfP- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKE--------HLELYaavKGLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:cd03235 85 ISVRDvvlmglygHKGLF---RRLSKADKAK-VDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPF 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 1368 TGMDPEGQQQMWQILqATVKNKERGTLLTTHYMSEAEAVCDRMAMM 1413
Cdd:cd03235 161 AGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
391-603 |
1.60e-27 |
|
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: 112.66 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEE--IR 468
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCpqfnFQfDF-----LTVREN-----------LRVFAkikGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQ 532
Cdd:cd03256 78 RQIGMI----FQ-QFnlierLSVLENvlsgrlgrrstWRSLF---GLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQ 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 533 KRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:cd03256 150 QQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
391-604 |
4.05e-27 |
|
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: 110.70 E-value: 4.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS-EITDMEEIRK 469
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTdDKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ-FNFqFDFLTVRENLrVFA--KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDP 546
Cdd:cd03262 77 KVGMVFQqFNL-FPHLTVLENI-TLApiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 547 QVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRL-ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMtMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1221-1418 |
5.35e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 111.67 E-value: 5.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQ----------QHdnslkflgycp 1287
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGrdiTGLPPHRiarlgiartfQN----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 qeNSLWPKLTMKEHLEL----------YAAVKGLG---KEDAALS--ISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVL 1352
Cdd:COG0411 88 --PRLFPELTVLENVLVaaharlgrglLAALLRLPrarREEREARerAEELLERVGLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1353 SILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRL--RDERGItiLLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1216-1423 |
6.35e-27 |
|
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: 111.29 E-value: 6.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQE 1289
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGrdlaslSRRELARR-------IAYVPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLWPKLTMKE--------HLELYAavkGLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:COG1120 84 PPAPFGLTVRElvalgrypHLGLFG---RPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1362 LLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1218-1426 |
1.03e-26 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 110.56 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHdnslkfLGYCPQENS------ 1291
Cdd:COG1121 18 GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR------IGYVPQRAEvdwdfp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 ----------LWPKLtmkehlelyAAVKGLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:COG1121 92 itvrdvvlmgRYGRR---------GLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1362 LLDEPFTGMDPEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRmAMMVSGTLRCIGSIQH 1426
Cdd:COG1121 162 LLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1217-1423 |
1.24e-26 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 110.37 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKL 1296
Cdd:PRK10895 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAV-KGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:PRK10895 94 SVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1376 QQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:PRK10895 174 IDIKRIIEH-LRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
391-604 |
1.33e-26 |
|
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: 109.42 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngkTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD--MEEIR 468
Cdd:cd03292 1 IEFINVTKTY---PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:cd03292 78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1213-1418 |
1.56e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 109.52 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSlKFLGYCPQ 1288
Cdd:cd03257 11 FPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGkdlLKLSRRLRKIRR-KEIQMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 E--NSLWPKLTMKEHLE--LYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCFVLSILGNPSVVL 1362
Cdd:cd03257 90 DpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnRYPHE-LSGGQRQRVAIARALALNPKLLI 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1363 LDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03257 169 ADEPTSALDVSVQAQILDLLKKL--QEELGLtlLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
390-604 |
1.69e-26 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 109.89 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEeIRK 469
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA-FRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIgfcpQFNFQ-----FD-FLTVRENLRVFAKIKGIqpKEVEQEVKRIIMELDM-QSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:COG1124 80 RV----QMVFQdpyasLHpRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLI--LFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLtyLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
391-625 |
1.75e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 111.27 E-value: 1.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT---DMEE 466
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKNIGFCPQF-NFQFDFLTVRENLrVFAKIK-GIQPKEVEQEVKRIIMELDMQsiQDIIAK---KLSGGQKRKltlgIA 541
Cdd:PRK13634 83 LRKKVGIVFQFpEHQLFEETVEKDI-CFGPMNfGVSEEDAKQKAREMIELVGLP--EELLARspfELSGGQMRR----VA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 542 ILG----DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRL-ILFSTQFMDEADILADRKVFLSNGKLKCAGS--SLFL 613
Cdd:PRK13634 156 IAGvlamEPEVLVLDEPTAGLDPKGRKEMMEMFYKlHKEKGLtTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFA 235
|
250
....*....|..
gi 296439455 614 KRKWGIGYHLSL 625
Cdd:PRK13634 236 DPDELEAIGLDL 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1216-1422 |
2.48e-26 |
|
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: 108.77 E-value: 2.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAsvrqqhdnSLKFLGYcpqenSLWPK 1295
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS--------SLLGLGG-----GFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:cd03220 99 LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 1376 QQMWQILQATVKNkERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03220 179 EKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
391-604 |
4.59e-26 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 108.54 E-value: 4.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktGKVeALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI--TDMEEIR 468
Cdd:TIGR02315 2 LEVENLSKVYPN--GKQ-ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQ-FNFqFDFLTVRENL---RVFAK--IKGIQ---PKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLG 539
Cdd:TIGR02315 79 RRIGMIFQhYNL-IERLTVLENVlhgRLGYKptWRSLLgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRL-ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:TIGR02315 158 RALAQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGItVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1221-1417 |
4.90e-26 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 116.76 E-value: 4.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRA-----SVRQQhdnslkfLGYCPQENSLWPK 1295
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagdiATRRR-------VGYMSQAFSLYGE 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:NF033858 354 LTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVAR 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 296439455 1376 QQMWQILqATVKNKERGTL-LTTHYMSEAEAvCDRMAMM------VSGT 1417
Cdd:NF033858 434 DMFWRLL-IELSREDGVTIfISTHFMNEAER-CDRISLMhagrvlASDT 480
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
420-608 |
6.11e-26 |
|
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: 107.19 E-value: 6.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEIRKNIGFCPQFNFQFDFLTVRENLRVfAKIKGI 499
Cdd:cd03298 24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV---DVTAAPPADRPVSMLFQENNLFAHLTVEQNVGL-GLSPGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 500 QPKEVEQE-VKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR- 577
Cdd:cd03298 100 KLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETk 179
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 578 -LILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03298 180 mTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
391-604 |
6.28e-26 |
|
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: 105.59 E-value: 6.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitDMEEIRkn 470
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILV---------DGKEVS-- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 igfcpqfnfqfdFLTVREnlrvfAKIKGIQPkeVEQevkriimeldmqsiqdiiakkLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03216 66 ------------FASPRD-----ARRAGIAM--VYQ---------------------LSVGERQMVEIARALARNARLLI 105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKehkvdRL------ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03216 106 LDEPTAALTPAEVERLFKVIR-----RLraqgvaVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
391-609 |
6.48e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 6.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITD----ME 465
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGV---DITDkkvkLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIRKNIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRI--IMELDMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:PRK13637 80 DIRKKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HK-VDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKElHKeYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
391-560 |
6.83e-26 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 107.81 E-value: 6.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDM---EEI 467
Cdd:COG1137 4 LEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGE---DITHLpmhKRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQ 547
Cdd:COG1137 77 RLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170
....*....|...
gi 296439455 548 VLLLDEPTAGLDP 560
Cdd:COG1137 157 FILLDEPFAGVDP 169
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1221-1429 |
8.36e-26 |
|
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: 107.76 E-value: 8.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELyAAVKGLGKEDAALSISRlVEAL--KLQEQLKAPVKTLSEG------IKRKLcfvlsiLGNPSVVLLDEPFTGMDP 1372
Cdd:COG0410 98 NLLL-GAYARRDRAEVRADLER-VYELfpRLKERRRQRAGTLSGGeqqmlaIGRAL------MSRPKLLLLDEPSLGLAP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1373 EGQQQMWQILQATvknKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:COG0410 170 LIVEEIFEIIRRL---NREGVtiLLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1196-1413 |
9.10e-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: 107.17 E-value: 9.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1196 ITASCLHKEYyetkkscFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQ 1275
Cdd:cd03293 1 LEVRNVSKTY-------GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1276 HDNslkfLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL 1355
Cdd:cd03293 72 GPD----RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMM 1413
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
390-604 |
1.04e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 107.82 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVikeyNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL-----SVSTEGSAT-----IYNTQls 459
Cdd:COG1117 11 KIEVRNL----NVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILldgedIYDPD-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 eiTDMEEIRKNIGFCPQ----FNFqfdflTVRENLrVFA-KIKGIQPKE-----VEQ---------EVK-RiimeLDMQs 519
Cdd:COG1117 85 --VDVVELRRRVGMVFQkpnpFPK-----SIYDNV-AYGlRLHGIKSKSeldeiVEEslrkaalwdEVKdR----LKKS- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 520 iqdiiAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFL 599
Cdd:COG1117 152 -----ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFF 226
|
....*
gi 296439455 600 SNGKL 604
Cdd:COG1117 227 YLGEL 231
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1215-1417 |
1.08e-25 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 105.35 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR-ASVRQQHDNSLKFLGYCPQENSLW 1293
Cdd:cd03229 9 RYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDlTDLEDELPPLRRRIGMVFQDFALF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKLTMKEHLELyaavkglgkedaalsisrlvealklqeqlkapvkTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPE 1373
Cdd:cd03229 89 PHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 1374 GQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGT 1417
Cdd:cd03229 135 TRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
388-604 |
1.13e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 113.72 E-value: 1.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEI 467
Cdd:COG1132 337 RGEIEFENVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL-TLESL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQFNFQFDfLTVRENLRvFAKiKGIQPKEVEQ-----EVKRIIMELDmQSIQDIIAK---KLSGGQKRKLTLG 539
Cdd:COG1132 413 RRQIGVVPQDTFLFS-GTIRENIR-YGR-PDATDEEVEEaakaaQAHEFIEALP-DGYDTVVGErgvNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLIL-----FSTqfmdeadIL-ADRKVFLSNGKL 604
Cdd:COG1132 489 RALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIviahrLST-------IRnADRILVLDDGRI 552
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
387-609 |
1.52e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.25 E-value: 1.52e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEY--NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDM 464
Cdd:PRK13633 1 MNEMIKCKNVSYKYesNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKltlgIAIL 543
Cdd:PRK13633 81 WDIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR----VAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 544 G----DPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEAdILADRKVFLSNGKLKCAGS 609
Cdd:PRK13633 157 GilamRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
362-599 |
1.61e-25 |
|
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: 112.77 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 362 EIFENEINPEHSSDDSFEPVSPefhgkeAIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILS 441
Cdd:TIGR02857 299 AVLDAAPRPLAGKAPVTAAPAS------SLEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 442 GLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDfLTVRENLRvFAKiKGIQPKEVEQEVKRI-IMELDmQSI 520
Cdd:TIGR02857 370 GFVDPTEGSIAVNGVPLADA-DADSWRDQIAWVPQHPFLFA-GTIAENIR-LAR-PDASDAEIREALERAgLDEFV-AAL 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 521 QDIIAKK-------LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQfmDEADI-L 592
Cdd:TIGR02857 445 PQGLDTPigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTH--RLALAaL 522
|
....*..
gi 296439455 593 ADRKVFL 599
Cdd:TIGR02857 523 ADRIVVL 529
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
390-609 |
1.93e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 107.91 E-value: 1.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQL---SEITDME 465
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIRKNIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRiimELDMQSIQDIIAKK----LSGGQKRKLTLGI 540
Cdd:PRK13649 82 QIRKKVGLVFQFpESQLFEETVLKDVAFGPQNFGVSQEEAEALARE---KLALVGISESLFEKnpfeLSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
390-616 |
2.02e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.51 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRK 469
Cdd:PRK13647 4 IIEVEDLHFRYKDGT---KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKltlgIAILG---- 544
Cdd:PRK13647 80 KVGLVFQDpDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR----VAIAGvlam 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLKRK 616
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
405-604 |
2.06e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 107.17 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLS-----VSTEGSaTIYNTQ--LSEITDMEEIRKNIGFCPQF 477
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNdlnpeVTITGS-IVYNGHniYSPRTDTVDLRKEIGMVFQQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 478 NFQFDFlTVRENLRVFAKIKGIQPKEVEQEVkrIIMELDMQSIQDII-------AKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:PRK14239 95 PNPFPM-SIYENVVYGLRLKGIKDKQVLDEA--VEKSLKGASIWDEVkdrlhdsALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
391-604 |
2.55e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 109.12 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYN---TQLSEiTDMEEI 467
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdlTALSE-KELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCpqfnFQ-FDFL---TVRENLRVFAKIKGIQPKEVEQEVKRIimeLDMQSIQDiiaKK------LSGGQKRKLT 537
Cdd:PRK11153 81 RRQIGMI----FQhFNLLssrTVFDNVALPLELAGTPKAEIKARVTEL---LELVGLSD---KAdrypaqLSGGQKQRVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 538 LGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEhkVDRL----ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11153 151 IARALASNPKVLLCDEATSALDPATTRSILELLKD--INRElgltIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
409-572 |
4.23e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 105.97 E-value: 4.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEI--------RKnigfcpqfnFQ 480
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGT---DLTGLDEHeiarlgigRK---------FQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 481 ----FDFLTVRENL--------RVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:COG4674 93 kptvFEELTVFENLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKL 172
|
170 180
....*....|....*....|....
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:COG4674 173 LLLDEPVAGMTDAETERTAELLKS 196
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1214-1416 |
6.02e-25 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 104.97 E-value: 6.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1214 STRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQHDNslkfLGYCP 1287
Cdd:cd03258 13 DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGtdltllSGKELRKARRR----IGMIF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 QE-NSLWPKlTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:cd03258 89 QHfNLLSSR-TVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1367 FTGMDPEGQQQMWQILQATvkNKERG--TLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:cd03258 168 TSALDPETTQSILALLRDI--NRELGltIVLITHEMEVVKRICDRVAVMEKG 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
388-653 |
7.29e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 106.25 E-value: 7.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYngKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEI 467
Cdd:PRK13635 3 EEIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEET-VWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQF-NFQFDFLTVRENLrVFA-KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGD 545
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDV-AFGlENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 546 PQVLLLDEPTAGLDPFSRHRVWS---LLKEHKvdRLILFS-TQFMDEAdILADRKVFLSNGKLKCAG--SSLF-----LK 614
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLEtvrQLKEQK--GITVLSiTHDLDEA-AQADRVIVMNKGEILEEGtpEEIFksghmLQ 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 296439455 615 RkwgIGYHLSLhrnemcdTEKITSLIKQH---IPDAKLTTES 653
Cdd:PRK13635 236 E---IGLDVPF-------SVKLKELLKRNgilLPNTYLTMES 267
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
391-560 |
7.32e-25 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 105.08 E-value: 7.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSE-ITDMEEIRK 469
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDsKKDINKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ-FNFqFDFLTVRENLrVFA--KIKGIQPKEVEQEVKRIimeLDMQSIQDIIAK---KLSGGQK-RkltlgIAI 542
Cdd:COG1126 78 KVGMVFQqFNL-FPHLTVLENV-TLApiKVKKMSKAEAEERAMEL---LERVGLADKADAypaQLSGGQQqR-----VAI 147
|
170 180
....*....|....*....|..
gi 296439455 543 ---LG-DPQVLLLDEPTAGLDP 560
Cdd:COG1126 148 araLAmEPKVMLFDEPTSALDP 169
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
390-590 |
8.02e-25 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.53 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRK 469
Cdd:NF033858 1 VARLEGVSHRY----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ---FNFQFDfLTVRENLRVFAKIKGIQPKEVEQevkRIiMEL----DMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:NF033858 77 RIAYMPQglgKNLYPT-LSVFENLDFFGRLFGQDAAERRR---RI-DELlratGLAPFADRPAGKLSGGMKQKLGLCCAL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLlkehkVDRL--------ILFSTQFMDEAD 590
Cdd:NF033858 152 IHDPDLLILDEPTTGVDPLSRRQFWEL-----IDRIraerpgmsVLVATAYMEEAE 202
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
408-625 |
8.32e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 8.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 408 EALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD---MEEIRKNIGFCPQF-NFQFDF 483
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyIRPVRKRIGMVFQFpESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 484 LTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQsiQDIIAK---KLSGGQKRKLTLgIAILG-DPQVLLLDEPTAGLD 559
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQspfQMSGGQMRKIAI-VSILAmNPDIIVLDEPTAGLD 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 560 PFSRHRVWSLLKEHKVD--RLILFSTQFMDEADILADRKVFLSNGKL--KCAGSSLFLKRKWGIGYHLSL 625
Cdd:PRK13646 178 PQSKRQVMRLLKSLQTDenKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKKLADWHIGL 247
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1213-1422 |
1.20e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 102.51 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQhdnsLKFLGYCPQe 1289
Cdd:cd03214 7 VGYGGRTV-LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGkdlASLSPKEL----ARKIAYVPQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 nslwpkltmkehlelyaavkglgkedaALsisrlvEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTG 1369
Cdd:cd03214 81 ---------------------------AL------ELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSH 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1370 MDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03214 128 LDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
415-608 |
1.39e-24 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 103.53 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIyEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQL--SEIT-DMEEIRKNIGFCPQFNFQFDFLTVRENLr 491
Cdd:cd03297 19 FDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 492 VFAkIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK 571
Cdd:cd03297 97 AFG-LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 296439455 572 EHKVDRLI--LFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03297 176 QIKKNLNIpvIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
391-608 |
1.98e-24 |
|
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: 101.62 E-value: 1.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmeEIRKN 470
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDfLTVRENLrvfakikgiqpkeveqevkriimeldmqsiqdiiAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03247 77 ISVLNQRPYLFD-TTLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGKLKCAG 608
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1195-1424 |
2.01e-24 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1195 VITASCLHKEY------YETKKSCFSTRKK-----KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV 1263
Cdd:COG1134 4 MIEVENVSKSYrlyhepSRSLKELLLRRRRtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1264 VLQGSRASVrqqhdnsLKF-LGYCPQenslwpkLTMKEHLELYAAVKGLGKEDaalsISRLVEALK----LQEQLKAPVK 1338
Cdd:COG1134 84 EVNGRVSAL-------LELgAGFHPE-------LTGRENIYLNGRLLGLSRKE----IDEKFDEIVefaeLGDFIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1339 TLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG1134 146 TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 296439455 1419 RCIGSI 1424
Cdd:COG1134 225 VMDGDP 230
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
410-608 |
2.27e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 103.57 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLsVSTEGSATIYNTQlsEITDMEEIRKNIGFCPQFNFQFDFLTVREN 489
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGF-IKPDSGKILLNGK--DITNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 296439455 570 LKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:cd03299 172 LKKirKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1191-1427 |
2.42e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 109.22 E-value: 2.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1191 EEEPVITASCLHKEYYETKKscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG--- 1267
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGK------GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGkdl 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1268 ---SRASVRQQHdnslKFLGYCPQ--ENSLWPKLTMKEHLELYAAVKGLG-KEDAALSISRLVEALKLQEQLK-APVKTL 1340
Cdd:COG1123 330 tklSRRSLRELR----RRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPDLAdRYPHEL 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1341 SEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG1123 406 SGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDL--QRELGLtyLFISHDLAVVRYIADRVAVMYDGRI 483
|
....*....
gi 296439455 1419 RCIGSIQHL 1427
Cdd:COG1123 484 VEDGPTEEV 492
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
389-600 |
3.26e-24 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 103.79 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitDMEEIR 468
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL---------DGVPVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KnigfcPQFN----FQFD----FLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGI 540
Cdd:COG4525 73 G-----PGADrgvvFQKDallpWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLL-----KEHKvdrLILFSTQFMDEADILADRKVFLS 600
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLldvwqRTGK---GVFLITHSVEEALFLATRLVVMS 209
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
405-589 |
3.32e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 101.73 E-value: 3.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS-EITDMEEIRKNIGFCPQF-NFQFD 482
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDySRKGLLERRQRVGLVFQDpDDQLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 483 FLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFS 562
Cdd:TIGR01166 83 AADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180 190
....*....|....*....|....*....|...
gi 296439455 563 RHRVWSLLkehkvDRL------ILFSTQFMDEA 589
Cdd:TIGR01166 163 REQMLAIL-----RRLraegmtVVISTHDVDLA 190
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
391-604 |
4.00e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.00 E-value: 4.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS-EITDMEEIRK 469
Cdd:PRK13639 2 LETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFLTVRENLrVFAKIK-GIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKltlgIAILG--- 544
Cdd:PRK13639 79 TVGIVFQNpDDQLFAPTVEEDV-AFGPLNlGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKR----VAIAGila 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 545 -DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK13639 154 mKPEIIVLDEPTSGLDPMGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
403-604 |
4.42e-24 |
|
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: 103.49 E-value: 4.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 403 KTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME--EIR-KNIGFCPQfNF 479
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElrELRrKKISMVFQ-SF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 Q-FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:cd03294 112 AlLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 559 DPFSRHRVWSLL----KEHKvdRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:cd03294 192 DPLIRREMQDELlrlqAELQ--KTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
391-609 |
5.92e-24 |
|
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: 102.31 E-value: 5.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRKN 470
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFlTVRENLRvFAKiKGIQPKEVEQEVK-----RIIMELDmQSIQDIIAK---KLSGGQKRKLTLGIAI 542
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENIA-YGR-PGATREEVEEAARaanahEFIMELP-EGYDTVIGErgvKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLIL-----FSTqFMDeadilADRKVFLSNGKLKCAGS 609
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST-IEN-----ADRIVVLEDGKIVERGT 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
415-589 |
6.44e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.83 E-value: 6.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtQLSEITDMEeIRKNIGFCPQFnfqfdF-----LTVREN 489
Cdd:NF033858 287 FRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFG-QPVDAGDIA-TRRRVGYMSQA-----FslygeLTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180
....*....|....*....|....
gi 296439455 570 L----KEHKVDrlILFSTQFMDEA 589
Cdd:NF033858 440 LielsREDGVT--IFISTHFMNEA 461
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
390-560 |
7.26e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 7.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS-----EITDM 464
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpSEKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFCPQfnfQFDF---LTVRENLrVFAKIK--GIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLG 539
Cdd:COG4161 78 RLLRQKVGMVFQ---QYNLwphLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180
....*....|....*....|.
gi 296439455 540 IAILGDPQVLLLDEPTAGLDP 560
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDP 174
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
391-605 |
7.73e-24 |
|
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: 101.71 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-KDLHKIGSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFqfdfLTVRENLRVFAKIKGIQPKEVEqEVKRIImelDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:TIGR03740 76 IESPPLYEN----LTARENLKVHTTLLGLPDSRID-EVLNIV---DLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKVDRL-ILFSTQFMDEADILADRKVFLSNGKLK 605
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGItVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
405-612 |
8.33e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 101.88 E-value: 8.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFDFL 484
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRV---FAKikgiqPKEVEQEVKRI---IMELDMQSIQDiiAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:PRK11614 96 TVEENLAMggfFAE-----RDQFQERIKWVyelFPRLHERRIQR--AGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 559 DPFSRHRVWSLLKEHKVDRLILFST-QFMDEADILADRKVFLSNGK--LKCAGSSLF 612
Cdd:PRK11614 169 APIIIQQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENGHvvLEDTGDALL 225
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
390-624 |
9.99e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 102.99 E-value: 9.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYN-GKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT---DME 465
Cdd:PRK13641 2 SIKFENVDYIYSpGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnkNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIRKNIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQsiQDIIAK---KLSGGQKRKLTLGIA 541
Cdd:PRK13641 82 KLRKKVSLVFQFpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLS--EDLISKspfELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEH-KVDRLILFSTQFMDEADILADRKVFLSNGKL--KCAGSSLFLKRKWG 618
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKLikHASPKEIFSDKEWL 239
|
....*.
gi 296439455 619 IGYHLS 624
Cdd:PRK13641 240 KKHYLD 245
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
390-604 |
1.43e-23 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.24 E-value: 1.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQ--LSEITDMEEI 467
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 ---RKNIGFC-PQFNFqFDFLTVRENLrVFA--KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIA 541
Cdd:PRK11124 78 relRRNVGMVfQQYNL-WPHLTVQQNL-IEApcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE---HKVDRLILfsTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRElaeTGITQVIV--THEVEVARKTASRVVYMENGHI 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
390-604 |
5.22e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 104.72 E-value: 5.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRK 469
Cdd:COG1129 4 LLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ-FNfQFDFLTVRENL---RVFAKIKGIQPKEVEQEVKRIIMELDMqSIQ-DIIAKKLSGGQKRKLTLGIAILG 544
Cdd:COG1129 80 GIAIIHQeLN-LVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 545 DPQVLLLDEPTAGLDpfsrhrvwsllkEHKVDRL-------------ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:COG1129 158 DARVLILDEPTASLT------------EREVERLfriirrlkaqgvaIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
410-602 |
5.38e-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: 99.46 E-value: 5.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI-TDMEEIRKNIGFCPqfnfqfdFLTVRE 488
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPgPDRMVVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 489 NlrVFAKIKGIQPKEVEQEVKRIIME-LDMQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSR- 563
Cdd:TIGR01184 74 N--IALAVDRVLPDLSKSERRAIVEEhIALVGLTEAADKRpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRg 151
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 296439455 564 ---HRVWSLLKEHKVDRLILfsTQFMDEADILADRKVFLSNG 602
Cdd:TIGR01184 152 nlqEELMQIWEEHRVTVLMV--THDVDEALLLSDRVVMLTNG 191
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
391-615 |
5.70e-23 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 99.22 E-value: 5.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRKN 470
Cdd:cd03254 3 IEFENVNFSYDEKK---PVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFlTVRENLRVFAKIkgIQPKEVEQEVKRI-----IMEL--DMQSIQDIIAKKLSGGQKRKLTLGIAIL 543
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLGRPN--ATDEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 544 GDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRlilfsTQFMdEADIL-----ADRKVFLSNGKLKCAGS--SLFLKR 615
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGR-----TSII-IAHRLstiknADKILVLDDGKIIEEGThdELLAKK 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
391-627 |
6.08e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.69 E-value: 6.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS-EITDMEEIRK 469
Cdd:PRK13636 6 LKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK13636 83 SVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAG--SSLFLKRKWGIGYHLS 624
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEIMKLLVEmqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLR 242
|
...
gi 296439455 625 LHR 627
Cdd:PRK13636 243 LPR 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
391-560 |
6.86e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 99.78 E-value: 6.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYN-GKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEIR- 468
Cdd:COG1101 2 LELKNLSKTFNpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK---DVTKLPEYKr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 -KNIG--F-------CPQfnfqfdfLTVRENLRVFAK-------IKGIQPKEVEqEVKRIIMELDMqSIQDIIAKK---L 528
Cdd:COG1101 79 aKYIGrvFqdpmmgtAPS-------MTIEENLALAYRrgkrrglRRGLTKKRRE-LFRELLATLGL-GLENRLDTKvglL 149
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 529 SGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDP 181
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
415-629 |
1.58e-22 |
|
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: 100.96 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQL---SEITDMEEIRKNIGFCPQFNFQFDFLTVRENLR 491
Cdd:TIGR02142 18 FTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfdsRKGIFLPPEKRRIGYVFQEARLFPHLSVRGNLR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 492 VfaKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK 571
Cdd:TIGR02142 98 Y--GMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 572 E-HKVDRL-ILFSTQFMDEADILADRKVFLSNGKLKCAGSslfLKRKWGIGYHLSLHRNE 629
Cdd:TIGR02142 176 RlHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGP---IAEVWASPDLPWLARED 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1221-1427 |
1.60e-22 |
|
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: 103.44 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTA---GVVVLQG-----SRASVRQQHdnslkfLGYCPQE--N 1290
Cdd:COG1123 21 AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGrdlleLSEALRGRR------IGMVFQDpmT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 SLWPkLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:COG1123 95 QLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1371 DPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:COG1123 174 DVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
391-608 |
1.68e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 99.06 E-value: 1.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSaTIYNTQLSEITDMEEIRKN 470
Cdd:PRK13648 8 IVFKNVSFQYQSDASF--TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGE-IFYNNQAITDDNFEKLRKH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFC---PQFNF-----QFDFLTVRENLRVfakikgiQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:PRK13648 85 IGIVfqnPDNQFvgsivKYDVAFGLENHAV-------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR--LILFSTQFMDEAdILADRKVFLSNGKLKCAG 608
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEG 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1222-1455 |
1.76e-22 |
|
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: 97.92 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsRASVRQQHDNSLKFLGYcpqenSLWPKLTMKEH 1301
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRMVVFQNY-----SLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LELY--AAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP----EGQ 1375
Cdd:TIGR01184 75 IALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAltrgNLQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1376 QQMWQILQatvkNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIqhLKNKFGRDYLLEIKMKEPtQVEALHTEIL 1455
Cdd:TIGR01184 155 EELMQIWE----EHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI--LEVPFPRPRDRLEVVEDP-SYYDLRNEAL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
390-661 |
1.81e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.10 E-value: 1.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSV---STEGSATIYNTQLSEITdMEE 466
Cdd:PRK13640 5 IVEFKHVSFTY--PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLpddNPNSKITVDGITLTAKT-VWD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKNIGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTL-GIAILG 544
Cdd:PRK13640 82 IREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 545 dPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR-LILFS-TQFMDEADiLADRKVFLSNGKLKCAGSSL-------FLKR 615
Cdd:PRK13640 162 -PKIIILDESTSMLDPAGKEQILKLIRKLKKKNnLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSPVeifskveMLKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 296439455 616 kwgIGYHLSLhrnemcdTEKITSLIKQ---HIPDaklTTESEEKLVYSL 661
Cdd:PRK13640 240 ---IGLDIPF-------VYKLKNKLKEkgiSVPQ---EINTEEKLVQYL 275
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
394-559 |
1.88e-22 |
|
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: 96.54 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSG--LSVSTEGSATIyNTQLSEITdmeeIRKNI 471
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILI-NGRPLDKN----FQRST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 GFCPQFNFQFDFLTVRENLRVFAKIKGiqpkeveqevkriimeldmqsiqdiiakkLSGGQKRKLTLGIAILGDPQVLLL 551
Cdd:cd03232 82 GYVEQQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFL 132
|
....*...
gi 296439455 552 DEPTAGLD 559
Cdd:cd03232 133 DEPTSGLD 140
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1207-1418 |
2.41e-22 |
|
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: 96.56 E-value: 2.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQhdnsLKFLGYC 1286
Cdd:cd03226 1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER----RKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQE-------NSLWpkltmkehLELYaavkgLGKEDAALSISRLVEALKL----QEQLKAPvKTLSEGIKRKLCFVLSIL 1355
Cdd:cd03226 77 MQDvdyqlftDSVR--------EELL-----LGLKELDAGNEQAETVLKDldlyALKERHP-LSLSGGQKQRLAIAAALL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03226 143 SGKDLLIFDEPTSGLDYKNMERVGELIR-ELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1216-1398 |
2.65e-22 |
|
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: 96.27 E-value: 2.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGS-RASVRQQHDNSLKFLGYCPqenSLWP 1294
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTpLAEQRDEPHENILYLGHLP---GLKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGlgkeDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:TIGR01189 87 ELSALENLHFWAAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....*.
gi 296439455 1375 QQQMWQILQATVknkERG--TLLTTH 1398
Cdd:TIGR01189 163 VALLAGLLRAHL---ARGgiVLLTTH 185
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
405-604 |
3.18e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 97.68 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL-----SVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNF 479
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM-DVIELRRRVQMVFQIPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 QFDFLTVRENLRVFAKIKGI--QPKEVEQEVKRIIMELDM-QSIQDII---AKKLSGGQKRKLTLGIAILGDPQVLLLDE 553
Cdd:PRK14247 93 PIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 296439455 554 PTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK14247 173 PTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
417-572 |
3.74e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 103.20 E-value: 3.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 417 IYEGQITAILGHNGAGKSTLLNILSGLS---VSTEGSATIYNTQLseitDMEEIRKNIGFCPQFNFQFDFLTVRENLRVF 493
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSpkgVKGSGSVLLNGMPI----DAKEMRAISAYVQQDDLFIPTLTVREHLMFQ 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 494 A--KIKGIQPKEVEQE-VKRIIMELDMQSIQDII------AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:TIGR00955 124 AhlRMPRRVTKKEKRErVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAY 203
|
....*...
gi 296439455 565 RVWSLLKE 572
Cdd:TIGR00955 204 SVVQVLKG 211
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1217-1422 |
3.77e-22 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 96.17 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR-ASVRQQHDN-SLKFLGYcpqenSLWP 1294
Cdd:cd03301 11 GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvTDLPPKDRDiAMVFQNY-----ALYP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:cd03301 86 HMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1375 QQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:cd03301 166 RVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
415-609 |
6.25e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 99.40 E-value: 6.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntqlsEITDMEEI-------------RKNIGFCpqfnFQ- 480
Cdd:COG4148 20 FTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSG----------RIRLGGEVlqdsargiflpphRRRIGYV----FQe 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 481 ---FDFLTVRENLRvFAkIKGIQPKEVEQEVKRIImelDMQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEP 554
Cdd:COG4148 86 arlFPHLSVRGNLL-YG-RKRAPRAERRISFDEVV---ELLGIGHLLDRRpatLSGGERQRVAIGRALLSSPRLLLMDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 555 TAGLDPFSRHRVWSLLKehkvdRL-------ILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:COG4148 161 LAALDLARKAEILPYLE-----RLrdeldipILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
389-609 |
7.93e-22 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 96.30 E-value: 7.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEY------------------NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGS 450
Cdd:COG1134 3 SMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 451 ATIyNTQLSEITDMeeirkNIGFCPQfnfqfdfLTVRENLRVFAKIKGIQPKEVEQEVKRIImelDMQSIQDII---AKK 527
Cdd:COG1134 83 VEV-NGRVSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEKFDEIV---EFAELGDFIdqpVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 528 LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKC 606
Cdd:COG1134 147 YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESgRTVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
...
gi 296439455 607 AGS 609
Cdd:COG1134 227 DGD 229
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
390-609 |
8.67e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.00 E-value: 8.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEeirK 469
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDFLTVREN----LRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGD 545
Cdd:PRK10851 75 KVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 546 PQVLLLDEPTAGLDPFSRH--RVW--SLLKEHKVDRliLFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKelRRWlrQLHEELKFTS--VFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
409-609 |
1.14e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 97.11 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYN---TQLSEITDMEEIRKNIGFCPQF-NFQFDFL 484
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRKKVGVVFQFpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEVKRiimELDMQSIQDIIAKK----LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:PRK13643 101 TVLKDVAFGPQNFGIPKEKAEKIAAE---KLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 561 FSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK13643 178 KARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1221-1423 |
1.31e-21 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 98.25 E-value: 1.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAS-VRQQHDNslkfLGYCPQENSLWPKLTMK 1299
Cdd:COG3842 20 ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTgLPPEKRN----VGMVFQDYALFPHLTVA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 EHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPFTGMDPE 1373
Cdd:COG3842 96 ENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGqqqrvaLARALAP------EPRVLLLDEPLSALDAK 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1374 GQQQMwqilQATVKN--KERG--TLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG3842 170 LREEM----REELRRlqRELGitFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
391-604 |
1.61e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 97.08 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSA------------------ 451
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 452 -----TIYNTQLSEITDMEEIRKNIGFCPQF-NFQFDFLTVRENLrVFAKIK-GIQPKEVEQEVKRIIMELDM-QSIQDI 523
Cdd:PRK13651 83 vleklVIQKTRFKKIKKIKEIRRRVGVVFQFaEYQLFEQTIEKDI-IFGPVSmGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 524 IAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNG 602
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 296439455 603 KL 604
Cdd:PRK13651 242 KI 243
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1207-1435 |
1.64e-21 |
|
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: 96.17 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQ--QHDN 1278
Cdd:cd03294 25 KSKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGqdiaamSRKELRElrRKKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1279 SLKFlgycpQENSLWPKLTMKEHLELYAAVKGLGKEDaalSISRLVEALK---LQEQLKAPVKTLSEGIKRKLCFVLSIL 1355
Cdd:cd03294 105 SMVF-----QSFALLPHRTVLENVAFGLEVQGVPRAE---REERAAEALElvgLEGWEHKYPDELSGGMQQRVGLARALA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRDY 1435
Cdd:cd03294 177 VDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
420-605 |
2.27e-21 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 94.16 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyNTQlsEITDMEEIRKNIGFCPQFNFQFDFLTVRENLRVfakikGI 499
Cdd:TIGR01277 24 GEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKV-NDQ--SHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGL-----GL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 500 QP-----KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-- 572
Cdd:TIGR01277 96 HPglklnAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQlc 175
|
170 180 190
....*....|....*....|....*....|...
gi 296439455 573 HKVDRLILFSTQFMDEADILADRKVFLSNGKLK 605
Cdd:TIGR01277 176 SERQRTLLMVTHHLSDARAIASQIAVVSQGKIK 208
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
387-711 |
2.28e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 97.50 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTllnilSGLSVSTEGSATIYNTQ--LSEITDM 464
Cdd:NF000106 10 ARNAVEVRGLVKHF----GEVKAVDGVDLDVREGTVLGVLGP*GAA**R-----GALPAHV*GPDAGRRPWrf*TWCANR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFC-PQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAIL 543
Cdd:NF000106 81 RALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 544 GDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLKRKWGiGYH 622
Cdd:NF000106 161 GRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 623 LSLHRNEMCDTEKITSLIKQHIPD--AKLTTESEEKLVySLPLEKTNKFPDLYSDLdkcsdqGIRNYAVS-----VTSLN 695
Cdd:NF000106 240 LQIRPAHAAELDRMVGAIAQAGLDgiAGATADHEDGVV-NVPIVSDEQLSAVVGML------GERGFTISghqhpSAQL* 312
|
330
....*....|....*.
gi 296439455 696 EVFLNLEGKSAIDEPD 711
Cdd:NF000106 313 EVFLAITGQKTSEAAD 328
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
390-604 |
3.45e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 94.82 E-value: 3.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATI----------YNTQLS 459
Cdd:PRK11264 3 AIEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtarsLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 EItdmEEIRKNIGFCPQ-FNFqFDFLTVRENLRVFAKI-KGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLT 537
Cdd:PRK11264 79 LI---RQLRQHVGFVFQnFNL-FPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 538 LGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL---LKEHKvdRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTirqLAQEK--RTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1218-1436 |
4.17e-21 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 93.94 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVR--QQHDnslkfLGYCPQENSLWPK 1295
Cdd:cd03299 11 KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLppEKRD-----ISYVPQNYALFPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:cd03299 86 MTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1376 QQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQ----HLKNKFGRDYL 1436
Cdd:cd03299 166 EKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEevfkKPKNEFVAEFL 230
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1213-1436 |
5.14e-21 |
|
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: 93.90 E-value: 5.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSL-KFLGYCPQENS 1291
Cdd:cd03295 8 KRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE--DIREQDPVELrRKIGYVIQQIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKA---PvKTLSEGIKRKLCFVLSILGNPSVVLLDEPFT 1368
Cdd:cd03295 86 LFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFAdryP-HELSGGQQQRVGVARALAADPPLLLMDEPFG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1369 GMDP----EGQQQMWQILQATVKNkergTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS----IQHLKNKFGRDYL 1436
Cdd:cd03295 165 ALDPitrdQLQEEFKRLQQELGKT----IVFVTHDIDEAFRLADRIAIMKNGEIVQVGTpdeiLRSPANDFVAEFV 236
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
389-609 |
5.22e-21 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.45 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIR 468
Cdd:PRK13548 1 AMLEARNLSVRLGGRT----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQ-FNFQFDFlTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQK------RKLTLGIA 541
Cdd:PRK13548 76 RRRAVLPQhSSLSFPF-TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKehkvdrlilfstQFMDEAD-----IL---------ADRKVFLSNGKLKCA 607
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLAHQHHVLRLAR------------QLAHERGlavivVLhdlnlaaryADRIVLLHQGRLVAD 222
|
..
gi 296439455 608 GS 609
Cdd:PRK13548 223 GT 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
405-573 |
5.41e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.63 E-value: 5.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATiYNTQLSEITDMEEIRKNIGfcPQfNFQFDFL 484
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIK-LDGGDIDDPDVAEACHYLG--HR-NAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEVKRIimelDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:PRK13539 89 TVAENLEFWAAFLGGEELDIAAALEAV----GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
....*....
gi 296439455 565 RVWSLLKEH 573
Cdd:PRK13539 165 LFAELIRAH 173
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
390-599 |
5.47e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 94.33 E-value: 5.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNgkTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLS-----VSTEGSATIYNTQLSEI-TD 463
Cdd:PRK14258 7 AIKVNNLSFYYD--TQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNeleseVRVEGRVEFFNQNIYERrVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIGFC-PQFNFqFDfLTVRENLRVFAKIKGIQPK-EVEQEVKRIIMELDM-QSIQDIIAK---KLSGGQKRKLT 537
Cdd:PRK14258 83 LNRLRRQVSMVhPKPNL-FP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwDEIKHKIHKsalDLSGGQQQRLC 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 538 LGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKV--DRLILFSTQFMDEADILADRKVFL 599
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLrsELTMVIVSHNLHQVSRLSDFTAFF 224
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
1218-1444 |
6.51e-21 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 94.42 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQ--ENSLwpk 1295
Cdd:TIGR04520 14 EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWEIRKKVGMVFQnpDNQF--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 ltmkehlelyaaVKGLGKEDAALS-----------ISRLVEALK---LQEQLKAPVKTLSEGIKRKLCfVLSILG-NPSV 1360
Cdd:TIGR04520 91 ------------VGATVEDDVAFGlenlgvpreemRKRVDEALKlvgMEDFRDREPHLLSGGQKQRVA-IAGVLAmRPDI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1361 VLLDEPfTGM-DPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAeAVCDRMAMMVSGTLRCIGSIQHLknkFGR-DYL 1436
Cdd:TIGR04520 158 IILDEA-TSMlDPKGRKEVLETIRKL--NKEEGItvISITHDMEEA-VLADRVIVMNKGKIVAEGTPREI---FSQvELL 230
|
....*...
gi 296439455 1437 LEIKMKEP 1444
Cdd:TIGR04520 231 KEIGLDVP 238
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
361-570 |
6.77e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.59 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 361 HEIFENEINPEHSSDDSFEPVSPEFHGKEAIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNIL 440
Cdd:TIGR02868 305 ERIVEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLSAGYPGAP---PVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 441 SGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDfLTVRENLRVFAKikGIQPKEVEQEVKRIIMELDMQSI 520
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSL-DQDEVRRRVSVCAQDAHLFD-TTVRENLRLARP--DATDEELWAALERVGLADWLRAL 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 521 QDII-------AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLL 570
Cdd:TIGR02868 458 PDGLdtvlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDL 514
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
395-609 |
6.90e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 93.42 E-value: 6.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 395 NVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFC 474
Cdd:PRK10895 8 NLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 475 PQFNFQFDFLTVRENLRVFAKI-KGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDE 553
Cdd:PRK10895 84 PQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 554 PTAGLDPFSRHRVWSLLkEHKVDR--LILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK10895 164 PFAGVDPISVIDIKRII-EHLRDSglGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
387-605 |
8.54e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 8.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyNTQLseitdmee 466
Cdd:COG0488 312 GKKVLELEGLSKSYGDKT----LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 irkNIGFCPQFNFQFDfltvrENLRVFAKIKGIQPKEVEQEVkRIIMEL-----DMqsiQDIIAKKLSGGQKRKLTLGIA 541
Cdd:COG0488 379 ---KIGYFDQHQEELD-----PDKTVLDELRDGAPGGTEQEV-RGYLGRflfsgDD---AFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE---------HkvDRlilfstQFMDEadiLADRKVFLSNGKLK 605
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgtvllvsH--DR------YFLDR---VATRILEFEDGGVR 508
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
388-604 |
8.84e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 93.75 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL-----SVSTEGSATIYNTQL-SEI 461
Cdd:PRK14267 2 KFAIETVNLRVYY----GSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 462 TDMEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQ------PKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRK 535
Cdd:PRK14267 78 VDPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALWDEVKDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1221-1437 |
1.28e-20 |
|
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: 98.75 E-value: 1.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQENSLWP 1294
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqiDPASLRRQ-------IGVVLQDVFLFS 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KlTMKEHLelyaavkGLGKEDAalSISRLVEALK----------LQEQLKAPV----KTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:COG2274 563 G-TIRENI-------TLGDPDA--TDEEIIEAARlaglhdfieaLPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSEAEAvCDRMAMMVSGTLRCIGSIQHLKNKFGRDYLL 1437
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
390-560 |
1.71e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.02 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsaTIY-NTQLSEITD-MEEI 467
Cdd:COG3845 5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--EILiDGKPVRIRSpRDAI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQfNFQ-FDFLTVRENLRVFAKIKG---IQPKEVEQEVKRII----MELDMqsiqDIIAKKLSGGQKRKLTlg 539
Cdd:COG3845 79 ALGIGMVHQ-HFMlVPNLTVAENIVLGLEPTKggrLDRKAARARIRELSerygLDVDP----DAKVEDLSVGEQQRVE-- 151
|
170 180
....*....|....*....|...
gi 296439455 540 I--AILGDPQVLLLDEPTAGLDP 560
Cdd:COG3845 152 IlkALYRGARILILDEPTAVLTP 174
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
405-573 |
2.93e-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: 90.50 E-value: 2.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmeEIRKNIGFCPQFNFQFDFL 484
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD--EPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEVKRIimelDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAV----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
....*....
gi 296439455 565 RVWSLLKEH 573
Cdd:TIGR01189 165 LLAGLLRAH 173
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
391-609 |
3.15e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 92.56 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngkTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:PRK13652 4 IETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIK-GIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK13652 80 VGLVFQNPDDQIFSPTVEQDIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKEHKVD--RLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK13652 160 VLDEPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGT 221
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1223-1398 |
3.63e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 90.25 E-value: 3.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR-ASVRQQHDNSLKFLGYCPQENSLwpkLTMKEH 1301
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPiRRQRDEYHQDLLYLGHQPGIKTE---LTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LELYAAVKGLGKEDAALSIsrlVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQI 1381
Cdd:PRK13538 95 LRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
170
....*....|....*....
gi 296439455 1382 LQATVknkERG--TLLTTH 1398
Cdd:PRK13538 172 LAQHA---EQGgmVILTTH 187
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
387-609 |
3.84e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 93.38 E-value: 3.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEYNGKT-GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEG---------------- 449
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 450 SATIYNTQlSEITDMEEIRKNIGFCPQF-NFQFDFLTVRENLrVFAKIK-GIQPKEVEQEVKRII--MELDmQSIQDIIA 525
Cdd:PRK13631 98 ELITNPYS-KKIKNFKELRRRVSMVFQFpEYQLFKDTIEKDI-MFGPVAlGVKKSEAKKLAKFYLnkMGLD-DSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 526 KKLSGGQKRKltlgIAILG----DPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLS 600
Cdd:PRK13631 175 FGLSGGQKRR----VAIAGilaiQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMD 250
|
....*....
gi 296439455 601 NGKLKCAGS 609
Cdd:PRK13631 251 KGKILKTGT 259
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
405-600 |
4.44e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 91.77 E-value: 4.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLL---NILSGL--SVSTEGSATIYNTQL--SEItDMEEIRKNIGFCPQF 477
Cdd:PRK14243 21 GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLipGFRVEGKVTFHGKNLyaPDV-DPVEVRRRIGMVFQK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 478 NFQFDfLTVRENLRVFAKIKGIQ---PKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEP 554
Cdd:PRK14243 100 PNPFP-KSIYDNIAYGARINGYKgdmDELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 555 TAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLS 600
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFN 224
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
391-609 |
5.16e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.97 E-value: 5.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN 470
Cdd:PRK13644 2 IRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADIlADRKVFLSNGKLKCAGS 609
Cdd:PRK13644 159 IFDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
391-609 |
8.60e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.61 E-value: 8.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYN----TQLSEITDME 465
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIRKNIGFCPQF-NFQFDFLTVRENLrVFAKIK-GIQPKEVEQEVKRIimeLDMQSIQDIIAKK----LSGGQKRKLTLG 539
Cdd:PRK13645 87 RLRKEIGLVFQFpEYQLFQETIEKDI-AFGPVNlGENKQEAYKKVPEL---LKLVQLPEDYVKRspfeLSGGQKRRVALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLL----KEHKvdRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK13645 163 GIIAMDGNTLVLDEPTGGLDPKGEEDFINLFerlnKEYK--KRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1223-1429 |
1.24e-19 |
|
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: 89.87 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSLKFlGYCPQENSLWPKLT-- 1297
Cdd:cd03261 17 KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGediSGLSEAELYRLRRRM-GMLFQSGALFDSLTvf 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 ------MKEHLELYAAVkglgkedaalsISRLVeALKLQE-QLKAPVK----TLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:cd03261 96 envafpLREHTRLSEEE-----------IREIV-LEKLEAvGLRGAEDlypaELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1367 FTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1215-1375 |
1.25e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSrASVRQQHDNSLKFLGYcpqENSLWP 1294
Cdd:PRK13539 11 VRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGG-DIDDPDVAEACHYLGH---RNAMKP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGlgkeDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:PRK13539 87 ALTVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAA 162
|
.
gi 296439455 1375 Q 1375
Cdd:PRK13539 163 V 163
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
391-559 |
1.30e-19 |
|
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: 89.60 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRKN 470
Cdd:cd03253 1 IEFENVTFAYDPG---RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQ----FNfqfDflTVRENLRvFAKIkGIQPKEVEQEVKRIImeldmqsIQDIIAK--------------KLSGGQ 532
Cdd:cd03253 77 IGVVPQdtvlFN---D--TIGYNIR-YGRP-DATDEEVIEAAKAAQ-------IHDKIMRfpdgydtivgerglKLSGGE 142
|
170 180
....*....|....*....|....*..
gi 296439455 533 KRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALD 169
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
391-609 |
1.31e-19 |
|
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: 89.09 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:cd03244 3 IEFKNVSLRYRP--NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI-GLHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFlTVRENL---------RVFAKIKGIQPKE-VEQEVKRIIMELDMQSiqdiiaKKLSGGQKRKLTLGI 540
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLdpfgeysdeELWQALERVGLKEfVESLPGGLDTVVEEGG------ENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQ----FMDeadilADRKVFLSNGKLKCAGS 609
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKGRVVEFDS 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1221-1423 |
1.45e-19 |
|
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: 87.10 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRasvrqqhdnslkflgycpqenslwpkltmke 1300
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKE------------------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 hlelyaaVKGLGKEDA-ALSIsrlvealklqeqlkAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMW 1379
Cdd:cd03216 64 -------VSFASPRDArRAGI--------------AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLF 122
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 1380 QILqATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGtlRCIGS 1423
Cdd:cd03216 123 KVI-RRLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
405-609 |
1.86e-19 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 89.79 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIT--DMEEIRkniGFCPQF-NFQF 481
Cdd:COG4559 12 GGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSpwELARRR---AVLPQHsSLAF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 DFlTVRENLRvFAKIKGIQPKEVEQEVKRIIMEL-DMQSIQDIIAKKLSGGQK------RKLT-LGIAILGDPQVLLLDE 553
Cdd:COG4559 89 PF-TVEEVVA-LGRAPHGSSAAQDRQIVREALALvGLAHLAGRSYQTLSGGEQqrvqlaRVLAqLWEPVDGGPRWLFLDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 554 PTAGLDPFSRHRVWSLLKEHKVDRLILFStqfmdeadIL---------ADRKVFLSNGKLKCAGS 609
Cdd:COG4559 167 PTSALDLAHQHAVLRLARQLARRGGGVVA--------VLhdlnlaaqyADRILLLHQGRLVAQGT 223
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
391-609 |
1.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 90.18 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK13650 83 IGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFS-TQFMDEAdILADRKVFLSNGKLKCAGS 609
Cdd:PRK13650 163 ILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTST 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1216-1398 |
2.08e-19 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 88.57 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSLKFL----GYCPQENS 1291
Cdd:COG2884 12 PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNG--QDLSRLKRREIPYLrrriGVVFQDFR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKGLGKEDAAlsiSRLVEALK---LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFT 1368
Cdd:COG2884 90 LLPDRTVYENVALPLRVTGKSRKEIR---RRVREVLDlvgLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 1369 GMDPEgqqQMWQILQATVKNKERGT--LLTTH 1398
Cdd:COG2884 167 NLDPE---TSWEIMELLEEINRRGTtvLIATH 195
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
391-622 |
2.45e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.63 E-value: 2.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEeirKN 470
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 551 LDEPTAGLDPFSR--HRVwSLLKEHK-VDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSSLFLkrkwgigYH 622
Cdd:PRK11000 157 LDEPLSNLDAALRvqMRI-EISRLHKrLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
393-559 |
2.64e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 2.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATiyntqlseitdmeeIRKN-- 470
Cdd:COG0488 1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS--------------IPKGlr 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVREN-LRVFAKIkgiqpKEVEQEVKRIIMELDMQS--------IQDIIA---------------- 525
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTvLDGDAEL-----RALEAELEELEAKLAEPDedlerlaeLQEEFEalggweaearaeeils 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 526 -------------KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:COG0488 138 glgfpeedldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
391-603 |
3.06e-19 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 88.27 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktgkvEALQgifFD--IYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDME-EI 467
Cdd:COG3840 2 LRLDDLTYRYGD-----FPLR---FDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ---DLTALPpAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RK-NIGFcpQFNFQFDFLTVRENLRVfakikGIQP--KEVEQEVKRIIMELDMQSIQDIIAKK---LSGGQKRKLTLGIA 541
Cdd:COG3840 71 RPvSMLF--QENNLFPHLTVAQNIGL-----GLRPglKLTAEQRAQVEQALERVGLAGLLDRLpgqLSGGQRQRVALARC 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:COG3840 144 LVRKRPILLLDEPFSALDPALRQEMLDLVDElcRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
410-573 |
3.10e-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: 87.55 E-value: 3.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmeEIRKNIGFCPQFNFQFDFLTVREN 489
Cdd:cd03231 16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD--SIARGLLYLGHAPGIKTTLSVLEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKGiqpkevEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:cd03231 94 LRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEA 167
|
....
gi 296439455 570 LKEH 573
Cdd:cd03231 168 MAGH 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1221-1398 |
3.13e-19 |
|
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: 87.85 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFL----GYCPQENSLWPKL 1296
Cdd:cd03292 16 ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQ--DVSDLRGRAIPYLrrkiGVVFQDFRLLPDR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEgqq 1376
Cdd:cd03292 94 NVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD--- 170
|
170 180
....*....|....*....|....
gi 296439455 1377 QMWQILQATVKNKERGT--LLTTH 1398
Cdd:cd03292 171 TTWEIMNLLKKINKAGTtvVVATH 194
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
391-560 |
3.43e-19 |
|
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: 86.50 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:cd03246 1 LEVENVSFRYPG--AEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQfnfqfdfltvreNLRVFAKikgiqpkeveqevkriimeldmqSIQDIIakkLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03246 78 VGYLPQ------------DDELFSG-----------------------SIAENI---LSGGQRQRLGLARALYGNPRILV 119
|
170
....*....|
gi 296439455 551 LDEPTAGLDP 560
Cdd:cd03246 120 LDEPNSHLDV 129
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
391-612 |
3.85e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 89.38 E-value: 3.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNgKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:PRK13642 5 LEVENLVFKYE-KESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQF-NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK13642 83 IGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEAdILADRKVFLSNGKL--KCAGSSLF 612
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
422-609 |
4.64e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 4.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 422 ITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeitDMEE-I-----RKNIGFCpqfnFQ----FDFLTVRENLR 491
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLF---DAEKgIclppeKRRIGYV----FQdarlFPHYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 492 VfakikGIQPKEVEQeVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK 571
Cdd:PRK11144 99 Y-----GMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 296439455 572 E--HKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK11144 173 RlaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1219-1423 |
6.33e-19 |
|
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: 87.68 E-value: 6.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR-----ASVRQqhdnslkfLGYCPQENSLW 1293
Cdd:cd03300 13 FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDitnlpPHKRP--------VNTVFQNYALF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPE 1373
Cdd:cd03300 85 PHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLK 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1374 GQQQMwqilQATVKNKERGTLLT----THYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:cd03300 165 LRKDM----QLELKRLQKELGITfvfvTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
390-559 |
1.40e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 89.13 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQlseITDMEEIRK 469
Cdd:PRK11650 3 GLKLQAVRKSYDGKT---QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRV---VNELEPADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCpqfnFQ----FDFLTVRENLRVFAKIKGIQPKEVEQEVKRI--IMELDmqsiqDIIAKK---LSGGQKRKLTLGI 540
Cdd:PRK11650 77 DIAMV----FQnyalYPHMSVRENMAYGLKIRGMPKAEIEERVAEAarILELE-----PLLDRKpreLSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 296439455 541 AILGDPQVLLLDEPTAGLD 559
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
391-608 |
1.46e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 91.00 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN 470
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRV----FAKIKGIQP---KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAIL 543
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 544 GDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
391-559 |
1.56e-18 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 88.57 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL---SVSTEGSATIYNTQLSEIT--DME 465
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKLSekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIR-KNIGFCPQ-----FNfqfDFLTVR----ENLRVFAKIKGiqpKEVEQEVKRIIMELDMQSIQDIIAK---KLSGGQ 532
Cdd:COG0444 82 KIRgREIQMIFQdpmtsLN---PVMTVGdqiaEPLRIHGGLSK---AEARERAIELLERVGLPDPERRLDRyphELSGGM 155
|
170 180
....*....|....*....|....*..
gi 296439455 533 KRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:COG0444 156 RQRVMIARALALEPKLLIADEPTTALD 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1216-1402 |
1.93e-18 |
|
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: 86.68 E-value: 1.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAG-VVVLQGSR---ASVRQ--QHdnslkfLGYCpqE 1289
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERrggEDVWElrKR------IGLV--S 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLwpkltmkeHLELYAAVKGLgkeDAALS-------------------ISRLVEALKLQEQLKAPVKTLSEGIKRKlcf 1350
Cdd:COG1119 85 PAL--------QLRFPRDETVL---DVVLSgffdsiglyreptdeqrerARELLELLGLAHLADRPFGTLSQGEQRR--- 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1351 VL---SILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSE 1402
Cdd:COG1119 151 VLiarALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEE 205
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
387-610 |
2.06e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.64 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEYNGKTGKVeALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL------SVSTEGSATIYNTQLSE 460
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydsKIKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 461 ItDMEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKE-----VEQEVKRIIMELDMQSIQDIIAKKLSGGQKRK 535
Cdd:PRK14246 83 I-DAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1221-1409 |
2.15e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.46 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDnslkfLG----YcpQENSLW 1293
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepvRFRSPRDAQA-----AGiaiiH--QELNLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKLTMKEHLELYAAVKGLG-------KEDAAlsisRLVEALKLQEQLKAPVKTLSEGiKRKLcfVL---SILGNPSVVLL 1363
Cdd:COG1129 92 PNLSVAENIFLGREPRRGGlidwramRRRAR----ELLARLGLDIDPDTPVGDLSVA-QQQL--VEiarALSRDARVLIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1364 DEPFTGMDPEGQQQMWQILQatvKNKERGT--LLTTHYMSEAEAVCDR 1409
Cdd:COG1129 165 DEPTASLTEREVERLFRIIR---RLKAQGVaiIYISHRLDEVFEIADR 209
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
390-604 |
2.31e-18 |
|
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: 85.95 E-value: 2.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEE--- 466
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQ---DLFALDEdar 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 --IR-KNIGFCPQfNFQF-DFLTVRENLRVFAKIKGIqpKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAI 542
Cdd:COG4181 85 arLRaRHVGFVFQ-SFQLlPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR---LILFSTqfmDEAdiLA---DRKVFLSNGKL 604
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIDLLFELNRERgttLVLVTH---DPA--LAarcDRVLRLRAGRL 224
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
391-566 |
2.60e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.29 E-value: 2.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEiTDMEEIRKN 470
Cdd:COG4604 2 IEIKNVSKRYGGKV----VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT-TPSRELAKR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNfqfDF---LTVREnL----RvFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAIL 543
Cdd:COG4604 77 LAILRQEN---HInsrLTVRE-LvafgR-FPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180
....*....|....*....|...
gi 296439455 544 GDPQVLLLDEPTAGLDPfsRHRV 566
Cdd:COG4604 152 QDTDYVLLDEPLNNLDM--KHSV 172
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
389-602 |
2.61e-18 |
|
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: 85.56 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEY-----NGKTgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSaTIYNTQLSEIT- 462
Cdd:COG4778 3 TLLEVENLSKTFtlhlqGGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWVDl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 463 ------DMEEIRKN-IGFCPQFnfqfdfltvrenLRVFAKI------------KGIQPKEVEQEVKRIIMELDmqsiqdi 523
Cdd:COG4778 80 aqasprEILALRRRtIGYVSQF------------LRVIPRVsaldvvaeplleRGVDREEARARARELLARLN------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 524 IAKKL--------SGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTqFMDEA--DILA 593
Cdd:COG4778 141 LPERLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVA 219
|
....*....
gi 296439455 594 DRKVFLSNG 602
Cdd:COG4778 220 DRVVDVTPF 228
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
392-604 |
2.92e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 89.97 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNI 471
Cdd:PRK11288 6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 472 G-------FCPQfnfqfdfLTVRENL---RVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIA 541
Cdd:PRK11288 82 AiiyqelhLVPE-------MTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 542 ILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
394-572 |
3.87e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 3.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME--EIRKN- 470
Cdd:PRK11629 9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaELRNQk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:PRK11629 89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
|
170 180
....*....|....*....|..
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKE 572
Cdd:PRK11629 169 ADEPTGNLDARNADSIFQLLGE 190
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1208-1418 |
4.46e-18 |
|
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: 84.14 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1208 TKKSCFSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTA--GVVVLQGsrasvRQQHDNSLK-FLG 1284
Cdd:cd03213 12 TVKSSPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLING-----RPLDKRSFRkIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1285 YCPQENSLWPKLTMKEHLELYAAVKGlgkedaalsisrlvealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLD 1364
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1365 EPFTGMDPEGQQQMWQILQATVKNKeRGTLLTTHYMS-EAEAVCDRMAMMVSGTL 1418
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTG-RTIICSIHQPSsEIFELFDKLLLLSQGRV 190
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
393-572 |
5.10e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.17 E-value: 5.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEI----R 468
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALaqlrR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK10535 86 EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180
....*....|....*....|....
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQ 189
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
387-604 |
5.54e-18 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 5.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEY-NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSatiYNTQL-SEITDM 464
Cdd:TIGR03269 276 GEPIIKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE---VNVRVgDEWVDM 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIR--------KNIGFCPQFNFQFDFLTVRENLrvfAKIKGIQ-PKEVeqEVKRIIMELDM--------QSIQDIIAKK 527
Cdd:TIGR03269 353 TKPGpdgrgrakRYIGILHQEYDLYPHRTVLDNL---TEAIGLElPDEL--ARMKAVITLKMvgfdeekaEEILDKYPDE 427
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 528 LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVW-SLLKEHK-VDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREeMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
391-603 |
6.30e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 6.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeitDMEEIRKN 470
Cdd:PRK11607 20 LEIRNLTKSFDGQ----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS---HVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 551 LDEPTAGLDPFSRHR----VWSLLKehKVDRLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:PRK11607 173 LDEPMGALDKKLRDRmqleVVDILE--RVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
409-599 |
6.52e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 83.44 E-value: 6.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL------SVSTEGSATI-YNTQLSEITDMeeirknigfCPqfnfqf 481
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVlrptsgTVRRAGGARVaYVPQRSEVPDS---------LP------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 dfLTVRENLRV--FAKIKGIQP------KEVEQEVKRI-IMELDMQSIQDiiakkLSGGQKRKLTLGIAILGDPQVLLLD 552
Cdd:NF040873 72 --LTVRDLVAMgrWARRGLWRRltrddrAAVDDALERVgLADLAGRQLGE-----LSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 553 EPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEAdILADRKVFL 599
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELV-RRADPCVLL 191
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
391-572 |
7.03e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN 470
Cdd:PRK15439 12 LCARSISKQYSG----VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLrVFAKIKgiqPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENI-LFGLPK---RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILI 163
|
170 180
....*....|....*....|..
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKE 572
Cdd:PRK15439 164 LDEPTASLTPAETERLFSRIRE 185
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
391-609 |
7.66e-18 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 87.31 E-value: 7.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyNTQlsEITDMEEIRKN 470
Cdd:PRK09452 15 VELRGISKSFDGKE----VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIML-DGQ--DITHVPAENRH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IgfcpqfN--FQ----FDFLTVRENLRVFAKIKgiqpKEVEQEVKRIIME-LDMQSIQDIIAKK---LSGGQKRKLTLGI 540
Cdd:PRK09452 88 V------NtvFQsyalFPHMTVFENVAFGLRMQ----KTPAAEITPRVMEaLRMVQLEEFAQRKphqLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 541 AILGDPQVLLLDEPTAGLDPFSRHRVWSLLK--EHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
315-571 |
7.80e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 90.17 E-value: 7.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 315 ILAFdTLFYLIFTLYFERVLPDKDGHGDSpLFFLKSSFwSKHQNTHHEIFENEINPEHSSDDSFEPVSPEFH-------- 386
Cdd:TIGR00956 675 IIGF-TVFFFFVYILLTEFNKGAKQKGEI-LVFRRGSL-KRAKKAGETSASNKNDIEAGEVLGSTDLTDESDdvndekdm 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 ----GKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSG---LSVSTEGSATIYNTQLS 459
Cdd:TIGR00956 752 ekesGEDIFHWRNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAErvtTGVITGGDRLVNGRPLD 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 eitdmEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKgiQPKEVEQE-----VKRIIMELDMQSIQDII----AKKLSG 530
Cdd:TIGR00956 832 -----SSFQRSIGYVQQQDLHLPTSTVRESLRFSAYLR--QPKSVSKSekmeyVEEVIKLLEMESYADAVvgvpGEGLNV 904
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 296439455 531 GQKRKLTLGIAILGDPQVLL-LDEPTAGLDPFSrhrVWSLLK 571
Cdd:TIGR00956 905 EQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQT---AWSICK 943
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
90-329 |
8.07e-18 |
|
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: 86.67 E-value: 8.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 90 AFQAAINAAIIEVTTNHSVMEELTSVIGINMKIPPFISKGEIMN-EWFHFTCLVSFSSFIYFASL--NVARERG-KFKKL 165
Cdd:pfam12698 115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGyAYYLVGLILMIIILIGAAIIavSIVEEKEsRIKER 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 166 MTVMGLRESAFWLSWGLTYICFIFIMSIFMALVITSIPIvFHTGFMVIFTLYSLYGLSLIALAFLMSVLIRKPMLA-GLA 244
Cdd:pfam12698 195 LLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGI-PFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAqSII 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 245 GFLFTVFWGCLGFTVLYRQLPLSLGWVLSLLSPFAFTAGMAQITHLDNYLSgvifpdpsgdsykMIATFFILAFDTLFYL 324
Cdd:pfam12698 274 GIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWE-------------IAPSLIILLLFAVVLL 340
|
....*
gi 296439455 325 IFTLY 329
Cdd:pfam12698 341 LLALL 345
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
361-578 |
8.21e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.13 E-value: 8.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 361 HEIFENEINPEHSSDDSFEPVSPEfhgkeAIRIRN-VIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNI 439
Cdd:PRK11174 325 VTFLETPLAHPQQGEKELASNDPV-----TIEAEDlEILSPDGKT----LAGPLNFTLPAGQRIALVGPSGAGKTSLLNA 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 440 LSGLsVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQfNFQFDFLTVRENLRvFAKIKgIQPKEVEQEVKRI-IME---- 514
Cdd:PRK11174 396 LLGF-LPYQGSLKINGIELREL-DPESWRKHLSWVGQ-NPQLPHGTLRDNVL-LGNPD-ASDEQLQQALENAwVSEflpl 470
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 515 ----LDMQsIQDIiAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-----------HKVDRL 578
Cdd:PRK11174 471 lpqgLDTP-IGDQ-AAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAasrrqttlmvtHQLEDL 547
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1221-1416 |
8.84e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.79 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSL-KFLGYCPQENSLWpKLTMK 1299
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLDPADLrRNIGYVPQDVTLF-YGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 EHLELyaavkglgkedAALSIS--RLVEALK--------------LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLL 1363
Cdd:cd03245 96 DNITL-----------GAPLADdeRILRAAElagvtdfvnkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1364 DEPFTGMDPEGQQQMWQILQATVknKERGTLLTTHYMSeAEAVCDRMAMMVSG 1416
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRPS-LLDLVDRIIVMDSG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
391-594 |
1.02e-17 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.37 E-value: 1.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQ-LSEITDMEEIRK 469
Cdd:PRK09493 2 IEFKNVSKHF----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKvNDPKVDERLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFC-PQFNFqFDFLTVRENLrVFA--KIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDP 546
Cdd:PRK09493 78 EAGMVfQQFYL-FPHLTALENV-MFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 547 QVLLLDEPTAGLDPFSRHRVWSLLKE------------------HKV-DRLIlfstqFMDEADILAD 594
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDlaeegmtmvivtheigfaEKVaSRLI-----FIDKGRIAED 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
425-610 |
1.03e-17 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 86.01 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 425 ILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlsEITDMEEIRKNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEV 504
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGE---DVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 505 EQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK--EHKVDRLILFS 582
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 296439455 583 TQFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1221-1423 |
1.32e-17 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 83.93 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrqQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:cd03296 17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT---DVPVQERNVGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQL-----KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:cd03296 94 NVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLdwladRYPAQ-LSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1376 QQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:cd03296 173 KELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1221-1427 |
1.34e-17 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 88.28 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQeNSLWP 1294
Cdd:COG4988 352 ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGvdlsdlDPASWRRQ-------IAWVPQ-NPYLF 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLelyaavkGLGKEDAalSISRLVEALK----------LQEQLKAPV----KTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:COG4988 424 AGTIRENL-------RLGRPDA--SDEELEAALEaagldefvaaLPDGLDTPLgeggRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSEAEAvCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1216-1418 |
1.35e-17 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 83.47 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG---CTKPTAGVVVLQGsRASVRQQhdnSLKFLGYCPQENSL 1292
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNG-QPRKPDQ---FQKCVAYVRQDDIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLTMKEHLeLYAAVKGLGKEDAALSISRLVEALKLQEQLKAPV-----KTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:cd03234 93 LPGLTVRETL-TYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1368 TGMDPEGQQQMWQILQATVKnKERGTLLTTHY-MSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLAR-RNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1221-1403 |
2.06e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 81.90 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAsvrqqhdnslkfLGYCPQENSL---WPkLT 1297
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGAR------------VAYVPQRSEVpdsLP-LT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 MKEHLEL-----YAAVKGLGKEDAAlSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:NF040873 74 VRDLVAMgrwarRGLWRRLTRDDRA-AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|.
gi 296439455 1373 EGQQQMWQILQATVKNKeRGTLLTTHYMSEA 1403
Cdd:NF040873 153 ESRERIIALLAEEHARG-ATVVVVTHDLELV 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1217-1413 |
2.21e-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: 81.28 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQEN 1290
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGvdlrdlDLESLRKN-------IAYVPQDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 SLWPKlTMKEHLelyaavkglgkedaalsisrlvealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:cd03228 86 FLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSAL 127
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1371 DPEGQQQMWQILQAtvKNKERGTLLTTHYMSEAEAvCDRMAMM 1413
Cdd:cd03228 128 DPETEALILEALRA--LAKGKTVIVIAHRLSTIRD-ADRIIVL 167
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1444 |
2.40e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 83.89 E-value: 2.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFS-TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVR--------- 1273
Cdd:PRK13632 9 KVENVSFSyPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGitiSKENLKeirkkigii 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1274 -QQHDNslKFLGYCPQ-------ENSLWPKLTMKEHLELYAAVKGlgkedaalsisrlvealkLQEQLKAPVKTLSEGIK 1345
Cdd:PRK13632 89 fQNPDN--QFIGATVEddiafglENKKVPPKKMKDIIDDLAKKVG------------------MEDYLDKEPQNLSGGQK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1346 RKLCfVLSILG-NPSVVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLT-THYMSEAeAVCDRMAMMVSGTLRCIGS 1423
Cdd:PRK13632 149 QRVA-IASVLAlNPEIIIFDESTSMLDPKGKREIKKIMV-DLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
250 260
....*....|....*....|..
gi 296439455 1424 IQH-LKNKfgrDYLLEIKMKEP 1444
Cdd:PRK13632 226 PKEiLNNK---EILEKAKIDSP 244
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1221-1474 |
2.42e-17 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 87.64 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVrqqhdnslkflgycPQENSLWPKLTMKE 1300
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALI--------------AISSGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDpegQQQMWQ 1380
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1381 ILQATVKNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGrDYLLEIKMKEPTQVEALHTEILKLF 1458
Cdd:PRK13545 182 CLDKMNEFKEQGKtiFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYD-EFLKKYNQMSVEERKDFREEQISQF 260
|
250
....*....|....*.
gi 296439455 1459 PQAAWQERYSSLMAYK 1474
Cdd:PRK13545 261 QHGLLQEDQTGRERKR 276
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1192-1422 |
2.62e-17 |
|
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: 87.17 E-value: 2.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1192 EEPVITASCLHKEYYETKKSCFStrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAG-VVVLQGS-- 1268
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVDRGVVK------AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGeVNVRVGDew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1269 ------------RASvrqqhdnslKFLGYCPQENSLWPKLTMKEHLelyaaVKGLGKE-DAALSISRLVEALKL------ 1329
Cdd:TIGR03269 350 vdmtkpgpdgrgRAK---------RYIGILHQEYDLYPHRTVLDNL-----TEAIGLElPDELARMKAVITLKMvgfdee 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1330 --QEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVC 1407
Cdd:TIGR03269 416 kaEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVC 495
|
250
....*....|....*
gi 296439455 1408 DRMAMMVSGTLRCIG 1422
Cdd:TIGR03269 496 DRAALMRDGKIVKIG 510
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1220-1419 |
3.07e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 87.00 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1220 IAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHD-NSLKfLGYCPQENSLWPKLTM 1298
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALG-IGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAAVKGLGKED---AALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:COG3845 98 AENIVLGLEPTKGGRLDrkaARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 1376 QQMWQILQatvKNKERGT--LLTTHYMSEAEAVCDRMAMM----VSGTLR 1419
Cdd:COG3845 178 DELFEILR---RLAAEGKsiIFITHKLREVMAIADRVTVLrrgkVVGTVD 224
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1213-1413 |
3.16e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 84.72 E-value: 3.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKP---TAGVVVLQG---SRASVRQQHDNSLKFLGY 1285
Cdd:COG0444 11 FPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGedlLKLSEKELRKIRGREIQM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1286 CPQE--NSLWPKLTMKEHL-ELYAAVKGLGKEDAalsISRLVEALKLQeQLKAPVKT-------LSEGIKRKLCFVLSIL 1355
Cdd:COG0444 91 IFQDpmTSLNPVMTVGDQIaEPLRIHGGLSKAEA---RERAIELLERV-GLPDPERRldrypheLSGGMRQRVMIARALA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQqmwQILQATVK-NKERGT--LLTTHYMSEAEAVCDRMAMM 1413
Cdd:COG0444 167 LEPKLLIADEPTTALDVTIQA---QILNLLKDlQRELGLaiLFITHDLGVVAEIADRVAVM 224
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
391-603 |
3.66e-17 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.80 E-value: 3.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQlseitdmeeirkN 470
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV------------K 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQfnfqfdfltvrenlrvfakikgiqpkeveqevkriimeldmqsiqdiiakkLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03221 65 IGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 551 LDEPTAGLDPFSRHRVWSLLKEHKvDRLILFS--TQFMDEadiLADRKVFLSNGK 603
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYP-GTVILVShdRYFLDQ---VATKIIELEDGK 144
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1213-1401 |
4.32e-17 |
|
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: 82.27 E-value: 4.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYC 1286
Cdd:cd03254 10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGidirdiSRKSLRSM-------IGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQENSLWPKlTMKEHLEL---YAAVKGLGKEDAALSISRLVEALK--LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLgrpNATDEEVIEAAKEAGAHDFIMKLPngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 296439455 1362 LLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMS 1401
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKG--RTSIIIAHRLS 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
391-611 |
4.83e-17 |
|
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: 86.39 E-value: 4.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLS--VSTEGSaTIYNTQLSEITDMEEIR 468
Cdd:TIGR03269 1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGR-IIYHVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGF-CPQFN-----FQFDFL----TVRENL---------RVFA----------KIKGIQPKEVEQE--VKRIIMELDM 517
Cdd:TIGR03269 76 SKVGEpCPVCGgtlepEEVDFWnlsdKLRRRIrkriaimlqRTFAlygddtvldnVLEALEEIGYEGKeaVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 518 QSIQDI---IAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDR---LILFS--TQFMDEa 589
Cdd:TIGR03269 156 VQLSHRithIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgisMVLTShwPEVIED- 234
|
250 260
....*....|....*....|..
gi 296439455 590 diLADRKVFLSNGKLKCAGSSL 611
Cdd:TIGR03269 235 --LSDKAIWLENGEIKEEGTPD 254
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1219-1448 |
5.00e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 83.53 E-value: 5.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLqGSR---ASVRQQHDNSL-KFLGYCPQ--ENSL 1292
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERvitAGKKNKKLKPLrKKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKlTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCF--VLSIlgNPSVVLLDEPFT 1368
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlaRSPFE-LSGGQMRRVAIagVLAM--EPEVLVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1369 GMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKfgRDYLLEIKMKEPTQVE 1448
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD--PDELEAIGLDLPETVK 252
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
410-605 |
5.68e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 5.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdmEEIR-----KNIGFCPQFNFQFDFL 484
Cdd:PRK10584 26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMD--EEARaklraKHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 565 RV----WSLLKEHKVDrLILFStqfMDEAdiLA---DRKVFLSNGKLK 605
Cdd:PRK10584 184 KIadllFSLNREHGTT-LILVT---HDLQ--LAarcDRRLRLVNGQLQ 225
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1219-1424 |
6.59e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.79 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSL-KFLGYCPQ--ENSLWPK 1295
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIrKKVGLVFQypEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 lTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQ-EQLK--APVKtLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:PRK13637 100 -TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyEDYKdkSPFE-LSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1373 EGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSI 1424
Cdd:PRK13637 178 KGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
405-559 |
8.80e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRKNIGFCPQFNFQFDFL 484
Cdd:PRK11231 13 GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSS-RQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRE--------NLRVFAKIKGIQPKEVEQEVKRI-IMELDMQSIQDiiakkLSGGQKRKLTLGIAILGDPQVLLLDEPT 555
Cdd:PRK11231 92 TVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTrINHLADRRLTD-----LSGGQRQRAFLAMVLAQDTPVVLLDEPT 166
|
....
gi 296439455 556 AGLD 559
Cdd:PRK11231 167 TYLD 170
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
391-623 |
9.45e-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: 81.43 E-value: 9.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTGkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKN 470
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDL-NLRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDfLTVRENLRvFAKIKGIQpKEVEQEVK-----RIIMELdMQSIQDII---AKKLSGGQKRKLTLGIAI 542
Cdd:cd03249 79 IGLVSQEPVLFD-GTIAENIR-YGKPDATD-EEVEEAAKkanihDFIMSL-PDGYDTLVgerGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLIL-----FSTqfmdeadIL-ADRKVFLSNGKLKCAGSSLFLKRK 616
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIviahrLST-------IRnADLIAVLQNGQVVEQGTHDELMAQ 227
|
....*..
gi 296439455 617 WGIGYHL 623
Cdd:cd03249 228 KGVYAKL 234
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
403-609 |
9.87e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.31 E-value: 9.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 403 KTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDME--EIR-KNIGFCPQFNF 479
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrEVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 QFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 560 PFSRHRVW-SLLK-EHKVDRLILFSTQFMDEADILADRKVFLSNGKLKCAGS 609
Cdd:PRK10070 197 PLIRTEMQdELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1437 |
1.65e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 81.77 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHdnslKFL 1283
Cdd:PRK13652 5 ETRDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGepiTKENIREVR----KFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1284 GYC---PQENSLWPklTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:PRK13652 81 GLVfqnPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLknkFGRDYLL 1437
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI---FLQPDLL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1221-1423 |
1.87e-16 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 82.89 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG----SRASVRQQHdnslkfLGYCPQENSLWPKL 1296
Cdd:COG1118 17 LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlfTNLPPRERR------VGFVFQHYALFPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKRklcfVLSIlgNPSVVLLDEPFTGM 1370
Cdd:COG1118 91 TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGqrqrvaLAR----ALAV--EPEVLLLDEPFGAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1371 DPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG1118 165 DAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGT 217
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1215-1416 |
2.01e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 80.90 E-value: 2.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---------SRAS----VRQqhdNSLK 1281
Cdd:COG1101 15 TVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeyKRAKyigrVFQ---DPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1282 flGYCpqenslwPKLTMKEHLELyAAVKG--------LGKEDAALSISRLVE-ALKLQEQLKAPVKTLSEGIKRKLCFVL 1352
Cdd:COG1101 92 --GTA-------PSMTIEENLAL-AYRRGkrrglrrgLTKKRRELFRELLATlGLGLENRLDTKVGLLSGGQRQALSLLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1353 SILGNPSVVLLDEPFTGMDPEGQQqmwQILQAT---VKNKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:COG1101 162 ATLTKPKLLLLDEHTAALDPKTAA---LVLELTekiVEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
361-609 |
2.74e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 2.74e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 361 HEIFENEINPEHSSDDSFEPVSPefhgkeAIRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNIL 440
Cdd:PRK11160 315 NEITEQKPEVTFPTTSTAAADQV------SLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 441 SGLSVSTEGSATIYNTQLSEITDmEEIRKNIGFCPQ----FNfqfdfLTVRENLRvFAKikgiqPKEVEQEVKRIIMELD 516
Cdd:PRK11160 387 TRAWDPQQGEILLNGQPIADYSE-AALRQAISVVSQrvhlFS-----ATLRDNLL-LAA-----PNASDEALIEVLQQVG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 517 MQSIQDIIA----------KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFST--- 583
Cdd:PRK11160 455 LEKLLEDDKglnawlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIThrl 534
|
250 260 270
....*....|....*....|....*....|
gi 296439455 584 ----QFmdeadilaDRKVFLSNGKLKCAGS 609
Cdd:PRK11160 535 tgleQF--------DRICVMDNGQIIEQGT 556
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1213-1398 |
2.80e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 2.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsrasvrqQHDNSLKfLGYCPQENSL 1292
Cdd:PRK09544 14 FGQRR---VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR-IGYVPQKLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPK--LTMKEHLELYAAVKglgKEDAALSISRlVEALKLqeqLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:PRK09544 79 DTTlpLTVNRFLRLRPGTK---KEDILPALKR-VQAGHL---IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151
|
170 180
....*....|....*....|....*...
gi 296439455 1371 DPEGQQQMWQILQATVKNKERGTLLTTH 1398
Cdd:PRK09544 152 DVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1221-1448 |
2.82e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.58 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGycpQENSLWPKLTMKE 1300
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF---QSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMwQ 1380
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRM-Q 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1381 IlqATVKNKER---GTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS----IQHLKNKFGRDYLLEIKMKEPTQVE 1448
Cdd:PRK11607 190 L--EVVDILERvgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFIGSVNVFEGVLKE 262
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1219-1416 |
2.84e-16 |
|
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: 79.92 E-value: 2.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQHDNslkfLGYCPQENSL 1292
Cdd:cd03256 14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGtdinklKGKALRQLRRQ----IGMIFQQFNL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLTMKE---------HLELYAAVKGLGKEDAALSISRLvEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLL 1363
Cdd:cd03256 90 IERLSVLEnvlsgrlgrRSTWRSLFGLFPKEEKQRALAAL-ERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1364 DEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:cd03256 169 DEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
390-602 |
2.91e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 80.51 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI-TDMEEIR 468
Cdd:PRK11248 1 MLQISHLYADYGGK----PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPgAERGVVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNfqfdfltVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK11248 77 QNEGLLPWRN-------VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQFMDEADILADRKVFLSNG 602
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1221-1432 |
3.05e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.09 E-value: 3.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSiKMITGCTKPTAG-----VVVLQGSRASVRQqhdnslKFLGYCPQENSLWPK 1295
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGrrpwrF*TWCANRRALRR------TIG*HRPVR*GRRES 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:NF000106 101 FSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1376 QQMWQILQATVKNKERgTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFG 1432
Cdd:NF000106 181 NEVWDEVRSMVRDGAT-VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1201-1418 |
3.11e-16 |
|
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: 79.11 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1201 LHKEYyetkkscfstrKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSL 1280
Cdd:cd03262 6 LHKSF-----------GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1281 -KFLGYCPQENSLWPKLTMKEHLELyaA---VKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKRKLCF 1350
Cdd:cd03262 75 rQKVGMVFQQFNLFPHLTVLENITL--ApikVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGqqqrvaIARALAM 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1351 vlsilgNPSVVLLDEPFTGMDPEGQQqmwQILQATVKNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03262 153 ------NPKVMLFDEPTSALDPELVG---EVLDVMKDLAEEGMtmVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1220-1436 |
3.42e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.77 E-value: 3.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1220 IAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSLKFLGYCPQENSLWPKL 1296
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGvdiAKISDAELREVRRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1377 QMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGRDYL 1436
Cdd:PRK10070 202 EMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYV 261
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1222-1366 |
3.82e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 83.58 E-value: 3.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLqGSRASVrqqhdnslkflGYCPQEN-SLWPKLTMKE 1300
Cdd:COG0488 331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKI-----------GYFDQHQeELDPDKTVLD 398
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1301 HLelyaavKGLGKEDAALSISRLVEALKL-QEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:COG0488 399 EL------RDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEP 459
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1222-1418 |
4.42e-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: 77.64 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrASVRQQHDNSL-KFLGYCPQENSLWPKltmke 1300
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDG--ADISQWDPNELgDHVGYLPQDDELFSG----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 hlelyaavkglgkedaalSISRLVealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQqmwQ 1380
Cdd:cd03246 91 ------------------SIAENI---------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER---A 134
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 296439455 1381 ILQATVKNKERGT--LLTTHYMSEAEAvCDRMAMMVSGTL 1418
Cdd:cd03246 135 LNQAIAALKAAGAtrIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1222-1444 |
5.49e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 80.16 E-value: 5.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAS-------------VRQQHDNslKFLGycpq 1288
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTeenvwdirhkigmVFQNPDN--QFVG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 enslwpkLTMKEHLELYAAVKGLGKEDAalsISRLVEALKLQEQL----KAPVKtLSEGIKRKLCFVLSILGNPSVVLLD 1364
Cdd:PRK13650 97 -------ATVEDDVAFGLENKGIPHEEM---KERVNEALELVGMQdfkeREPAR-LSGGQKQRVAIAGAVAMRPKIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1365 EPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAeAVCDRMAMMVSGTLRCIGSIQHLknkFGR-DYLLEIKMKE 1443
Cdd:PRK13650 166 EATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL---FSRgNDLLQLGLDI 241
|
.
gi 296439455 1444 P 1444
Cdd:PRK13650 242 P 242
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1221-1430 |
5.68e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 82.91 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsRASVRQQHDNSLKF-LGYCPQENSLWPKLTMK 1299
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINN-INYNKLDHKLAAQLgIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 EHL----ELYAAVKGLGKEDAALSISRLVEALK---LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:PRK09700 99 ENLyigrHLTKKVCGVNIIDWREMRVRAAMMLLrvgLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1373 EGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNK 1430
Cdd:PRK09700 179 KEVDYLFLIMN-QLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND 235
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1217-1416 |
6.87e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 6.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-------------SRAS-VRQQHDNSLkf 1282
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldtsdeenlwdirNKAGmVFQNPDNQI-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1283 lgycpqenslwpkltmkehlelyaaVKGLGKEDAA-----LSI------SRLVEALK---LQEQLKAPVKTLSEGIKRKL 1348
Cdd:PRK13633 99 -------------------------VATIVEEDVAfgpenLGIppeeirERVDESLKkvgMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1349 CFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQilqaTVK--NKERG--TLLTTHYMSEAeAVCDRMAMMVSG 1416
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVN----TIKelNKKYGitIILITHYMEEA-VEADRIIVMDSG 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1192-1427 |
7.17e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 79.67 E-value: 7.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1192 EEPVITASCLHKEYYETKKScfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAS 1271
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATY---------ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLS 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1272 -------------VRQQHDNslKFLGYCPQ-------ENSLWPKLTMKEHLElyAAVKGLGKEDAAlsisrlvealkLQE 1331
Cdd:PRK13635 73 eetvwdvrrqvgmVFQNPDN--QFVGATVQddvafglENIGVPREEMVERVD--QALRQVGMEDFL-----------NRE 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1332 qlkaPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLT-THYMSEAeAVCDRM 1410
Cdd:PRK13635 138 ----PHR-LSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVR-QLKEQKGITVLSiTHDLDEA-AQADRV 210
|
250
....*....|....*..
gi 296439455 1411 AMMVSGTLRCIGSIQHL 1427
Cdd:PRK13635 211 IVMNKGEILEEGTPEEI 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1229-1418 |
8.22e-16 |
|
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: 77.92 E-value: 8.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDN--SLKFlgycpQENSLWPKLTMKEHLELyA 1306
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRpvSMLF-----QENNLFAHLTVEQNVGL-G 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1307 AVKGLG-KEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQAT 1385
Cdd:cd03298 95 LSPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174
|
170 180 190
....*....|....*....|....*....|...
gi 296439455 1386 VKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03298 175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
388-609 |
8.28e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 82.70 E-value: 8.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEI 467
Cdd:PRK13657 332 KGAVEFDDVSFSYDNSR---QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQ----FNfqfdfLTVRENLRVfakikGiQPKEVEQEVKRiimELDMQSIQDIIAKK--------------LS 529
Cdd:PRK13657 408 RRNIAVVFQdaglFN-----RSIEDNIRV-----G-RPDATDEEMRA---AAERAQAHDFIERKpdgydtvvgergrqLS 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 530 GGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRlilfsTQFMDeADIL-----ADRKVFLSNGKL 604
Cdd:PRK13657 474 GGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-----TTFII-AHRLstvrnADRILVFDNGRV 547
|
....*
gi 296439455 605 KCAGS 609
Cdd:PRK13657 548 VESGS 552
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
410-597 |
9.56e-16 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 77.52 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSG-LS--VSTEGSATIYNTqlsEITDMEEIRKNIGFCPQFNFQFDFLTV 486
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtLSpaFSASGEVLLNGR---RLTALPAEQRRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 487 RENLRvFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRV 566
Cdd:COG4136 94 GENLA-FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180 190
....*....|....*....|....*....|...
gi 296439455 567 WSLLKEHKVDRLI--LFSTQfmDEADILADRKV 597
Cdd:COG4136 173 REFVFEQIRQRGIpaLLVTH--DEEDAPAAGRV 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
391-604 |
1.32e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 77.61 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktGKvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEE--IR 468
Cdd:PRK10908 2 IRFEHVSKAYLG--GR-QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNFQFDFLTVRENLRVFAKIKGIQPKEVEqevKRIIMELDMQSIQDiIAK----KLSGGQKRKLTLGIAILG 544
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIR---RRVSAALDKVGLLD-KAKnfpiQLSGGEQQRVGIARAVVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 545 DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK10908 155 KPAVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1192-1418 |
2.03e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 77.55 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1192 EEPVITASCLHKEYYETKKSCFstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---- 1267
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSVQTD-------VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGqpms 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1268 -----SRASVRQQHdnslkfLGYCPQENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSE 1342
Cdd:PRK11629 75 klssaAKAELRNQK------LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1343 GIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVcDRMAMMVSGTL 1418
Cdd:PRK11629 149 GERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL--NRLQGTafLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
391-627 |
2.17e-15 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 81.30 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRKN 470
Cdd:TIGR02203 331 VEFRNVTFRYPGR--DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT-LASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFlTVRENLRvFAKIKGIQPKEVEQEvkriimeLDMQSIQDIIAK--------------KLSGGQKRKL 536
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIA-YGRTEQADRAEIERA-------LAAAYAQDFVDKlplgldtpigengvLLSGGQRQRL 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 537 TLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGKLKCAGS-SLFLKR 615
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRIVERGThNELLAR 557
|
250
....*....|..
gi 296439455 616 KwgiGYHLSLHR 627
Cdd:TIGR02203 558 N---GLYAQLHN 566
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1213-1418 |
2.53e-15 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 78.97 E-value: 2.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQ---------QH 1276
Cdd:COG1135 11 FPTKGGPVtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGvdltalSERELRAarrkigmifQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1277 DNSLK----FlgycpqENSLWPkltmkehLELyaavKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKR 1346
Cdd:COG1135 91 FNLLSsrtvA------ENVALP-------LEI----AGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGqkqrvgIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1347 KLCfvlsilGNPSVVLLDEPFTGMDPEGQQqmwQILQATVK-NKERG-T-LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG1135 154 ALA------NNPKVLLCDEATSALDPETTR---SILDLLKDiNRELGlTiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
409-604 |
2.65e-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: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQ---FDFLT 485
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKReglVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 486 VRENLrvfakikgiqpkeveqevkriimeldmqsiqdIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHR 565
Cdd:cd03215 95 VAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 296439455 566 VWSLLKEHKVDRL--ILFSTQfMDEADILADRKVFLSNGKL 604
Cdd:cd03215 143 IYRLIRELADAGKavLLISSE-LDELLGLCDRILVMYEGRI 182
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1176-1413 |
2.77e-15 |
|
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: 80.79 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1176 AERVQAANALTA-------PNLEEEPVITASCLHKEYYETKkscFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTS 1248
Cdd:TIGR02857 288 ADGVAAAEALFAvldaaprPLAGKAPVTAAPASSLEFSGVS---VAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1249 IKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQENSLWPKlTMKEHLELYAavkglgKEDAALSISR 1322
Cdd:TIGR02857 365 LNLLLGFVDPTEGSIAVNGvpladaDADSWRDQ-------IAWVPQHPFLFAG-TIAENIRLAR------PDASDAEIRE 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1323 LVEALKLQEQLKA-PVKT----------LSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNkeR 1391
Cdd:TIGR02857 431 ALERAGLDEFVAAlPQGLdtpigeggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQG--R 508
|
250 260
....*....|....*....|..
gi 296439455 1392 GTLLTTHYMSEAEAvCDRMAMM 1413
Cdd:TIGR02857 509 TVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1418 |
2.82e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.81 E-value: 2.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG--------SRASVR----- 1273
Cdd:PRK13639 3 ETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikydkkSLLEVRktvgi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1274 --QQHDNSLkflgYCPqenslwpklTMKEHLELYAAVKGLGKEDAAlsiSRLVEALK---LQEQLKAPVKTLSEGIKRKL 1348
Cdd:PRK13639 83 vfQNPDDQL----FAP---------TVEEDVAFGPLNLGLSKEEVE---KRVKEALKavgMEGFENKPPHHLSGGQKKRV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1349 CFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGTL-LTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK13639 147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKEGITIiISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
415-604 |
2.99e-15 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 76.93 E-value: 2.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNtqlSEITDMEEIRKNIGFCPQFNFQFDFLTVRENLRVfa 494
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG---QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 495 kikGIQP-----KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:PRK10771 95 ---GLNPglklnAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 296439455 570 LKEHKVDR---LILFSTQFMDEADIlADRKVFLSNGKL 604
Cdd:PRK10771 172 VSQVCQERqltLLMVSHSLEDAARI-APRSLVVADGRI 208
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1225-1398 |
3.02e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 75.99 E-value: 3.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLKFLGYCPQENSLWPKLTMKEHLEL 1304
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG--PLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1305 YAAVKGLGKEDAALSISRL--VEalklqeqlKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQqmwQIL 1382
Cdd:cd03231 97 WHADHSDEQVEEALARVGLngFE--------DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVA---RFA 165
|
170
....*....|....*...
gi 296439455 1383 QATVKNKERG--TLLTTH 1398
Cdd:cd03231 166 EAMAGHCARGgmVVLTTH 183
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
408-623 |
3.63e-15 |
|
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: 76.76 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 408 EALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSeITDMEEIRKNIGFCPQFNFQFDfLTVR 487
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFN-RSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENLrvfAKIKGIQPKEVEQEVKRI------IMELDmQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:cd03252 94 DNI---ALADPGMSMERVIEAAKLagahdfISELP-EGYDTIVGEQgagLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 559 DPFSRHRVWSLLKEHKVDRLILFSTQFMdEADILADRKVFLSNGKLKCAGSSLFLKRKWGIGYHL 623
Cdd:cd03252 170 DYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
408-609 |
4.13e-15 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 80.94 E-value: 4.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 408 EALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDFlTVR 487
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENLrvfakIKGIQPKEVEQEVKRIimeLDMQSIQDIIAK--------------KLSGGQKRKLTLGIAILGDPQVLLLDE 553
Cdd:TIGR01193 566 ENL-----LLGAKENVSQDEIWAA---CEIAEIKDDIENmplgyqtelseegsSISGGQKQRIALARALLTDSKVLILDE 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 554 PTAGLDPFSRHRVWSLLKEHKvDRLILFSTQFMDEADiLADRKVFLSNGKLKCAGS 609
Cdd:TIGR01193 638 STSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGS 691
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1221-1383 |
5.50e-15 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 76.20 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQ-HDNSLKFL----GYCPQENSLWPK 1295
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFSQKpSEKAIRLLrqkvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:COG4161 97 LTVMENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
....*....
gi 296439455 1375 QQQMWQILQ 1383
Cdd:COG4161 177 TAQVVEIIR 185
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
397-608 |
6.11e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 76.55 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 397 IKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD------------M 464
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkvadknqL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFCPQ-FNFqFDFLTVREN-LRVFAKIKGIQPKEVEQevkRIIMELDMQSIQDIIAKK----LSGGQKRKLTL 538
Cdd:PRK10619 88 RLLRTRLTMVFQhFNL-WSHMTVLENvMEAPIQVLGLSKQEARE---RAVKYLAKVGIDERAQGKypvhLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 539 GIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEgKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEG 234
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
386-604 |
7.30e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 75.59 E-value: 7.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 386 HGKEAIRIRNVIKEYNGKTgKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDME 465
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQY-EHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 466 EIRKNIGFCPQFNFQFDfLTVRENLRVfakikGIQPKEVEqEVKR---------IIMELDMQSIQDIIAK--KLSGGQKR 534
Cdd:cd03248 85 YLHSKVSLVGQEPVLFA-RSLQDNIAY-----GLQSCSFE-CVKEaaqkahahsFISELASGYDTEVGEKgsQLSGGQKQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 535 KLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADiLADRKVFLSNGKL 604
Cdd:cd03248 158 RVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1215-1421 |
7.40e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 7.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQ---ENS 1291
Cdd:PRK09700 272 TSRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKgLGKEDAALSISRLVEALKLQEQLKA-----------PVKTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLK-DGGYKGAMGLFHEVDEQRTAENQREllalkchsvnqNITELSGGNQQKVLISKWLCCCPEV 430
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCI 1421
Cdd:PRK09700 431 IIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
393-604 |
7.76e-15 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 76.25 E-value: 7.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmeEIRknig 472
Cdd:PRK11247 15 LNAVSKRYGERT----VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARE--DTR---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 473 fcpqFNFQFDFL----TVRENlrVFAKIKGIQPKEVEQEVKRIIMEldmQSIQDIIAKkLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK11247 85 ----LMFQDARLlpwkKVIDN--VGLGLKGQWRDAALQALAAVGLA---DRANEWPAA-LSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 549 LLLDEPTAGLDPFSR----HRVWSLLKEHKVDrlILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11247 155 LLLDEPLGALDALTRiemqDLIESLWQQHGFT--VLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1215-1445 |
8.91e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.79 E-value: 8.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVrQQHDNSLKFL----GYCPQ-- 1288
Cdd:PRK13641 16 TPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITP-ETGNKNLKKLrkkvSLVFQfp 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 ENSLWPKlTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK13641 95 EAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLisKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1367 FTGMDPEGQQQMWQILqatvKNKERG---TLLTTHYMSEAEAVCDRMAMMVSGTLrcigsIQHL--KNKFG-RDYLLEIK 1440
Cdd:PRK13641 173 AAGLDPEGRKEMMQLF----KDYQKAghtVILVTHNMDDVAEYADDVLVLEHGKL-----IKHAspKEIFSdKEWLKKHY 243
|
....*
gi 296439455 1441 MKEPT 1445
Cdd:PRK13641 244 LDEPA 248
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1207-1427 |
8.93e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.43 E-value: 8.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1207 ETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-----SRAS---------- 1271
Cdd:PRK13636 7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidySRKGlmklresvgm 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1272 VRQQHDNSLkFLGYCPQENSLWPkLTMkehlelyaavkGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFV 1351
Cdd:PRK13636 87 VFQDPDNQL-FSASVYQDVSFGA-VNL-----------KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1352 LSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV 229
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1195-1418 |
9.33e-15 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 77.53 E-value: 9.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1195 VITASCLHKEYYETKKscfstrkKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------S 1268
Cdd:PRK11153 1 MIELKNISKVFPQGGR-------TIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGqdltalS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1269 RASVRQ---------QHDNSLK----FlgycpqENSLWPkltmkehLELyaavKGLGKEDAALSISRLVEALKLQEQLKA 1335
Cdd:PRK11153 74 EKELRKarrqigmifQHFNLLSsrtvF------DNVALP-------LEL----AGTPKAEIKARVTELLELVGLSDKADR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1336 PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERG--TLLTTHYMSEAEAVCDRMAMM 1413
Cdd:PRK11153 137 YPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRELGltIVLITHEMDVVKRICDRVAVI 214
|
....*
gi 296439455 1414 VSGTL 1418
Cdd:PRK11153 215 DAGRL 219
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1203-1398 |
9.39e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 9.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1203 KEYYETKKSCFSTRK-KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITgCTKPT----AGVVVLQGSRASVRQQHD 1277
Cdd:TIGR00955 21 KQLVSRLRGCFCRERpRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPIDAKEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1278 NSlkflGYCPQENSLWPKLTMKEHLELYAAVK---GLGKEDAALSISRLVEALKLQE------QLKAPVKTLSEGIKRKL 1348
Cdd:TIGR00955 100 IS----AYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKcantriGVPGRVKGLSGGERKRL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 1349 CFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQAtVKNKERGTLLTTH 1398
Cdd:TIGR00955 176 AFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKG-LAQKGKTIICTIH 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1218-1436 |
1.11e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAG-VVVLQGSRASVRqqHDNSL-KFLGYCPQ---ENsL 1292
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGrVEVLGGDMADAR--HRRAVcPRIAYMPQglgKN-L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRK--LCFVLsiLGNPSVVLLDEPFTGM 1370
Cdd:NF033858 90 YPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDEPTTGV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1371 DPEGQQQMWQiLQATVKnKERGT---LLTTHYMSEAEAvCDRMAMMVSGTLRCIGSIQHLKNKFGRDYL 1436
Cdd:NF033858 168 DPLSRRQFWE-LIDRIR-AERPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADTL 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
389-609 |
1.20e-14 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 75.61 E-value: 1.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS--------- 459
Cdd:COG4598 7 PALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 EITDM---EEIRKNIGFCPQ-FNFqFDFLTVRENLrVFAKI--KGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQK 533
Cdd:COG4598 83 VPADRrqlQRIRTRLGMVFQsFNL-WSHMTVLENV-IEAPVhvLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 534 RKLTLGIAILGDPQVLLLDEPTAGLDPfsrHRVWSLLK-------EHkvdRLILFSTQFMDEADILADRKVFLSNGKLKC 606
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDP---ELVGEVLKvmrdlaeEG---RTMLVVTHEMGFARDVSSHVVFLHQGRIEE 234
|
...
gi 296439455 607 AGS 609
Cdd:COG4598 235 QGP 237
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1221-1437 |
1.27e-14 |
|
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: 75.22 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQENSLWP 1294
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGhdlalaDPAWLRRQ-------VGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KlTMKEHLELyaavkglgkEDAALSISRLVEALKLQE------QLKAPVKT--------LSEGIKRKLCFVLSILGNPSV 1360
Cdd:cd03252 90 R-SIRDNIAL---------ADPGMSMERVIEAAKLAGahdfisELPEGYDTivgeqgagLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSEAEAVcDRMAMMVSGTLRCIGSIQHLKNKFGRDYLL 1437
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
403-566 |
1.64e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 74.37 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 403 KTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRKNIGFCPQFNFQF- 481
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYRQQVSYCAQTPTLFg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 DflTVRENLRVFAKIKGIQPKEveqevKRIIMELDMQSIQDIIAKK----LSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:PRK10247 95 D--TVYDNLIFPWQIRNQQPDP-----AIFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
|
....*....
gi 296439455 558 LDPFSRHRV 566
Cdd:PRK10247 168 LDESNKHNV 176
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1222-1398 |
1.79e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.83 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGS-----RASVRQQhdnsLKFLGYcpqENSLWPKL 1296
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQsikkdLCTYQKQ----LCFVGH---RSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLeLYaavkGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDpegQQ 1376
Cdd:PRK13540 90 TLRENC-LY----DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---EL 161
|
170 180
....*....|....*....|....
gi 296439455 1377 QMWQILQATVKNKERG--TLLTTH 1398
Cdd:PRK13540 162 SLLTIITKIQEHRAKGgaVLLTSH 185
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1223-1419 |
1.95e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 1.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsraSVRqqhdnslkfLGYCPQENSLWPKLT----- 1297
Cdd:COG0488 15 DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK---GLR---------IGYLPQEPPLDDDLTvldtv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 ----------MKEHLELYAAVKGLGKEDAALS-----------------ISRLVEALKL-QEQLKAPVKTLSEGIKRK-- 1347
Cdd:COG0488 83 ldgdaelralEAELEELEAKLAEPDEDLERLAelqeefealggweaearAEEILSGLGFpEEDLDRPVSELSGGWRRRva 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1348 LCFVLsiLGNPSVVLLDEPFTGMDPEGQQqmWqiLQATVKNkERGTLLT-TH--YMseAEAVCDRMAMMVSGTLR 1419
Cdd:COG0488 163 LARAL--LSEPDLLLLDEPTNHLDLESIE--W--LEEFLKN-YPGTVLVvSHdrYF--LDRVATRILELDRGKLT 228
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
409-603 |
2.06e-14 |
|
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: 73.66 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTqlseitdmeeirknIGFCPQFNF-QFDflTVR 487
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPWiQNG--TIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENLrVFAKIkgIQPKEVEQEVKRIIMELDMQS----IQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:cd03250 84 ENI-LFGKP--FDEERYEKVIKACALEPDLEIlpdgDLTEIGEKginLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 561 FSRHRVW-----SLLKEHKVDRLILFSTQFMDEadilADRKVFLSNGK 603
Cdd:cd03250 161 HVGRHIFencilGLLLNNKTRILVTHQLQLLPH----ADQIVVLDNGR 204
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1185-1423 |
2.24e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.91 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1185 LTAPNLEEEPVITASCLHKeYYETKKscfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVV 1264
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISK-SFDGKE----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1265 LQG---SRASVRQQHDNSLkFLGYcpqenSLWPKLTMKEHLELYAAVKGLGKEDAAlsiSRLVEALK---LQEQLKAPVK 1338
Cdd:PRK09452 73 LDGqdiTHVPAENRHVNTV-FQSY-----ALFPHMTVFENVAFGLRMQKTPAAEIT---PRVMEALRmvqLEEFAQRKPH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1339 TLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMwqilQATVKNKERGTLLT----THYMSEAEAVCDRMAMMV 1414
Cdd:PRK09452 144 QLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM----QNELKALQRKLGITfvfvTHDQEEALTMSDRIVVMR 219
|
....*....
gi 296439455 1415 SGTLRCIGS 1423
Cdd:PRK09452 220 DGRIEQDGT 228
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1226-1427 |
2.45e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 74.02 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1226 SFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrasvrQQHDN--------SLKFlgycpQENSLWPKLT 1297
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG------QDLTAlppaerpvSMLF-----QENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 MKEHLelyaavkGLGkedaalsisrLVEALKLQEQLKAPVKTLSE-----GIKRKLCFVLS------------ILGNPSV 1360
Cdd:COG3840 88 VAQNI-------GLG----------LRPGLKLTAEQRAQVEQALErvglaGLLDRLPGQLSggqrqrvalarcLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
388-584 |
2.62e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 74.92 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEY-NGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitdmeE 466
Cdd:PRK15056 4 QAGIVVNDVTVTWrNGHT----ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ-----A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKN-IGFCPQFN-FQFDFLTVRENLRVFAKIKGI----QPKEVEQE-VKRIIMELDMQSIQDIIAKKLSGGQKRKLTLG 539
Cdd:PRK15056 75 LQKNlVAYVPQSEeVDWSFPVLVEDVVMMGRYGHMgwlrRAKKRDRQiVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQ 584
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTH 200
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
391-604 |
3.49e-14 |
|
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: 74.46 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEY-----NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI--TD 463
Cdd:TIGR02769 3 LEVRDVTHTYrtgglFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIgfcpQFNFQFDFLTV----------RENLRVFAKIKgiqpkEVEQEvKRIIMELDMQSIQDIIAKK----LS 529
Cdd:TIGR02769 83 RRAFRRDV----QLVFQDSPSAVnprmtvrqiiGEPLRHLTSLD-----ESEQK-ARIAELLDMVGLRSEDADKlprqLS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 530 GGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLI--LFSTQFMDEADILADRKVFLSNGKL 604
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1201-1418 |
3.66e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 74.24 E-value: 3.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1201 LHKEYYETKkscfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSL 1280
Cdd:PRK10619 11 LHKRYGEHE-----------VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1281 KF------------LGYCPQENSLWPKLTMKEH-LELYAAVKGLGKEDAALSISRLVEALKLQE--QLKAPVKtLSEGIK 1345
Cdd:PRK10619 80 KVadknqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDEraQGKYPVH-LSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1346 RKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQatvKNKERG--TLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQ---QLAEEGktMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
410-570 |
3.68e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 77.61 E-value: 3.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL--SVSTEGSATIYNTQLSEitdmeEIRKNIGFCPQFNFQFDFLTVR 487
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRiqGNNFTGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENLrVFAKIKGIqPKEVEQEVK-----RIIMELDMQSIQDIIA-----KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:PLN03211 159 ETL-VFCSLLRL-PKSLTKQEKilvaeSVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236
|
170
....*....|...
gi 296439455 558 LDPFSRHRVWSLL 570
Cdd:PLN03211 237 LDATAAYRLVLTL 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1222-1418 |
4.71e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 76.63 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDnslkfLG-Y-CPQENSLWPKL 1296
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGnpcARLTPAKAHQ-----LGiYlVPQEPLLFPNL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELyaavkGLGKEDAALS-ISRLVEALKLQEQLKAPVKTLsEGIKRKLCFVL-SILGNPSVVLLDEPFTGMDPEG 1374
Cdd:PRK15439 102 SVKENILF-----GLPKRQASMQkMKQLLAALGCQLDLDSSAGSL-EVADRQIVEILrGLMRDSRILILDEPTASLTPAE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 1375 QQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK15439 176 TERLFSRIRE-LLAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1212-1425 |
4.71e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 74.04 E-value: 4.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-------------SRASVRQQHdn 1278
Cdd:PRK13548 9 SVRLGGRTL-LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGrpladwspaelarRRAVLPQHS-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1279 SLKFlgycPqenslwpkLTMKEHLELYAAVKGLGKE------DAALsisRLVEALKLQEQlkaPVKTLSEGIK------R 1346
Cdd:PRK13548 86 SLSF----P--------FTVEEVVAMGRAPHGLSRAeddalvAAAL---AQVDLAHLAGR---DYPQLSGGEQqrvqlaR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1347 KLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVknKERGT--------L-LTTHYmseaeavCDRMAMMVSGT 1417
Cdd:PRK13548 148 VLAQLWEPDGPPRWLLLDEPTSALDLAHQHHVLRLARQLA--HERGLavivvlhdLnLAARY-------ADRIVLLHQGR 218
|
....*...
gi 296439455 1418 LRCIGSIQ 1425
Cdd:PRK13548 219 LVADGTPA 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
379-604 |
5.47e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.60 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 379 EPVSPefhGKEAIRIRNVikEYNGKTGkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQL 458
Cdd:COG3845 249 APAEP---GEVVLEVENL--SVRDDRG-VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 459 S-----EITDM------EEiRKNIGFCPQFnfqfdflTVRENL-------RVFAKIKGIQPKEVEQEVKRIIMELD--MQ 518
Cdd:COG3845 323 TglsprERRRLgvayipED-RLGRGLVPDM-------SVAENLilgryrrPPFSRGGFLDRKAIRAFAEELIEEFDvrTP 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 519 SIqDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKvDR---LILFSTQfMDEADILADR 595
Cdd:COG3845 395 GP-DTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELR-DAgaaVLLISED-LDEILALSDR 471
|
....*....
gi 296439455 596 KVFLSNGKL 604
Cdd:COG3845 472 IAVMYEGRI 480
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
410-572 |
5.70e-14 |
|
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: 76.78 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEIRKNIGFCPQ----FNfqfDflT 485
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASLRAAIGIVPQdtvlFN---D--T 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 486 VRENLRvFAKIkGIQPKEVEQEVKriimeldMQSIQDIIAK--------------KLSGGQKRKltLGIA--ILGDPQVL 549
Cdd:COG5265 448 IAYNIA-YGRP-DASEEEVEAAAR-------AAQIHDFIESlpdgydtrvgerglKLSGGEKQR--VAIArtLLKNPPIL 516
|
170 180
....*....|....*....|...
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALRE 539
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
410-579 |
5.95e-14 |
|
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: 77.64 E-value: 5.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLsVSTEGSATIYNTQLSEITdMEEIRKNIGFCPQFNFQFDFlTVREN 489
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT-LQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKgiqpkevEQEVKRIIMELDMQSIQDIIAKKL-----------SGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:TIGR01271 1312 LDPYEQWS-------DEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 559 DPFSRHRVWSLLK-----------EHKVDRLI 579
Cdd:TIGR01271 1385 DPVTLQIIRKTLKqsfsnctvilsEHRVEALL 1416
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1222-1418 |
6.73e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 73.97 E-value: 6.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKEH 1301
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LELYAAVKGLGKEDAalsISRLVEAL----KLQEQLKAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQ 1377
Cdd:PRK13642 103 VAFGMENQGIPREEM---IKRVDEALlavnMLDFKTREPAR-LSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 296439455 1378 MWQILQaTVKNKERGTLLT-THYMSEAeAVCDRMAMMVSGTL 1418
Cdd:PRK13642 179 IMRVIH-EIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
416-595 |
8.05e-14 |
|
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: 72.83 E-value: 8.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 416 DIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntqlseitDMEEIRKNIGFCPQFnFQFDF-LTVRENLRVFA 494
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-------------DIEIELDTVSYKPQY-IKADYeGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 495 KIKGIQPkeveQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKehk 574
Cdd:cd03237 87 KDFYTHP----YFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR--- 159
|
170 180
....*....|....*....|....*...
gi 296439455 575 vdRLILF--STQFMDEADI-----LADR 595
Cdd:cd03237 160 --RFAENneKTAFVVEHDIimidyLADR 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1218-1427 |
8.11e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 74.76 E-value: 8.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVR--QQHDNSLKFLGYcpqenSLWPK 1295
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRsiQQRDICMVFQSY-----ALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAAlsiSRLVEALKL------QEQLkapVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTG 1369
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERK---QRVKEALELvdlagfEDRY---VDQISGGQQQRVALARALILKPKVLLFDEPLSN 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1370 MDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:PRK11432 167 LDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1205-1423 |
8.17e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1205 YYETKKSCFSTRkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSLK 1281
Cdd:PRK13643 9 YTYQPNSPFASR----ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvSSTSKQKEIKPVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1282 FLGYCPQ--ENSLWPKLTMKEhLELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCFVLSILGN 1357
Cdd:PRK13643 85 KVGVVFQfpESQLFEETVLKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFweKSPFE-LSGGQMRRVAIAGILAME 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1358 PSVVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:PRK13643 163 PEVLVLDEPTAGLDPKARIEMMQLFE-SIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1225-1419 |
8.54e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 72.50 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGS---------RASVRQQHdnslkfLGYCPQENSLWPK 1295
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQplhqmdeeaRAKLRAKH------VGFVFQSFMLIPT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:PRK10584 103 LNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTG 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 1376 QQMWQILQATvkNKERGT--LLTTHyMSEAEAVCDRMAMMVSGTLR 1419
Cdd:PRK10584 183 DKIADLLFSL--NREHGTtlILVTH-DLQLAARCDRRLRLVNGQLQ 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1216-1418 |
8.54e-14 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 73.38 E-value: 8.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSLkfLGYCPQ-ENSLWP 1294
Cdd:PRK15056 17 RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQ--PTRQALQKNL--VAYVPQsEEVDWS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGLG-----KEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTG 1369
Cdd:PRK15056 93 FPVLVEDVVMMGRYGHMGwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 296439455 1370 MDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDrMAMMVSGTL 1418
Cdd:PRK15056 173 VDVKTEARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTV 219
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1218-1423 |
1.21e-13 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 74.34 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAS-VRQQHDNslkfLGYCPQENSLWPKL 1296
Cdd:COG3839 15 GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTdLPPKDRN----IAMVFQSYALYPHM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKRklcfvlSILGNPSVVLLDEPFTGM 1370
Cdd:COG3839 91 TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvaLGR------ALVREPKVFLLDEPLSNL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1371 DPEGQQQM-WQI--LQatvknKERG--TLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG3839 165 DAKLRVEMrAEIkrLH-----RRLGttTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
410-582 |
1.64e-13 |
|
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: 72.58 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLsVSTEGSATIYNTQLSEITdMEEIRKNIGFCPQFNFQFDFlTVREN 489
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSWNSVP-LQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKgiqpkevEQEVKRIIMELDMQSIQDIIAKKL-----------SGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:cd03289 97 LDPYGKWS-------DEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180
....*....|....*....|....
gi 296439455 559 DPFSRHRVWSLLKEHKVDRLILFS 582
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILS 193
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
394-559 |
2.12e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 70.75 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL---SVSTEGSATIYNTQLSEITdmEEIRKN 470
Cdd:cd03233 7 RNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegNVSVEGDIHYNGIPYKEFA--EKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQFNFQFDFLTVRENLRVFAKIKGiqpkeveqevkriimeldmqsiqDIIAKKLSGGQKRKLTLGIAILGDPQVLL 550
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 296439455 551 LDEPTAGLD 559
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
405-608 |
2.14e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.11 E-value: 2.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLsEITDMEEIRKNIGFCPQ---FNFQF 481
Cdd:PRK09536 14 GDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-EALSARAASRRVASVPQdtsLSFEF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 DFLTVRENLRV-----FAKIKGIQPKEVEQEVKRIimELDMQSIQDIIAkkLSGGQKRKLTLGIAILGDPQVLLLDEPTA 556
Cdd:PRK09536 93 DVRQVVEMGRTphrsrFDTWTETDRAAVERAMERT--GVAQFADRPVTS--LSGGERQRVLLARALAQATPVLLLDEPTA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 557 GLDpfSRHRVWSL-LKEHKVD--RLILFSTQFMDEADILADRKVFLSNGKLKCAG 608
Cdd:PRK09536 169 SLD--INHQVRTLeLVRRLVDdgKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
405-559 |
2.83e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 71.30 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSatiyntqlseITDMEEIRknIGFCPQfNFQFDF- 483
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV----------IKRNGKLR--IGYVPQ-KLYLDTt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 484 --LTVRENLRVFAkikGIQPKEVEQEVKRI----IMELDMQsiqdiiakKLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:PRK09544 82 lpLTVNRFLRLRP---GTKKEDILPALKRVqaghLIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
..
gi 296439455 558 LD 559
Cdd:PRK09544 151 VD 152
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1190-1427 |
2.84e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 74.51 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1190 LEEEPVITASCLHKEYYETkkscfstRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKS-TSIKMI-----TGCTKPTAGVV 1263
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQE-------QQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKML 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1264 VLQGSRA--SVRQQHDNSLKF-----LGYCPQE--NSLWPKLTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKL---Q 1330
Cdd:PRK10261 80 LRRRSRQviELSEQSAAQMRHvrgadMAMIFQEpmTSLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIpeaQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1331 EQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRM 1410
Cdd:PRK10261 160 TILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRV 239
|
250
....*....|....*..
gi 296439455 1411 AMMVSGTLRCIGSIQHL 1427
Cdd:PRK10261 240 LVMYQGEAVETGSVEQI 256
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1213-1389 |
2.88e-13 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 74.43 E-value: 2.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYC 1286
Cdd:COG1132 347 FSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGvdirdlTLESLRRQ-------IGVV 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQENSLWpKLTMKEHLelyaavkGLGKEDAalSISRLVEALK----------LQEQLKAPV----KTLSEGIKRKLCFVL 1352
Cdd:COG1132 420 PQDTFLF-SGTIRENI-------RYGRPDA--TDEEVEEAAKaaqahefieaLPDGYDTVVgergVNLSGGQRQRIAIAR 489
|
170 180 190
....*....|....*....|....*....|....*..
gi 296439455 1353 SILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNK 1389
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETEALIQEALERLMKGR 526
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
405-559 |
3.44e-13 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 74.31 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDFl 484
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRETFGKHIGYLPQDVELFPG- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRVFAKikGIQPKEVEQEVK-----RIIMELDMQSIQDIIAK--KLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:TIGR01842 407 TVAENIARFGE--NADPEKIIEAAKlagvhELILRLPDGYDTVIGPGgaTLSGGQRQRIALARALYGDPKLVVLDEPNSN 484
|
..
gi 296439455 558 LD 559
Cdd:TIGR01842 485 LD 486
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1221-1409 |
3.56e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.79 E-value: 3.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrasVRQQHDNSLKFLG------YcpQENSLWP 1294
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDG----QEMRFASTTAALAagvaiiY--QELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGLGKEDAALSISRLVEALK-LQEQL--KAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMD 1371
Cdd:PRK11288 93 EMTVAENLYLGQLPHKGGIVNRRLLNYEAREQLEhLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 296439455 1372 PEGQQQMWQILQAtVKNKERGTLLTTHYMSEAEAVCDR 1409
Cdd:PRK11288 173 AREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDA 209
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
383-580 |
4.22e-13 |
|
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: 69.75 E-value: 4.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 383 PEfHGKeaIRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEIt 462
Cdd:cd03369 2 PE-HGE--IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 463 DMEEIRKNIGFCPQFNFQFDFlTVRENLRVFakikgiqpkeveqevkriimelDMQSIQDIIA--------KKLSGGQKR 534
Cdd:cd03369 76 PLEDLRSSLTIIPQDPTLFSG-TIRSNLDPF----------------------DEYSDEEIYGalrvseggLNLSQGQRQ 132
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 535 KLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLIL 580
Cdd:cd03369 133 LLCLARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTIL 178
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
172-559 |
4.70e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 74.50 E-value: 4.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 172 RESAFWLSWGLTYICFIF--IMSIFMALVITSIPIV----------FHTGFMVIFTLYSLYGlsliALAFLMSVLIRKPM 239
Cdd:PLN03140 603 RDLLFHPPWTFTLPTFLLgiPISIIESVVWVVITYYsigfapeasrFFKQLLLVFLIQQMAA----GIFRLIASVCRTMI 678
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 240 LAGLAGFLFTVFWGCLG-FTVLYRQLPLSLGWVLsLLSPFAFTAGMAQITHL-----------DNYLS-GV----IFPDP 302
Cdd:PLN03140 679 IANTGGALVLLLVFLLGgFILPKGEIPNWWEWAY-WVSPLSYGFNALAVNEMfaprwmnkmasDNSTRlGTavlnIFDVF 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 303 SGDSYKMIATFFILAFDTLFYLIFTL---YF-----------ERVLPDKDGHGDSPLFFLKSSFWSKHQNTHHEIFENEI 368
Cdd:PLN03140 758 TDKNWYWIGVGALLGFTILFNVLFTLaltYLnplgkkqaiisEETAEEMEGEEDSIPRSLSSADGNNTREVAIQRMSNPE 837
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 369 NPEHSSDDS----------------FEPVSPEFHG-KEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGA 431
Cdd:PLN03140 838 GLSKNRDSSleaangvapkrgmvlpFTPLAMSFDDvNYFVDMPAEMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGA 917
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 432 GKSTLLNILSGLSVS--TEGSATIyntqlSEITDMEEIRKNI-GFCPQFNFQFDFLTVRENLRVFAKIKgiQPKEVEQEV 508
Cdd:PLN03140 918 GKTTLMDVLAGRKTGgyIEGDIRI-----SGFPKKQETFARIsGYCEQNDIHSPQVTVRESLIYSAFLR--LPKEVSKEE 990
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 509 KRI----IMEL-DMQSIQDIIA-----KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PLN03140 991 KMMfvdeVMELvELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
375-559 |
4.82e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 4.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 375 DDSFEPVSPEFhGKEAIRIRNVikeyngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIY 454
Cdd:COG1129 242 EDLFPKRAAAP-GEVVLEVEGL--------SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 455 NTQLSEITDMEEIRKNIGFCPQfnfqfD------FL--TVREN-----LRVFAKIKGIQPKEVEQEVKRIIMELD--MQS 519
Cdd:COG1129 313 GKPVRIRSPRDAIRAGIAYVPE-----DrkgeglVLdlSIRENitlasLDRLSRGGLLDRRRERALAEEYIKRLRikTPS 387
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 296439455 520 IQDIIaKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:COG1129 388 PEQPV-GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1222-1406 |
4.93e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 69.82 E-value: 4.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKP---TAGVVVLQGSRASVRQQHDnslKFLGYCPQENSLWPKLTM 1298
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQ---RRIGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLeLYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQM 1378
Cdd:COG4136 94 GENL-AFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQF 172
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 1379 --WQILQAtvknKERG--TLLTTHYMSEAEAV 1406
Cdd:COG4136 173 reFVFEQI----RQRGipALLVTHDEEDAPAA 200
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1216-1418 |
5.15e-13 |
|
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: 70.29 E-value: 5.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG-----CTKPTAGVVVLQGSRASVRQQHDNSLKF-LGYCPQE 1289
Cdd:cd03260 10 YGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVDVLELRRrVGMVFQK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLWPKlTMKEHLELYAAVKGLGKEDAalsISRLVE-ALK---LQEQLK--APVKTLSEGIKRKLCFVLSILGNPSVVLL 1363
Cdd:cd03260 90 PNPFPG-SIYDNVAYGLRLHGIKLKEE---LDERVEeALRkaaLWDEVKdrLHALGLSGGQQQRLCLARALANEPEVLLL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1364 DEPFTGMDPEGQQQMWQILQATvkNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03260 166 DEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
409-580 |
5.40e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.79 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIgfcpQFNFQ----FDFL 484
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGV----VRTFQhvrlFREM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRV----------FA---KIKGIQPKEVEQeVKRIIMELDMQSIQDII---AKKLSGGQKRKLTLGIAILGDPQV 548
Cdd:PRK11300 96 TVIENLLVaqhqqlktglFSgllKTPAFRRAESEA-LDRAATWLERVGLLEHAnrqAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 296439455 549 LLLDEPTAGLDPFSRHRVWSLL----KEHKVDRLIL 580
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIaelrNEHNVTVLLI 210
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
406-623 |
5.42e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.99 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 406 KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDfLT 485
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY-DHHYLHRQVALVGQEPVLFS-GS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 486 VRENLRV---FAKIKGIQPKEVEQEVKRIIMELDmQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:TIGR00958 571 VRENIAYgltDTPDEEIMAAAKAANAHDFIMEFP-NGYDTEVGEKgsqLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 560 PFSRHRVWSLLKehKVDRLILFSTQFMDEADiLADRKVFLSNGKLKCAGSSLFLKRKWGIGYHL 623
Cdd:TIGR00958 650 AECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
391-610 |
6.22e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 70.81 E-value: 6.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAT----IYNTQLSE---ITD 463
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShielLGRTVQREgrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIGFC-PQFNFqFDFLTVRENLRVFAKikGIQP----------KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQ 532
Cdd:PRK09984 81 IRKSRANTGYIfQQFNL-VNRLSVLENVLIGAL--GSTPfwrtcfswftREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 533 KRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFST-QFMDEADILADRKVFLSNGKLKCAGSS 610
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1220-1417 |
7.01e-13 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 70.40 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1220 IAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMK 1299
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 E------HLELYAAV-KGLGK-------EDAALSISRL-VEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLD 1364
Cdd:PRK11300 99 EnllvaqHQQLKTGLfSGLLKtpafrraESEALDRAATwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1365 EPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGT 1417
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1219-1418 |
9.06e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 68.23 E-value: 9.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCP---QENSLWPK 1295
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHlelyaavkglgkedaaLSISRLvealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:cd03215 93 LSVAEN----------------IALSSL----------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 296439455 1376 QQMWQILQATvknKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:cd03215 141 AEIYRLIREL---ADAGKavLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
411-559 |
1.04e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 411 QGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntqlsEIT-DMEEIRKNigfCPQFNFQF-------- 481
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAG----------EVLwQGEPIRRQ---RDEYHQDLlylghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 --DFLTVRENLRVFAKIKGIQPKEVEQEVkriimeLDMQSIQ---DIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTA 556
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGDDEALWEA------LAQVGLAgfeDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
...
gi 296439455 557 GLD 559
Cdd:PRK13538 159 AID 161
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
393-559 |
1.73e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 70.52 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitDMEEIRK--- 469
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI---------DGEDVTHrsi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 -NIGFCpqFNFQ----FDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILG 544
Cdd:PRK11432 76 qQRDIC--MVFQsyalFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALIL 153
|
170
....*....|....*
gi 296439455 545 DPQVLLLDEPTAGLD 559
Cdd:PRK11432 154 KPKVLLFDEPLSNLD 168
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1219-1435 |
2.25e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 68.96 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvRQQHDNSLKFlgycpQENSLWPKLTM 1298
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAERGVVF-----QNEGLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQM 1378
Cdd:PRK11248 88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1379 WQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCigsIQHLKNKFGRDY 1435
Cdd:PRK11248 168 QTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRF 221
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
410-559 |
2.45e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 71.32 E-value: 2.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGS-----ATIYNTqlseitDMEEIRKNIGFCPQfnfQFDFL 484
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSvrldgADLSQW------DREELGRHIGYLPQ---DVELF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 --TVRENLrvfAKIKGIQPKEVEQEVKR-----IIMEL---------DMQSIqdiiakkLSGGQKRKLTLGIAILGDPQV 548
Cdd:COG4618 419 dgTIAENI---ARFGDADPEKVVAAAKLagvheMILRLpdgydtrigEGGAR-------LSGGQRQRIGLARALYGDPRL 488
|
170
....*....|.
gi 296439455 549 LLLDEPTAGLD 559
Cdd:COG4618 489 VVLDEPNSNLD 499
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1217-1418 |
2.90e-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: 66.57 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQqhDNSLKFLGYCPQENSLWpkl 1296
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE--KALSSLISVLNQRPYLF--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 tmkehlelyaavkglgkedaalsisrlveALKLQEQLKAPvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:cd03247 88 -----------------------------DTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITER 135
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1377 QMWQILQATVKNKergTLL-TTHYMSEAEAVcDRMAMMVSGTL 1418
Cdd:cd03247 136 QLLSLIFEVLKDK---TLIwITHHLTGIEHM-DKILFLENGKI 174
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
408-571 |
3.75e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 408 EALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL------SVSTEGSATIYNTQlseitDMEEIRKNIGFCPQFNFQF 481
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLlrpqkgAVLWQGKPLDYSKR-----GLLALRQQVATVFQDPEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 482 DFLT-VRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:PRK13638 90 IFYTdIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169
|
170
....*....|.
gi 296439455 561 FSRHRVWSLLK 571
Cdd:PRK13638 170 AGRTQMIAIIR 180
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1229-1416 |
5.73e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 67.47 E-value: 5.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV-----------VLQGSRASVRQ--QHdnslkfLGYCPQENSLWPK 1295
Cdd:PRK11264 26 VKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgditidtarSLSQQKGLIRQlrQH------VGFVFQNFNLFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEH-LELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:PRK11264 100 RTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPEL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 296439455 1375 QQQMWQILQATVKNKeRGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK11264 180 VGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1221-1454 |
5.84e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVrqqhdnslkflgycPQENSLWPKLTMKE 1300
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVI--------------AISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQ 1380
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1381 ILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFgRDYLLEIKMKEPTQVEALHTEI 1454
Cdd:PRK13546 185 KIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAEQKEFRNKL 256
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1444 |
6.43e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.85 E-value: 6.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAS-------------VRQQHDNslKFLGYCP 1287
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITddnfeklrkhigiVFQNPDN--QFVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 Q-------ENSLWPKLTMKEhlelyaavkglgkedaalSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:PRK13648 102 KydvafglENHAVPYDEMHR------------------RVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAeAVCDRMAMMVSGTLRCIGSIQHLKNKfgRDYLLEIK 1440
Cdd:PRK13648 164 IILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDH--AEELTRIG 240
|
....
gi 296439455 1441 MKEP 1444
Cdd:PRK13648 241 LDLP 244
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1226-1427 |
6.76e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 6.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1226 SFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGS--RASVRQQHDNSLKFlgycpQENSLWPKLTMKEH-- 1301
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhTTTPPSRRPVSMLF-----QENNLFSHLTVAQNig 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 ------LELYAAVKGLGKEDAA-LSISRLVEALKLQeqlkapvktLSEGIKRKL----CFVLSilgNPsVVLLDEPFTGM 1370
Cdd:PRK10771 94 lglnpgLKLNAAQREKLHAIARqMGIEDLLARLPGQ---------LSGGQRQRValarCLVRE---QP-ILLLDEPFSAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1371 DPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:PRK10771 161 DPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1205-1423 |
8.13e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.73 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1205 YYETKKSCFSTRkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFL- 1283
Cdd:PRK13645 14 YTYAKKTPFEFK----ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVKRLr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1284 ---GYCPQ--ENSLWPKlTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCFVLSILG 1356
Cdd:PRK13645 90 keiGLVFQfpEYQLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYvkRSPFE-LSGGQKRRVALAGIIAM 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1357 NPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:PRK13645 168 DGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
406-604 |
1.01e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.26 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 406 KVEALQG-----IFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSE----------ITDMEEIRKN 470
Cdd:PRK10762 259 KVDNLSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangIVYISEDRKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQfnfqfdfLTVREN-----LRVFAKIKG-IQPKEVEQEVKRIIMELDMQ--SIQDIIaKKLSGGQKRKLTLGIAI 542
Cdd:PRK10762 339 DGLVLG-------MSVKENmsltaLRYFSRAGGsLKHADEQQAVSDFIRLFNIKtpSMEQAI-GLLSGGNQQKVAIARGL 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRL--ILFSTQfMDEADILADRKVFLSNGKL 604
Cdd:PRK10762 411 MTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLsiILVSSE-MPEVLGMSDRILVMHEGRI 473
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1221-1418 |
1.04e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 69.28 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDnSLKF-LGYCP---QENSLWPKL 1296
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD-AIRAgIAYVPedrKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLEL--YAAVKGLG-----KEDAAlsISRLVEALKLQEQ-LKAPVKTLSEGIKRKLcfVLS--ILGNPSVVLLDEP 1366
Cdd:COG1129 346 SIRENITLasLDRLSRGGlldrrRERAL--AEEYIKRLRIKTPsPEQPVGNLSGGNQQKV--VLAkwLATDPKVLILDEP 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1367 FTGMDPEGQQQMWQILQATVKNKeRGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAEG-KAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1220-1398 |
1.25e-11 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 68.93 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1220 IAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSlKFLGYCPQENSLWPKlTMK 1299
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 EHL----------ELYAAVKGLGKEDaalsisrLVEALK--LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:TIGR02868 427 ENLrlarpdatdeELWAALERVGLAD-------WLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|.
gi 296439455 1368 TGMDPEGQQQMWQILQATvkNKERGTLLTTH 1398
Cdd:TIGR02868 500 EHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
388-580 |
1.92e-11 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 388 KEAIRIRNVIKEYNGKtgKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITdMEEI 467
Cdd:PRK11176 339 KGDIEFRNVTFTYPGK--EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYT-LASL 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 RKNIGFCPQ----FNfqfDflTVRENLrVFAKIKGIQPKEVEQEVK-----RIIMELDmQSIQDIIAKK---LSGGQKRK 535
Cdd:PRK11176 416 RNQVALVSQnvhlFN---D--TIANNI-AYARTEQYSREQIEEAARmayamDFINKMD-NGLDTVIGENgvlLSGGQRQR 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLIL 580
Cdd:PRK11176 489 IAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSL 533
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
393-569 |
2.03e-11 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 65.86 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSG---LSVsTEGSATIYNTqlsEITDM---EE 466
Cdd:COG0396 3 IKNLHVSVEGK----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkYEV-TSGSILLDGE---DILELspdER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 IRKNIGFCpqfnFQ----------FDFLTVRENLRvfaKIKGIQPKEVEQEVKRIIMELDMQsiQDIIAK----KLSGGQ 532
Cdd:COG0396 75 ARAGIFLA----FQypveipgvsvSNFLRTALNAR---RGEELSAREFLKLLKEKMKELGLD--EDFLDRyvneGFSGGE 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 296439455 533 KRKL-TLGIAILgDPQVLLLDEPTAGLDpfsrhrVWSL 569
Cdd:COG0396 146 KKRNeILQMLLL-EPKLAILDETDSGLD------IDAL 176
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1227-1410 |
2.06e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.26 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1227 FCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvRQQHDNSLKFLGYCPqenSLWPKLTMKEHLELYA 1306
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAYLGHLP---GLKADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1307 AVKGLGKED---AALSIsrlveaLKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQ 1383
Cdd:PRK13543 108 GLHGRRAKQmpgSALAI------VGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMIS 181
|
170 180
....*....|....*....|....*..
gi 296439455 1384 ATVKNkERGTLLTTHYMSEAEAVCDRM 1410
Cdd:PRK13543 182 AHLRG-GGAALVTTHGAYAAPPVRTRM 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
403-572 |
2.23e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.04 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 403 KTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD--MEEIRKNIgfcpQFNFQ 480
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDI----QMIFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 481 fDFLT-----------VRENLRVFakikgiQPK----EVEQEVKRIIMELDMqsIQDIIAK---KLSGGQKRKLTLGIAI 542
Cdd:PRK15079 106 -DPLAslnprmtigeiIAEPLRTY------HPKlsrqEVKDRVKAMMLKVGL--LPNLINRyphEFSGGQCQRIGIARAL 176
|
170 180 190
....*....|....*....|....*....|
gi 296439455 543 LGDPQVLLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQ 206
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
377-605 |
2.23e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 68.31 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 377 SFEPVSPEFHGKEAIRIRNvIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVST-EGSATIYN 455
Cdd:TIGR02633 244 SLYPHEPHEIGDVILEARN-LTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 456 TQLSEITDMEEIRKNIGFCPQFNFQ---FDFLTVREN-----LRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQ-DIIAK 526
Cdd:TIGR02633 323 KPVDIRNPAQAIRAGIAMVPEDRKRhgiVPILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASpFLPIG 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 527 KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL---LKEHKVdRLILFSTQfMDEADILADRKVFLSNGK 603
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLinqLAQEGV-AIIVVSSE-LAEVLGLSDRVLVIGEGK 480
|
..
gi 296439455 604 LK 605
Cdd:TIGR02633 481 LK 482
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
410-559 |
2.54e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 65.63 E-value: 2.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSvSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDFLTVREN 489
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDW-SAAELARHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAkikgiQPKEVEQEVKRIIMEL--DMQsIQDIIAK---KLSGGQKRKLTLGIAIL-------GDPQVLLLDEPTAG 557
Cdd:COG4138 90 LALHQ-----PAGASSEAVEQLLAQLaeALG-LEDKLSRpltQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNS 163
|
..
gi 296439455 558 LD 559
Cdd:COG4138 164 LD 165
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
405-582 |
2.57e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 65.78 E-value: 2.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 405 GKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDmEEIRKNIGFCPQFNFQFDFL 484
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAS-KEVARRIGLLAQNATTPGDI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVRENLRvfakiKGIQP---------KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPT 555
Cdd:PRK10253 97 TVQELVA-----RGRYPhqplftrwrKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180
....*....|....*....|....*..
gi 296439455 556 AGLDpfsrhrvwsllKEHKVDRLILFS 582
Cdd:PRK10253 172 TWLD-----------ISHQIDLLELLS 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
420-559 |
2.92e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKnIGFCPQFNFQFDFLTVRENLRVfakikGI 499
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRELVAI-----GR 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 500 QP---------KEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK10575 111 YPwhgalgrfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
422-604 |
3.12e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 65.89 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 422 ITAILGHNGAGKSTLLNIL-------SGLSVSTE---GSATIYNTQlseitDMEEIRKNIGFCPQFNFQFDfLTVRENLR 491
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLnrmndkvSGYRYSGDvllGGRSIFNYR-----DVLEFRRRVGMLFQRPNPFP-MSIMDNVL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 492 VFAKIKGIQP-KEVEQEVKRIIMELDM-QSIQDIIAK---KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRV 566
Cdd:PRK14271 123 AGVRAHKLVPrKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKI 202
|
170 180 190
....*....|....*....|....*....|....*....
gi 296439455 567 WSLLKEhKVDRL-ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK14271 203 EEFIRS-LADRLtVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1234-1454 |
3.26e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 65.80 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1234 VLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRA--------SVRQQHDNSLKflgyCPQENSLWPKLTMkehlELY 1305
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllALRQQVATVFQ----DPEQQIFYTDIDS----DIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1306 AAVKGLGKEDAALSiSRLVEALKL---QEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQIL 1382
Cdd:PRK13638 101 FSLRNLGVPEAEIT-RRVDEALTLvdaQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1383 QATVKNKERgTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLknkFGRDYLLE-IKMKEPTQVEaLHTEI 1454
Cdd:PRK13638 180 RRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEV---FACTEAMEqAGLTQPWLVK-LHTQL 247
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1221-1430 |
3.85e-11 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 65.42 E-value: 3.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIK----MITGCTKPTAGVVVLQGS-RASVRQQHD--NSLKFLGYCPQENSLW 1293
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvQREGRLARDirKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKLTMKEHLELYAavkgLGKEDAALSISRLVEALKLQEQLKA------------PVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:PRK09984 99 NRLSVLENVLIGA----LGSTPFWRTCFSWFTREQKQRALQAltrvgmvhfahqRVSTLSGGQQQRVAIARALMQQAKVI 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1362 LLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNK 1430
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1218-1398 |
5.19e-11 |
|
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: 62.08 E-value: 5.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsrasvrqQHDNSLKFlGYCPQenslwpklt 1297
Cdd:cd03221 12 GKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV-----------TWGSTVKI-GYFEQ--------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 mkehlelyaavkglgkedaalsisrlvealklqeqlkapvktLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQ 1377
Cdd:cd03221 71 ------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEA 108
|
170 180
....*....|....*....|.
gi 296439455 1378 mwqiLQATVKNKERGTLLTTH 1398
Cdd:cd03221 109 ----LEEALKEYPGTVILVSH 125
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
377-604 |
5.40e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 377 SFEPVSPEFHGKEAIRIRNVIKEYNGKtgkveaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNT 456
Cdd:PRK09700 252 AMKENVSNLAHETVFEVRNVTSRDRKK------VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 457 QLSEITDMEEIRKNIGFCPQF---NFQFDFLTVRENLRVFAKIK--------GIQPKEVEQ---EVKRIIMELDMQSIQD 522
Cdd:PRK09700 326 DISPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLFHEVDEQrtaENQRELLALKCHSVNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 523 IIAKkLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVD-RLILFSTQFMDEADILADRKVFLSN 601
Cdd:PRK09700 406 NITE-LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCE 484
|
...
gi 296439455 602 GKL 604
Cdd:PRK09700 485 GRL 487
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1216-1398 |
5.59e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG--CTKPTAGVVVLQgsrasvrqqhDNSlkflgyCPQENSL- 1292
Cdd:COG2401 40 VVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVP----------DNQ------FGREASLi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 ---WPKLTMKEHLELYAAVkGLGkeDAALsisrlvealklqeqLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEpFT- 1368
Cdd:COG2401 104 daiGRKGDFKDAVELLNAV-GLS--DAVL--------------WLRRFKELSTGQKFRFRLALLLAERPKLLVIDE-FCs 165
|
170 180 190
....*....|....*....|....*....|
gi 296439455 1369 GMDPEGQQQMWQILQATVKNKERGTLLTTH 1398
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1216-1383 |
5.98e-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: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGctKPTAGVVvlQGS-RASVRQQHDNSLKFLGYCPQENSLWP 1294
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVI--TGEiLINGRPLDKNFQRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHLELYAAVKGLGKEDaalsisrlvealklqeqlkapvktlsegiKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:cd03232 93 NLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
....*....
gi 296439455 1375 QQQMWQILQ 1383
Cdd:cd03232 144 AYNIVRFLK 152
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
390-559 |
6.45e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.84 E-value: 6.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSatiynTQLSEitdmeeiRK 469
Cdd:PRK15064 319 ALEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT-----VKWSE-------NA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQ---FNFQFDfLTVRENLRVFAkikgiQPKEVEQEVKRIIMELDMQsiQDIIAKK---LSGGQKRKLTLGIAIL 543
Cdd:PRK15064 383 NIGYYAQdhaYDFEND-LTLFDWMSQWR-----QEGDDEQAVRGTLGRLLFS--QDDIKKSvkvLSGGEKGRMLFGKLMM 454
|
170
....*....|....*.
gi 296439455 544 GDPQVLLLDEPTAGLD 559
Cdd:PRK15064 455 QKPNVLVMDEPTNHMD 470
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1229-1410 |
6.66e-11 |
|
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: 64.35 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrqqhdnslkflgYCPQEnsLWPKLTMKEHLELYAAV 1308
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQY--IKADYEGTVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1309 KGLGKEdaALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKN 1388
Cdd:cd03237 87 KDFYTH--PYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180
....*....|....*....|..
gi 296439455 1389 KERGTLLTTHYMSEAEAVCDRM 1410
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRL 186
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1221-1429 |
7.46e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 64.27 E-value: 7.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQ-HDNSLKFL----GYCPQENSLWPK 1295
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpSDKAIRELrrnvGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEG 1374
Cdd:PRK11124 97 LTVQQNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1375 QQQMWQILqatvknKE-RGTLLT----THYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:PRK11124 177 TAQIVSII------RElAETGITqvivTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
391-559 |
8.87e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 62.93 E-value: 8.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKtgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVS--TEGSATIYNTQLSEITDMEEIR 468
Cdd:cd03217 1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDITDLPPEERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 469 KNIGFCPQFNFQFDFLTVRENLRvfakikgiqpkeveqevkriimELDMqsiqdiiakKLSGGQKRKLTLGIAILGDPQV 548
Cdd:cd03217 77 LGIFLAFQYPPEIPGVKNADFLR----------------------YVNE---------GFSGGEKKRNEILQLLLLEPDL 125
|
170
....*....|.
gi 296439455 549 LLLDEPTAGLD 559
Cdd:cd03217 126 AILDEPDSGLD 136
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
397-559 |
1.06e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.89 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 397 IKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSG---LSVsTEGSATIYNtqlSEITDME-EIRKNIG 472
Cdd:CHL00131 10 IKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaYKI-LEGDILFKG---ESILDLEpEERAHLG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 473 FCPQFNFQF--------DFLTVRENL-RVFAKIKGIQPKEVEQEVKRIIMELDMQS--IQDIIAKKLSGGQ-KRKLTLGI 540
Cdd:CHL00131 86 IFLAFQYPIeipgvsnaDFLRLAYNSkRKFQGLPELDPLEFLEIINEKLKLVGMDPsfLSRNVNEGFSGGEkKRNEILQM 165
|
170
....*....|....*....
gi 296439455 541 AILgDPQVLLLDEPTAGLD 559
Cdd:CHL00131 166 ALL-DSELAILDETDSGLD 183
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1225-1422 |
1.07e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 65.63 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSlKFLGYCPQENSLWPKLTMKEHLEL 1304
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-RRVASVPQDTSLSFEFDVRQVVEM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1305 -----YAAVKGLGKEDAAlSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMW 1379
Cdd:PRK09536 101 grtphRSRFDTWTETDRA-AVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTL 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1380 QILQATVKNkERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:PRK09536 180 ELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1218-1418 |
1.40e-10 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 63.49 E-value: 1.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSL-KFLGYCPQENSLWPKL 1296
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDK--PISMLSSRQLaRRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKE--------HLELYAAvkgLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPF 1367
Cdd:PRK11231 92 TVRElvaygrspWLSLWGR---LSAEDNAR-VNQAMEQTRINHLADRRLTDLSGG-QRQRAFLAMVLAqDTPVVLLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1368 TGMDPEGQQQMWQILQATvkNKERGTLLTT-HYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK11231 167 TYLDINHQVELMRLMREL--NTQGKTVVTVlHDLNQASRYCDHLVVLANGHV 216
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
415-560 |
1.41e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyNTQLSEITDMEEIRKNIGFCPQFNFQFDFLtvrENLRVFA 494
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQI-DGKTATRGDRSRFMAYLGHLPGLKADLSTL---ENLHFLC 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 495 KIKGIQPKEVEQEVKRIImelDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:PRK13543 108 GLHGRRAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
391-597 |
1.41e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYN-----GKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEI--TD 463
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLnrAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 464 MEEIRKNIgfcpQFNFQFDFLTVRENLRVFAKIKgiQP-------KEVEQEVKRIIMeLDMQSIQDIIAKK----LSGGQ 532
Cdd:PRK10419 84 RKAFRRDI----QMVFQDSISAVNPRKTVREIIR--EPlrhllslDKAERLARASEM-LRAVDLDDSVLDKrppqLSGGQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 533 KRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFSTQ-------------FMDEADILADRKV 597
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHdlrlverfcqrvmVMDNGQIVETQPV 236
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1194-1433 |
1.44e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 63.55 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1194 PVITASCLHKEYyeTKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------ 1267
Cdd:PRK10419 2 TLLNVSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGeplakl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1268 SRASVRQ-QHDNSLKFlgycpQE--NSLWPKLTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPvKTLS 1341
Cdd:PRK10419 80 NRAQRKAfRRDIQMVF-----QDsiSAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDDSVldKRP-PQLS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1342 EGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL- 1418
Cdd:PRK10419 154 GGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKL--QQQFGTacLFITHDLRLVERFCQRVMVMDNGQIv 231
|
250
....*....|....*..
gi 296439455 1419 --RCIGSIQHLKNKFGR 1433
Cdd:PRK10419 232 etQPVGDKLTFSSPAGR 248
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1212-1425 |
1.46e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 63.60 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-------------SRASVRQQHdn 1278
Cdd:COG4559 8 SVRLGGRTL-LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGrplaawspwelarRRAVLPQHS-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1279 SLKF---------LGYCPQENSlwpkltmkeHLELYAAVkglgkeDAALsisRLVEALKLQEQLkapVKTLSEGIK---- 1345
Cdd:COG4559 85 SLAFpftveevvaLGRAPHGSS---------AAQDRQIV------REAL---ALVGLAHLAGRS---YQTLSGGEQqrvq 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1346 --RKLCFVL-SILGNPSVVLLDEPFTGMDPeGQQQmwQILQATVKNKERGT--------L-LTTHYmseaeavCDRMAMM 1413
Cdd:COG4559 144 laRVLAQLWePVDGGPRWLFLDEPTSALDL-AHQH--AVLRLARQLARRGGgvvavlhdLnLAAQY-------ADRILLL 213
|
250
....*....|..
gi 296439455 1414 VSGTLRCIGSIQ 1425
Cdd:COG4559 214 HQGRLVAQGTPE 225
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1221-1371 |
1.48e-10 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 62.97 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrQQHDNSLKFL----GYCPQENSLWPKL 1296
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDIT--RLKNREVPFLrrqiGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1297 TMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMD 1371
Cdd:PRK10908 95 TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1215-1418 |
1.57e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 64.03 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGsrasVRQQHDNSLKFLGYCPQ------ 1288
Cdd:PRK13646 16 TPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDD----ITITHKTKDKYIRPVRKrigmvf 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 ---ENSLWPKLTMKEHLelyaavkgLGKEDAALSISRLVE-ALKLQEQL--------KAPVKtLSEGIKRKLCFVlSILG 1356
Cdd:PRK13646 92 qfpESQLFEDTVEREII--------FGPKNFKMNLDEVKNyAHRLLMDLgfsrdvmsQSPFQ-MSGGQMRKIAIV-SILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1357 -NPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK13646 162 mNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
393-559 |
1.61e-10 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.73 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGKTgkvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitdMEEIRknIG 472
Cdd:TIGR03719 7 MNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIK--VG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 473 FCPQfNFQFD-FLTVRENLrvfakikgiqpKEVEQEVKRIIMELD-------------------MQSIQDIIA------- 525
Cdd:TIGR03719 72 YLPQ-EPQLDpTKTVRENV-----------EEGVAEIKDALDRFNeisakyaepdadfdklaaeQAELQEIIDaadawdl 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 526 --------------------KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:TIGR03719 140 dsqleiamdalrcppwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1215-1401 |
1.84e-10 |
|
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: 62.94 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRasVRQQHDNSL-KFLGYCPQEnslw 1293
Cdd:cd03249 12 SRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVD--IRDLNLRWLrSQIGLVSQE---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKL---TMKEHLelyaavkGLGKEDA----ALSISRLVEA----LKLQEQLKAPV----KTLSEGIKRKLCFVLSILGNP 1358
Cdd:cd03249 86 PVLfdgTIAENI-------RYGKPDAtdeeVEEAAKKANIhdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 296439455 1359 SVVLLDEPFTGMDPEGQqqmwQILQATVKN--KERGTLLTTHYMS 1401
Cdd:cd03249 159 KILLLDEATSALDAESE----KLVQEALDRamKGRTTIVIAHRLS 199
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
389-605 |
1.86e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.30 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEY----------------NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAT 452
Cdd:PRK13546 3 VSVNIKNVTKEYriyrtnkermkdalipKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 453 IYNtqlseitDMEEIRKNIGFCPQfnfqfdfLTVRENLRVFAKIKGIQPKEVEQEVKRIImelDMQSIQDII---AKKLS 529
Cdd:PRK13546 83 RNG-------EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKII---EFSELGEFIyqpVKKYS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 530 GGQKRKLTLGIAILGDPQVLLLDEP-TAGLDPFSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKLK 605
Cdd:PRK13546 146 SGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1214-1383 |
1.87e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.97 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1214 STRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSL 1292
Cdd:PRK11614 12 SAHYGKIqALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLTMKEHLelyaAVKGL--GKEDAALSISRLVEAL-KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTG 1369
Cdd:PRK11614 92 FSRMTVEENL----AMGGFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
|
170
....*....|....
gi 296439455 1370 MDPEGQQQMWQILQ 1383
Cdd:PRK11614 168 LAPIIIQQIFDTIE 181
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1213-1398 |
1.89e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 62.42 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASV------RQQhdnslkfLGYC 1286
Cdd:PRK10247 15 YLAGDAKI-LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeiyRQQ-------VSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQ----------ENSLWPKLTMKEHLELYAAVKGLGKEDAALSIsrlvealklqeqLKAPVKTLSEGIKRKLCFVLSILG 1356
Cdd:PRK10247 87 AQtptlfgdtvyDNLIFPWQIRNQQPDPAIFLDDLERFALPDTI------------LTKNIAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 296439455 1357 NPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTH 1398
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1221-1489 |
2.11e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 63.47 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQE-NSLWPKLTMK 1299
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNpETQFVGRTVE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 EHLelyaavkGLGKEDAALS-------ISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:PRK13644 97 EDL-------AFGPENLCLPpieirkrVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1373 EGQQqmwQILQATVKNKERGTLL--TTHYMSEAEAVcDRMAMMVSGTLRCIGSIQhlkNKFGRDYLLEIKMKEPTQVEAl 1450
Cdd:PRK13644 170 DSGI---AVLERIKKLHEKGKTIvyITHNLEELHDA-DRIIVMDRGKIVLEGEPE---NVLSDVSLQTLGLTPPSLIEL- 241
|
250 260 270
....*....|....*....|....*....|....*....
gi 296439455 1451 hTEILKLFPQAAWQERYSSlmayklPVEDVHPLSRAFFK 1489
Cdd:PRK13644 242 -AENLKMHGVVIPWENTSS------PSSFAEEICRLFLK 273
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1222-1418 |
2.47e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 2.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKP----TAGVVVLQGSR---ASVRQQHDNSLkflgycpQEN---S 1291
Cdd:PRK10418 19 VHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPvapCALRGRKIATI-------MQNprsA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEH-LELYAAvkgLGKEDAALSISRLVEALKLQEQ---LKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:PRK10418 92 FNPLHTMHTHaRETCLA---LGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1368 TGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK10418 169 TDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
389-572 |
3.63e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 3.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 389 EAIRIRNVIKEYN-------GKTGkvealqgifFDIY------EGQITAILGHNGAGKSTLLNILSGLSVSTEGsatIYN 455
Cdd:COG1245 64 DAISIVNLPEELEedpvhryGENG---------FRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYD 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 456 TQLSEitdmEEIRKnigfcpqfNFQ----FDFLT-VREN-LRVFAKIKGIQ--PKEVEQEVK-------------RIIME 514
Cdd:COG1245 132 EEPSW----DEVLK--------RFRgtelQDYFKkLANGeIKVAHKPQYVDliPKVFKGTVRellekvdergkldELAEK 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 515 LDMQSI--QDIiaKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:COG1245 200 LGLENIldRDI--SELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRE 257
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1221-1422 |
3.75e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 64.49 E-value: 3.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR-----ASVRQQHDNSLKFLGYCPQEnSLWPK 1295
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRidtlsPGKLQALRRDIQFIFQDPYA-SLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALS-ISRLVE--ALKLQEQLKAPvKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:PRK10261 418 QTVGDSIMEPLRVHGLLPGKAAAArVAWLLErvGLLPEHAWRYP-HEFSGGQRQRICIARALALNPKVIIADEAVSALDV 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 1373 EGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:PRK10261 497 SIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1218-1443 |
4.12e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 62.51 E-value: 4.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTA---------GVVVLQGSRASVR-------QQHDNslK 1281
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAKTVWDIRekvgivfQNPDN--Q 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1282 FLGycpqenslwpkLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCfVLSILG-NPSV 1360
Cdd:PRK13640 97 FVG-----------ATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA-IAGILAvEPKI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEA-----VCDRMAMMVSGTLRCIGSIQHLKNKFGRD- 1434
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMadqvlVLDDGKLLAQGSPVEIFSKVEMLKEIGLDi 244
|
250
....*....|..
gi 296439455 1435 ---YLLEIKMKE 1443
Cdd:PRK13640 245 pfvYKLKNKLKE 256
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1193-1267 |
5.02e-10 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 62.83 E-value: 5.02e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1193 EPVITASCLHKeYYETKKSCFSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG 1267
Cdd:COG4608 5 EPLLEVRDLKK-HFPVRGGLFGRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDG 79
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
419-572 |
5.71e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 5.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 419 EGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntQLSEITDMEEIRKnigfcpQFN---FQFDFLTVREN-LRVFA 494
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLG-------DYEEEPSWDEVLK------RFRgteLQNYFKKLYNGeIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 495 KIKGIQ--PK----EVEQEVKR---------IIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK13409 165 KPQYVDliPKvfkgKVRELLKKvdergkldeVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170
....*....|...
gi 296439455 560 PFSRHRVWSLLKE 572
Cdd:PRK13409 245 IRQRLNVARLIRE 257
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1221-1427 |
5.93e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 5.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVK-------------KGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-------SRASVRQqhdnsl 1280
Cdd:PRK10575 13 ALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpleswsSKAFARK------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1281 kfLGYCPQENSLWPKLTMKEHLEL-----YAAVKGLGKEDAAlsisRLVEALKLQEqLKaP-----VKTLSEGIKRKLCF 1350
Cdd:PRK10575 87 --VAYLPQQLPAAEGMTVRELVAIgrypwHGALGRFGAADRE----KVEEAISLVG-LK-PlahrlVDSLSGGERQRAWI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1351 VLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERG-TLLTT-HYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:PRK10575 159 AMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL--SQERGlTVIAVlHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1222-1418 |
6.15e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 61.47 E-value: 6.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTK--PTA---GVVVLQGS------------RASVRQQHDNSLKFLG 1284
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQdifkmdvielrrRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1285 YCpqEN-SLWPKLT--MKEHLELYAAVKglgkedAALSISRLVEALKlqEQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:PRK14247 99 IF--ENvALGLKLNrlVKSKKELQERVR------WALEKAQLWDEVK--DRLDAPAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1362 LLDEPFTGMDPEGQQQMwQILQATVKnKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK14247 169 LADEPTANLDPENTAKI-ESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1217-1457 |
6.32e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 63.67 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCT--KPTAGVVVLQGSRASVRQQHDNSLKFLGYCP------- 1287
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIIYHVALCEKCGYVERPSKVGEPCPvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 -QENSLWP-------------KLTMKEHLELYA----------AVKGLGKE--DAALSISRLVEALKLQEQLKAPVKTLS 1341
Cdd:TIGR03269 91 pEEVDFWNlsdklrrrirkriAIMLQRTFALYGddtvldnvleALEEIGYEgkEAVGRAVDLIEMVQLSHRITHIARDLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1342 EGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCI 1421
Cdd:TIGR03269 171 GGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSDKAIWLENGEIKEE 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 296439455 1422 GSIQHLKNKFgrdyLLEIKMKEPTQVEALHTEILKL 1457
Cdd:TIGR03269 251 GTPDEVVAVF----MEGVSEVEKECEVEVGEPIIKV 282
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
391-572 |
1.02e-09 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 60.96 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTG-----KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS------ 459
Cdd:PRK15112 5 LEVRNLSKTFRYRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 ----------EITDMEEIRKNIGfcpqfnfQFDFLTVRENlrvfakiKGIQPKEVEqevKRIIMELDMQSIQDIIAK--- 526
Cdd:PRK15112 85 rsqrirmifqDPSTSLNPRQRIS-------QILDFPLRLN-------TDLEPEQRE---KQIIETLRQVGLLPDHASyyp 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 527 -KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE 572
Cdd:PRK15112 148 hMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLE 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
380-609 |
1.04e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.46 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPefhGKEAIRIRNVIKEYNGKTGKvEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqls 459
Cdd:PLN03232 607 PLQP---GAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------ 676
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 eitdmeeIRKNIGFCPQFNFQFDfLTVRENLRVFAKIkgiqpkeveqEVKRIIMELDMQSIQ---DIIAKK--------- 527
Cdd:PLN03232 677 -------IRGSVAYVPQVSWIFN-ATVRENILFGSDF----------ESERYWRAIDVTALQhdlDLLPGRdlteigerg 738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 528 --LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVW-SLLKEH---KVDRLILFSTQFMDeadiLADRKVFLSN 601
Cdd:PLN03232 739 vnISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFdSCMKDElkgKTRVLVTNQLHFLP----LMDRIILVSE 814
|
....*...
gi 296439455 602 GKLKCAGS 609
Cdd:PLN03232 815 GMIKEEGT 822
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
378-559 |
1.17e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.88 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 378 FE--PVSPEFHGKEAIRIRNVIKEYNGKTGKVEAlqGiffDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATiyn 455
Cdd:COG1245 327 FEvhAPRREKEEETLVEYPDLTKSYGGFSLEVEG--G---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD--- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 456 tqlseitdmEEIRknIGFCPQFNFQFDFLTVRENLRVFAKiKGIQPKEVEQEvkrIIMELDMQSIQDIIAKKLSGGQKRK 535
Cdd:COG1245 399 ---------EDLK--ISYKPQYISPDYDGTVEEFLRSANT-DDFGSSYYKTE---IIKPLGLEKLLDKNVKDLSGGELQR 463
|
170 180
....*....|....*....|....
gi 296439455 536 LTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:COG1245 464 VAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
394-604 |
1.18e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.82 E-value: 1.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGKTGKVE-ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEI----- 467
Cdd:PRK10982 247 GEVILEVRNLTSLRQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAInhgfa 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 468 -----RKNIGFCPQFNFQFDFLTvrENLRVF-AKIKGIQPKEVEQEVKRII--MELDMQSIQDIIAKkLSGGQKRKLTLG 539
Cdd:PRK10982 327 lvteeRRSTGIYAYLDIGFNSLI--SNIRNYkNKVGLLDNSRMKSDTQWVIdsMRVKTPGHRTQIGS-LSGGNQQKVIIG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 540 IAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK10982 404 RWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1221-1437 |
1.44e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYCPQENSLWP 1294
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGqpiadySEAALRQA-------ISVVSQRVHLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KlTMKEHLELyaavkglGKEDAalSISRLVEAL------KLQEQLKaPVKT--------LSEGIKRKLCFVLSILGNPSV 1360
Cdd:PRK11160 428 A-TLRDNLLL-------AAPNA--SDEALIEVLqqvgleKLLEDDK-GLNAwlgeggrqLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKergTLLT-THYMSEAEAVcDRMAMMVSGTLRCIGSIQHLKNKFGRDYLL 1437
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNK---TVLMiTHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1212-1402 |
1.73e-09 |
|
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: 59.94 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRasVRQQHDNSL-KFLGYCPQEN 1290
Cdd:cd03253 7 TFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQD--IREVTLDSLrRAIGVVPQDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 SLW------------PKLTmKEhlELYAAVKGLGKEDaalSISRLVEAL--KLQEQ-LKapvktLSEGIKRKLCFVLSIL 1355
Cdd:cd03253 85 VLFndtigynirygrPDAT-DE--EVIEAAKAAQIHD---KIMRFPDGYdtIVGERgLK-----LSGGEKQRVAIARAIL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSE 1402
Cdd:cd03253 154 KNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLST 198
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1217-1373 |
2.02e-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: 61.87 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAsvrqqhdnslkfLGYCPQENSLWPKL 1296
Cdd:TIGR03719 17 KKEI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIK------------VGYLPQEPQLDPTK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHL---------------ELYAAvkgLGKEDAALSiSRLVEALKLQEQLKA------------------------PV 1337
Cdd:TIGR03719 84 TVRENVeegvaeikdaldrfnEISAK---YAEPDADFD-KLAAEQAELQEIIDAadawdldsqleiamdalrcppwdaDV 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 296439455 1338 KTLSEGIKRK--LCFVLsiLGNPSVVLLDEPFTGMDPE 1373
Cdd:TIGR03719 160 TKLSGGERRRvaLCRLL--LSKPDMLLLDEPTNHLDAE 195
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
406-604 |
2.24e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 61.85 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 406 KVEALQG------IFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQfNF 479
Cdd:PRK11288 259 RLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPE-DR 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 QFD----FLTVRENL-----RVFAKIKG-IQPKEVEQEVKRIIMELDMQSI---QDIIAkkLSGGQKRKltlgiAILG-- 544
Cdd:PRK11288 338 KAEgiipVHSVADNInisarRHHLRAGClINNRWEAENADRFIRSLNIKTPsreQLIMN--LSGGNQQK-----AILGrw 410
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 545 ---DPQVLLLDEPTAGLDPFSRHRVWSLLKE-HKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK11288 411 lseDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
368-559 |
2.72e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 61.72 E-value: 2.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 368 INPEHSSDD-SFEPVSPEFHGKEAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVS 446
Cdd:PRK10636 289 IAPAHVDNPfHFSFRAPESLPNPLLKMEKVSAGYGDRI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAP 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 447 TEGsatiyntqlsEITDMEEIRknIGFCPQFnfQFDFLTVREN-LRVFAKIKgiqPKEVEQEVKRIIMELDMQSIQ-DII 524
Cdd:PRK10636 365 VSG----------EIGLAKGIK--LGYFAQH--QLEFLRADESpLQHLARLA---PQELEQKLRDYLGGFGFQGDKvTEE 427
|
170 180 190
....*....|....*....|....*....|....*
gi 296439455 525 AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK10636 428 TRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
425-559 |
2.80e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 425 ILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitdMEEIRknIGFCPQfNFQFD-FLTVRENlrvfakikgiqpke 503
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIK--VGYLPQ-EPQLDpEKTVREN-------------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 504 VE---QEVKRIIMELD-------------------MQSIQDIIA---------------------------KKLSGGQKR 534
Cdd:PRK11819 91 VEegvAEVKAALDRFNeiyaayaepdadfdalaaeQGELQEIIDaadawdldsqleiamdalrcppwdakvTKLSGGERR 170
|
170 180
....*....|....*....|....*
gi 296439455 535 KLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK11819 171 RVALCRLLLEKPDMLLLDEPTNHLD 195
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1418 |
3.15e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 60.25 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQ----GSRASVRQQHDNSL-----------KFLGY 1285
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYskkiknfkelrRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1286 CPQ--ENSLWpKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQL--KAPVKtLSEGIKRKLCF--VLSIlgNPS 1359
Cdd:PRK13631 121 VFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYleRSPFG-LSGGQKRRVAIagILAI--QPE 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1360 VVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLIL-DAKANNKTVFVITHTMEHVLEVADEVIVMDKGKI 254
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
357-566 |
3.66e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 3.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 357 QNTHHEIFENEINPEhSSDDSFEPVSPEfhGKEAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTL 436
Cdd:PRK10938 230 QLAHSEQLEGVQLPE-PDEPSARHALPA--NEPRIVLNNGVVSYNDRP----ILHNLSWQVNPGEHWQIVGPNGAGKSTL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 437 LNILSG-----------LSVSTEGSA-TIYntqlseitdmeEIRKNIGFCPQfNFQFDFlTVRENLR------VFAKIkG 498
Cdd:PRK10938 303 LSLITGdhpqgysndltLFGRRRGSGeTIW-----------DIKKHIGYVSS-SLHLDY-RVSTSVRnvilsgFFDSI-G 368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 499 IQpKEVEQEVKRIIME-LDMQSIQDIIAKK----LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRV 566
Cdd:PRK10938 369 IY-QAVSDRQQKLAQQwLDILGIDKRTADApfhsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLV 440
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
377-559 |
3.69e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 61.36 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 377 SFE--PVSPEFHGKEAIRIRNVIKEYNGKTGKVEALQgiffdIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIy 454
Cdd:PRK13409 325 EFEerPPRDESERETLVEYPDLTKKLGDFSLEVEGGE-----IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 455 ntqlseitdmeEIRknIGFCPQFnFQFDF-LTVRENLRVFAKIKGIQPKEVEqevkrIIMELDMQSIQDIIAKKLSGGQK 533
Cdd:PRK13409 399 -----------ELK--ISYKPQY-IKPDYdGTVEDLLRSITDDLGSSYYKSE-----IIKPLQLERLLDKNVKDLSGGEL 459
|
170 180
....*....|....*....|....*.
gi 296439455 534 RKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK13409 460 QRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1221-1413 |
4.11e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 58.60 E-value: 4.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAG-VVVLQG------SRASVRQ-----QHDnslkfLGYCPQ 1288
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsILVRHDggwvdlAQASPREilalrRRT-----IGYVSQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 ENSLWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQL-KAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:COG4778 101 FLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPT 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 296439455 1368 TGMDPEGQQQMWQILQATvknKERGTLLTT--HYMSEAEAVCDRMAMM 1413
Cdd:COG4778 181 ASLDAANRAVVVELIEEA---KARGTAIIGifHDEEVREAVADRVVDV 225
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1225-1384 |
4.57e-09 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 58.79 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTkPTAGVVVLQGSRASVRQQHDNSlKFLGYCPQENSLWPKLTMKEHLEL 1304
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELA-RHRAYLSQQQTPPFAMPVFQYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1305 YAAVkGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPFTGMDPEGQQQ 1377
Cdd:PRK03695 93 HQPD-KTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDVAQQAA 171
|
....*..
gi 296439455 1378 MWQILQA 1384
Cdd:PRK03695 172 LDRLLSE 178
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
376-609 |
5.01e-09 |
|
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: 61.50 E-value: 5.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 376 DSFE--PVSPefHGKEAIRIRNVIkeYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATi 453
Cdd:TIGR00957 622 DSIErrTIKP--GEGNSITVHNAT--FTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVH- 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 454 yntqlseitdmeeIRKNIGFCPQFNF-QFDflTVRENLrVFAkiKGIQPKEVEQEVKRIIMELDMQSI----QDIIAKK- 527
Cdd:TIGR00957 697 -------------MKGSVAYVPQQAWiQND--SLRENI-LFG--KALNEKYYQQVLEACALLPDLEILpsgdRTEIGEKg 758
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 528 --LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWS-------LLKeHKVDRLILFSTQFMDEADILadrkVF 598
Cdd:TIGR00957 759 vnLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEhvigpegVLK-NKTRILVTHGISYLPQVDVI----IV 833
|
250
....*....|.
gi 296439455 599 LSNGKLKCAGS 609
Cdd:TIGR00957 834 MSGGKISEMGS 844
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
370-564 |
5.52e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 5.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 370 PEHSSDDSFEPVSPEFHGKEAIRIRNVIKEYNGKTG-KVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTE 448
Cdd:COG4615 307 AAAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDGdEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPES 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 449 GSATIYNTQLSEiTDMEEIRKNigFCPQFNfqfDFltvrenlRVFAKIKGIQPKEVEQEVKRIIMELDMQ---SIQD--I 523
Cdd:COG4615 387 GEILLDGQPVTA-DNREAYRQL--FSAVFS---DF-------HLFDRLLGLDGEADPARARELLERLELDhkvSVEDgrF 453
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 296439455 524 IAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRH 564
Cdd:COG4615 454 STTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEFRR 494
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1213-1404 |
5.80e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 58.25 E-value: 5.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvrqQHDNslKFL----GYCPQ 1288
Cdd:cd03248 21 YPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS---QYEH--KYLhskvSLVGQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 ENSLWPK---------LTMKEHLELYAAVKGLGKEDaalSISRLveALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPS 1359
Cdd:cd03248 96 EPVLFARslqdniaygLQSCSFECVKEAAQKAHAHS---FISEL--ASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 296439455 1360 VVLLDEPFTGMDPEGQQQMWQILQATvkNKERGTLLTTHYMSEAE 1404
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVE 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1222-1418 |
5.92e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 5.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHD---NSLKFLGYCPQENSLWPKLTM 1298
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglaNGIVYISEDRKRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYA------AVKGLGKEDAALSISRLVEALKL----QEQlkaPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFT 1368
Cdd:PRK10762 348 KENMSLTAlryfsrAGGSLKHADEQQAVSDFIRLFNIktpsMEQ---AIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1369 GMDPEGQQQMWQILQatvKNKERG--TLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK10762 425 GVDVGAKKEIYQLIN---QFKAEGlsIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1212-1427 |
6.25e-09 |
|
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: 58.40 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIAI-RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLG 1284
Cdd:cd03251 7 TFRYPGDGPPVlRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGhdvrdyTLASLRRQ-------IG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1285 YCPQENSLWPKlTMKEHLeLYaavkglGKEDAA----LSISRLVEAL----KLQEQLKAPVK----TLSEGIKRKLCFVL 1352
Cdd:cd03251 80 LVSQDVFLFND-TVAENI-AY------GRPGATreevEEAARAANAHefimELPEGYDTVIGergvKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1353 SILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSEAEAVcDRMAMMVSGTLRCIGSIQHL 1427
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEEL 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
413-597 |
6.38e-09 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 58.62 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 413 IFFDIY----EGQITAILGHNGAGKSTLLNILSGlSVSTEGSATIYNTQ----LSEiTDMEEIRKNIGFCPQFNFQFDFL 484
Cdd:PRK11831 22 IFDNISltvpRGKITAIMGPSGIGKTTLLRLIGG-QIAPDHGEILFDGEnipaMSR-SRLYTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 485 TVREN----LRVFAKIkgiqPKEVEQEVkrIIMELD---MQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:PRK11831 100 NVFDNvaypLREHTQL----PAPLLHST--VMMKLEavgLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 558 LDPFSRHRVWSLLKE-------------HKVDRLIlfstQFMDEADILADRKV 597
Cdd:PRK11831 174 QDPITMGVLVKLISElnsalgvtcvvvsHDVPEVL----SIADHAYIVADKKI 222
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1222-1459 |
9.80e-09 |
|
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: 58.33 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKST----SIKMITgctkpTAGVVVLQG-SRASVRQQHDNslKFLGYCPQENSLWPKl 1296
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTllsaFLRLLN-----TEGDIQIDGvSWNSVPLQKWR--KAFGVIPQKVFIFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAVKG--LGKEDAALSISRLVEAL--KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:cd03289 92 TFRKNLDPYGKWSDeeIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDP 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1373 egqqQMWQILQATVKNKERG-TLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKfgrdylleikmKEPTQVEALH 1451
Cdd:cd03289 172 ----ITYQVIRKTLKQAFADcTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNE-----------KSHFKQAISP 236
|
....*...
gi 296439455 1452 TEILKLFP 1459
Cdd:cd03289 237 SDRLKLFP 244
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1224-1418 |
1.04e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.80 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1224 NVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG-----SRASVRQQHDNSlkflGYCPQENSLWPKLTM 1298
Cdd:PRK09493 19 NIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvndPKVDERLIRQEA----GMVFQQFYLFPHLTA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1299 KEHLELYAA-VKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQ 1377
Cdd:PRK09493 95 LENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1378 MWQILQATVknkERG--TLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK09493 175 VLKVMQDLA---EEGmtMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
409-553 |
1.05e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 409 ALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSatiyntqlseiTDMEEIRKNIGFCPQFNFQfdfLTVRE 488
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGT-----------VDIKGSAALIAISSGLNGQ---LTGIE 104
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 489 NLRVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDE 553
Cdd:PRK13545 105 NIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1221-1416 |
1.05e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 58.21 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKfLGYCPQEnslwP-----K 1295
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSK-VGLVFQD----PddqvfS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAAlsiSRLVEALK---LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP 1372
Cdd:PRK13647 95 STVWDDVAFGPVNMGLDKDEVE---RRVEEALKavrMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 296439455 1373 EGQQQMWQILqATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK13647 172 RGQETLMEIL-DRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
394-558 |
1.10e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 394 RNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL--SVSTEGSATIYNTQL--SEITDMEE--- 466
Cdd:PRK13549 9 KNITKTFGG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELqaSNIRDTERagi 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 --IRKNIGFCPQfnfqfdfLTVRENLRVFAKI-KG--IQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIA 541
Cdd:PRK13549 85 aiIHQELALVKE-------LSVLENIFLGNEItPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170
....*....|....*..
gi 296439455 542 ILGDPQVLLLDEPTAGL 558
Cdd:PRK13549 158 LNKQARLLILDEPTASL 174
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
357-572 |
1.10e-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: 59.70 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 357 QNTHHEIFENeinPEH-------SSDDSFEPVSPEFHGKEAIRIRNVIKEYNGKTG-------KVEALQGIFFDIYEGQI 422
Cdd:COG4172 238 QGPTAELFAA---PQHpytrkllAAEPRGDPRPVPPDAPPLLEARDLKVWFPIKRGlfrrtvgHVKAVDGVSLTLRRGET 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 423 TAILGHNGAGKSTL-LNILsGLsVSTEGSATIYNTQLSEIT--DMEEIRKNIgfcpQFNFQFDF------LTVR----EN 489
Cdd:COG4172 315 LGLVGESGSGKSTLgLALL-RL-IPSEGEIRFDGQDLDGLSrrALRPLRRRM----QVVFQDPFgslsprMTVGqiiaEG 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAkiKGIQPKEVEQEVKRIIME--LDmqsiQDIIAK---KLSGGQK-RkltLGIA---ILgDPQVLLLDEPTAGLDP 560
Cdd:COG4172 389 LRVHG--PGLSAAERRARVAEALEEvgLD----PAARHRyphEFSGGQRqR---IAIAralIL-EPKLLVLDEPTSALDV 458
|
250
....*....|..
gi 296439455 561 FSRHRVWSLLKE 572
Cdd:COG4172 459 SVQAQILDLLRD 470
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1222-1409 |
1.11e-08 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 57.77 E-value: 1.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvLQGSRASVRQQHDNSLKFlgycpQENSLWPKLTMKEH 1301
Cdd:PRK11247 28 LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTAPLAEAREDTRLMF-----QDARLLPWKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LELyaavkGL-GK-EDAALsisRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDP----EGQ 1375
Cdd:PRK11247 102 VGL-----GLkGQwRDAAL---QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDAltriEMQ 173
|
170 180 190
....*....|....*....|....*....|....*..
gi 296439455 1376 Q---QMWQILQATVknkergtLLTTHYMSEAEAVCDR 1409
Cdd:PRK11247 174 DlieSLWQQHGFTV-------LLVTHDVSEAVAMADR 203
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
406-604 |
1.21e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 59.29 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 406 KVEALQG-----IFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQ---- 476
Cdd:PRK15439 270 TVEDLTGegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPEdrqs 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 477 -----------------FNFQFDFL-TVRENLRV--FAKIKGIQPKEVEQEVKRiimeldmqsiqdiiakkLSGGQKRKL 536
Cdd:PRK15439 350 sglyldaplawnvcaltHNRRGFWIkPARENAVLerYRRALNIKFNHAEQAART-----------------LSGGNQQKV 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 537 TLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRL-ILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1221-1423 |
1.31e-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: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKfLGYCPQENSLWPKlTMKE 1300
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSS-LTIIPQDPTLFSG-TIRS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYaavkglGKEDAAlsisRLVEALKLQEQlkapVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQ 1380
Cdd:cd03369 101 NLDPF------DEYSDE----EIYGALRVSEG----GLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1381 ILQATVKNkerGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:cd03369 167 TIREEFTN---STILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1222-1373 |
1.56e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.14 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsrasvrQQHDNSLkfLGYCPQEN----------- 1290
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENAN--IGYYAQDHaydfendltlf 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 ---SLWpklTMKEHLELyaAVKG-LGkedaalsisRLveaLKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK15064 403 dwmSQW---RQEGDDEQ--AVRGtLG---------RL---LFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEP 465
|
....*..
gi 296439455 1367 FTGMDPE 1373
Cdd:PRK15064 466 TNHMDME 472
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1193-1436 |
1.65e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.09 E-value: 1.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1193 EPVITASCLHKeYYETKKscfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMIT--GCTKP---TAGVVVLQG 1267
Cdd:PRK14239 3 EPILQVSDLSV-YYNKKK----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1268 SRA-SVRQQHDNSLKFLGYCPQENSLWPkLTMKEHLeLY----AAVKGLGKEDAALSISRLVEAL--KLQEQLKAPVKTL 1340
Cdd:PRK14239 72 HNIySPRTDTVDLRKEIGMVFQQPNPFP-MSIYENV-VYglrlKGIKDKQVLDEAVEKSLKGASIwdEVKDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1341 SEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATvknKERGTLLT-THYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL---KDDYTMLLvTRSMQQASRISDRTGFFLDGDLI 226
|
250 260
....*....|....*....|.
gi 296439455 1420 CIGSIQHL----KNKFGRDYL 1436
Cdd:PRK14239 227 EYNDTKQMfmnpKHKETEDYI 247
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
415-559 |
1.76e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSaTIYNTQLSeITDMEEIrknigfcPQFNFQ---FDFLT-----V 486
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLI-VARLQQD-------PPRNVEgtvYDFVAegieeQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 487 RENLRVFAKIK---GIQPKE-VEQEVKRIIMELDMQS-------IQDIIAK----------KLSGGQKRKLTLGIAILGD 545
Cdd:PRK11147 95 AEYLKRYHDIShlvETDPSEkNLNELAKLQEQLDHHNlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 296439455 546 PQVLLLDEPTAGLD 559
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
410-574 |
1.76e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.11 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEitDMEEIRKNIGFCPQFNFQFDFLTVREN 489
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK--DLCTYQKQLCFVGHRSGINPYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LrvfakIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:PRK13540 95 C-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
....*
gi 296439455 570 LKEHK 574
Cdd:PRK13540 170 IQEHR 174
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1222-1459 |
2.00e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKpTAGVVVLQG-SRASVRQQhdNSLKFLGYCPQENSLWPKlTMKE 1300
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGvSWNSVTLQ--TWRKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYA--AVKGLGKEDAALSISRLVEAL--KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPegqq 1376
Cdd:TIGR01271 1311 NLDPYEqwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDP---- 1386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1377 QMWQILQATVKNK-ERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNKFGrdyLLEIKMKeptqvealHTEIL 1455
Cdd:TIGR01271 1387 VTLQIIRKTLKQSfSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETS---LFKQAMS--------AADRL 1455
|
....
gi 296439455 1456 KLFP 1459
Cdd:TIGR01271 1456 KLFP 1459
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
380-559 |
2.06e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 2.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPEFhGKEAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNT-QL 458
Cdd:TIGR03719 313 PPGPRL-GDKVIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvKL 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 459 S-----------------EITDMEEIRKnIG--------FCPQFNFqfdfltvrenlrvfakiKGiqpkeVEQEvKRIim 513
Cdd:TIGR03719 388 AyvdqsrdaldpnktvweEISGGLDIIK-LGkreipsraYVGRFNF-----------------KG-----SDQQ-KKV-- 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 514 eldmqsiqdiiaKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:TIGR03719 442 ------------GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1218-1423 |
2.13e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 57.02 E-value: 2.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSraSVRQQHDNSL-KFLGYCPQENSLWPKL 1296
Cdd:COG4604 13 GKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGL--DVATTPSRELaKRLAILRQENHINSRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLEL--YAAVKG-LGKEDAALsISRLVEALKLQEQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPFTGMDP 1372
Cdd:COG4604 91 TVRELVAFgrFPYSKGrLTAEDREI-IDEAIAYLDLEDLADRYLDELSGG-QRQRAFIAMVLAqDTDYVLLDEPLNNLDM 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1373 EGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:COG4604 169 KHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1224-1425 |
2.16e-08 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 58.17 E-value: 2.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1224 NVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHdnslkfLGYCPQENSLWPKLTMKE 1300
Cdd:PRK10851 20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGtdvSRLHARDRK------VGFVFQHYALFRHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HLELYAAVKGLGKEDAALSISRLVEALKLQEQL-----KAPVKtLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQ 1375
Cdd:PRK10851 94 NIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQLahladRYPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 296439455 1376 QQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQ 1425
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
391-566 |
2.20e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.27 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGKTgKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN 470
Cdd:PTZ00265 383 IQFKNVRFHYDTRK-DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 471 IGFCPQ------------------------------------------------------FNFQFDFLTVRENLRVFAKI 496
Cdd:PTZ00265 462 IGVVSQdpllfsnsiknnikyslyslkdlealsnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIEMRKNY 541
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 497 KGIQPKEVEQEVKRIIMELDMQSIQDII-------AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRV 566
Cdd:PTZ00265 542 QTIKDSEVVDVSKKVLIHDFVSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
387-581 |
2.39e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 58.71 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 387 GKEAIRIRNVIKEY-------NGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS 459
Cdd:PRK10261 310 GEPILQVRNLVTRFplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 EITD--MEEIRKNIgfcpQFNFQFDFL----------TVRENLRVFAKIKGiqpkevEQEVKRIIMELDMQSIQDIIA-- 525
Cdd:PRK10261 390 TLSPgkLQALRRDI----QFIFQDPYAsldprqtvgdSIMEPLRVHGLLPG------KAAAARVAWLLERVGLLPEHAwr 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 526 --KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILF 581
Cdd:PRK10261 460 ypHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAY 517
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1217-1430 |
2.99e-08 |
|
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: 55.61 E-value: 2.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGC--TKPTAGVVVLQGsrasvrqqhdnslkflgycpqENSLwp 1294
Cdd:cd03217 12 GKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKG---------------------EDIT-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1295 KLTMKEHlelyaAVKGLGkedaaLSISRLVE--ALKLQEQLKAPVKTLSEGiKRKLCFVLSILG-NPSVVLLDEPFTGMD 1371
Cdd:cd03217 68 DLPPEER-----ARLGIF-----LAFQYPPEipGVKNADFLRYVNEGFSGG-EKKRNEILQLLLlEPDLAILDEPDSGLD 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1372 PEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAV-CDRMAMMVSGTLRCIGS---IQHLKNK 1430
Cdd:cd03217 137 IDALRLVAEVIN-KLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDkelALEIEKK 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1225-1449 |
3.10e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQ---ENSLWPKLTMKEH 1301
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LELYAAVKGLG----------KEDAALSISRLVEALKLQEQlkaPVKTLSEGIKRKlcfvlSILG-----NPSVVLLDEP 1366
Cdd:PRK11288 352 INISARRHHLRagclinnrweAENADRFIRSLNIKTPSREQ---LIMNLSGGNQQK-----AILGrwlseDMKVILLDEP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1367 FTGMDPEGQQQMWQILQATVKNKeRGTLLTTHYMSEAEAVCDRMAMMVSGtlRCIGSIQHlkNKFGRDYLLEIKMKEPTQ 1446
Cdd:PRK11288 424 TRGIDVGAKHEIYNVIYELAAQG-VAVLFVSSDLPEVLGVADRIVVMREG--RIAGELAR--EQATERQALSLALPRTSA 498
|
...
gi 296439455 1447 VEA 1449
Cdd:PRK11288 499 AVA 501
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
392-558 |
3.20e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL--SVSTEGSaTIYNTQLSE---ITDMEE 466
Cdd:NF040905 3 EMRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGE-ILFDGEVCRfkdIRDSEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 -----IRKNIGFCPQfnfqfdfLTVRENLrvF-----AKIKGIQPKEVEQEVKRIIMELDMQS-----IQDI-------- 523
Cdd:NF040905 78 lgiviIHQELALIPY-------LSIAENI--FlgnerAKRGVIDWNETNRRARELLAKVGLDEspdtlVTDIgvgkqqlv 148
|
170 180 190
....*....|....*....|....*....|....*.
gi 296439455 524 -IAKKLSggQKRKLtlgiailgdpqvLLLDEPTAGL 558
Cdd:NF040905 149 eIAKALS--KDVKL------------LILDEPTAAL 170
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
407-558 |
3.40e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.09 E-value: 3.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 407 VEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL------SVSTEGSATIYN----TQLSEITDmeeIRKNIGFCPQ 476
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIytrdagSILYLGKEVTFNgpksSQEAGIGI---IHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 477 fnfqfdfLTVRENL---RVFAKIKG-IQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLD 552
Cdd:PRK10762 94 -------LTIAENIflgREFVNRFGrIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
....*.
gi 296439455 553 EPTAGL 558
Cdd:PRK10762 167 EPTDAL 172
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1225-1371 |
4.18e-08 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 56.00 E-value: 4.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTkPTAGVVVLQG---SRASVRQQHdnslKFLGYCPQENSLWPKLTMKEH 1301
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGrplSDWSAAELA----RHRAYLSQQQSPPFAMPVFQY 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1302 LELYAAVKGLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSIL-----GNPS--VVLLDEPFTGMD 1371
Cdd:COG4138 90 LALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
380-609 |
4.94e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 57.56 E-value: 4.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPEFHGKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKS-TLLNIL-----SGLSVSTEGSATI 453
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMrlleqAGGLVQCDKMLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 454 YNTQ----LSEITD--MEEIRkniGFCPQFNFQFDFLTVRENLRVFAKI-------KGIQPKEVEQEVKRIIMELDMQSI 520
Cdd:PRK10261 82 RRSRqvieLSEQSAaqMRHVR---GADMAMIFQEPMTSLNPVFTVGEQIaesirlhQGASREEAMVEAKRMLDQVRIPEA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 521 QDIIAK---KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLK--EHKVDRLILFSTQFMDEADILADR 595
Cdd:PRK10261 159 QTILSRyphQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIADR 238
|
250
....*....|....
gi 296439455 596 KVFLSNGKLKCAGS 609
Cdd:PRK10261 239 VLVMYQGEAVETGS 252
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1213-1433 |
5.35e-08 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 57.66 E-value: 5.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQhdnslkfLGYC 1286
Cdd:PRK13657 342 FSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGtdirtvTRASLRRN-------IAVV 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQENSLWPKlTMKEHLElyaavkgLGKEDAalSISRLVEALKLQEQL----KAPVK----------TLSEGIKRKLCFVL 1352
Cdd:PRK13657 415 FQDAGLFNR-SIEDNIR-------VGRPDA--TDEEMRAAAERAQAHdfieRKPDGydtvvgergrQLSGGERQRLAIAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1353 SILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNkeRGTLLTTHYMSE-AEAvcDRMAMMVSGTLRCIGSIQHLKNKF 1431
Cdd:PRK13657 485 ALLKDPPILILDEATSALDVETEAKVKAALDELMKG--RTTFIIAHRLSTvRNA--DRILVFDNGRVVESGSFDELVARG 560
|
..
gi 296439455 1432 GR 1433
Cdd:PRK13657 561 GR 562
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1213-1427 |
5.77e-08 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.42 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FS--TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRasVRQQHDNSL-KFLGYCPQE 1289
Cdd:TIGR00958 486 FSypNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVP--LVQYDHHYLhRQVALVGQE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLWPK---------LTMKEHLELYAAVKGLGKEDAalsISRLVEALKLQEQLKApvKTLSEGIKRKLCFVLSILGNPSV 1360
Cdd:TIGR00958 564 PVLFSGsvreniaygLTDTPDEEIMAAAKAANAHDF---IMEFPNGYDTEVGEKG--SQLSGGQKQRIAIARALVRKPRV 638
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 1361 VLLDEPFTGMDPEGQqqmwQILQATVKNKERGTLLTTHYMSEAEAvCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:TIGR00958 639 LILDEATSALDAECE----QLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQL 700
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
415-609 |
6.94e-08 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 55.32 E-value: 6.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSvSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFdfltvreNLRVFA 494
Cdd:PRK03695 17 AEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPF-------AMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 495 KIKGIQP-KEVEQEVKRIIMEL-DMQSIQDIIAK---KLSGGQKRKLTLGIAIL-----GDP--QVLLLDEPTAGLDpfs 562
Cdd:PRK03695 89 YLTLHQPdKTRTEAVASALNEVaEALGLDDKLGRsvnQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD--- 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 563 rhrvwsLLKEHKVDRLI-LFSTQ----FMDEADI-----LADRKVFLSNGKLKCAGS 609
Cdd:PRK03695 166 ------VAQQAALDRLLsELCQQgiavVMSSHDLnhtlrHADRVWLLKQGKLLASGR 216
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
391-558 |
7.02e-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: 57.14 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 391 IRIRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIY----NTQLSEITDMEe 466
Cdd:TIGR02633 2 LEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsgsPLKASNIRDTE- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 iRKNIGFCPQFNFQFDFLTVRENLRVFAKI--KG--IQPKEVEQEVKRIIMELDMQSIQD-IIAKKLSGGQKRKLTLGIA 541
Cdd:TIGR02633 77 -RAGIVIIHQELTLVPELSVAENIFLGNEItlPGgrMAYNAMYLRAKNLLRELQLDADNVtRPVGDYGGGQQQLVEIAKA 155
|
170
....*....|....*..
gi 296439455 542 ILGDPQVLLLDEPTAGL 558
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL 172
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1223-1418 |
7.06e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 56.98 E-value: 7.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSLKFLGYCPQENSLwpkltmk 1299
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGkeiNALSTAQRLARGLVYLPEDRQSSGL------- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1300 eHLE--LYAAVKGL-----------GKEDAALSISRLVEALKLqEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK15439 353 -YLDapLAWNVCALthnrrgfwikpARENAVLERYRRALNIKF-NHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1367 FTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK15439 431 TRGVDVSARNDIYQLIR-SIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
392-559 |
7.30e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 55.32 E-value: 7.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 392 RIRNVIKEYngktGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAtIYNT---QLSEITDMEE-- 466
Cdd:PRK11701 8 SVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV-HYRMrdgQLRDLYALSEae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 467 ----IRKNIGFCPQFNFQFDFLTVR------ENL-----RVFAKIKGIQPKEVEQevkriiMELDMQSIQDiIAKKLSGG 531
Cdd:PRK11701 83 rrrlLRTEWGFVHQHPRDGLRMQVSaggnigERLmavgaRHYGDIRATAGDWLER------VEIDAARIDD-LPTTFSGG 155
|
170 180
....*....|....*....|....*...
gi 296439455 532 QKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLD 183
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
404-571 |
7.33e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.02 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 404 TGKVEALQGIFFDIYEGQITAILGHNGAGKSTllnilSGLS----VSTEGSATIYNTQLSEIT--DMEEIRKNIGFCPQ- 476
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKST-----TGLAllrlINSQGEIWFDGQPLHNLNrrQLLPVRHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 477 ----FNFQFDFLT-VRENLRVFAKIkgIQPKEVEQEVKRIIME--LDMQSIQDIIAKkLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK15134 371 pnssLNPRLNVLQiIEEGLRVHQPT--LSAAQREQQVIAVMEEvgLDPETRHRYPAE-FSGGQRQRIAIARALILKPSLI 447
|
170 180
....*....|....*....|..
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLK 571
Cdd:PRK15134 448 ILDEPTSSLDKTVQAQILALLK 469
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
380-604 |
8.02e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 8.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPEFHGKEAIRIRNVIKEYnGKTGKveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLS 459
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAY-QDNGF--SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 460 EiTDMEEIRKNigfcpqfnfqfdFLTVRENLRVFAKIKGIQPKEVEQEVKRIIME-LDMQ---SIQD--IIAKKLSGGQK 533
Cdd:PRK10522 389 A-EQPEDYRKL------------FSAVFTDFHLFDQLLGPEGKPANPALVEKWLErLKMAhklELEDgrISNLKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 534 RKLTLGIAILGDPQVLLLDEPTAGLDP-FSRHRVWSLLKEHKVDRLILFSTQFMDEADILADRKVFLSNGKL 604
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPhFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1229-1417 |
9.16e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 9.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsrasvrqqhDNSLKfLGYCPQEnslwpkLTMKEHLELYAAV 1308
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV-------------DEDLK-ISYKPQY------ISPDYDGTVEEFL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1309 KGLGKEDAALSI--SRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATV 1386
Cdd:COG1245 423 RSANTDDFGSSYykTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
|
170 180 190
....*....|....*....|....*....|.
gi 296439455 1387 KNKERGTLLTTHYMSEAEAVCDRMaMMVSGT 1417
Cdd:COG1245 503 ENRGKTAMVVDHDIYLIDYISDRL-MVFEGE 532
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1219-1427 |
1.14e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.10 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV----VLQGSRASVrqQHDNSLKF---LGYCPQENS 1291
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdVLLGGRSIF--NYRDVLEFrrrVGMLFQRPN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKGLG-KEDAALSISRLVEA---LKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPrKEFRGVAQARLTEVglwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1368 TGMDPEGQQQMWQILQATVknkERGT-LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL 1427
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLA---DRLTvIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1215-1399 |
1.18e-07 |
|
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: 53.81 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVvvlqgsrasvrqqhDNSLKFLG---------- 1284
Cdd:cd03233 17 RSKIPI-LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSV--------------EGDIHYNGipykefaeky 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1285 -----YCPQENSLWPKLTMKEHLELYAAVKGlgkedaalsisrlvealklqeqlKAPVKTLSEGIKRKLCFVLSILGNPS 1359
Cdd:cd03233 82 pgeiiYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRAS 138
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 296439455 1360 VVLLDEPFTGMDPEGQQQMWQILQATVKnKERGTLLTTHY 1399
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMAD-VLKTTTFVSLY 177
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
390-559 |
1.24e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.91 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYngKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRK 469
Cdd:PLN03232 1234 SIKFEDVHLRY--RPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF-GLTDLRR 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDFlTVRENLRVFAK------IKGIQPKEVEQEVKRIIMELDMQSIQDiiAKKLSGGQKRKLTLGIAIL 543
Cdd:PLN03232 1311 VLSIIPQSPVLFSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEG--GENFSVGQRQLLSLARALL 1387
|
170
....*....|....*.
gi 296439455 544 GDPQVLLLDEPTAGLD 559
Cdd:PLN03232 1388 RRSKILVLDEATASVD 1403
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1222-1388 |
1.36e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 56.78 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGctKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKEH 1301
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LeLYAAV----KGLGKEDAALSISRLVEALKLqEQLK------APVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMD 1371
Cdd:PLN03140 974 L-IYSAFlrlpKEVSKEEKMMFVDEVMELVEL-DNLKdaivglPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
170
....*....|....*..
gi 296439455 1372 PEGQqqmwQILQATVKN 1388
Cdd:PLN03140 1052 ARAA----AIVMRTVRN 1064
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1223-1431 |
1.49e-07 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 55.42 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1223 RNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLkflGYCPQENSLWPKLTMKEHL 1302
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGV---GMVFQSYALYPHLSVAENM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1303 ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMwQIL 1382
Cdd:PRK11000 97 SFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRVQM-RIE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1383 QATVKNKERGTLL-TTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL----KNKF 1431
Cdd:PRK11000 176 ISRLHKRLGRTMIyVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRF 229
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1217-1366 |
1.53e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1217 KKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQ-GsrASVrqqhdnslkflGYCPQENSLWPK 1295
Cdd:PRK11819 19 KKQI-LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApG--IKV-----------GYLPQEPQLDPE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELyaavkGLGKEDAALS----ISRL-------VEAL-----KLQEQLKA------------------------ 1335
Cdd:PRK11819 85 KTVRENVEE-----GVAEVKAALDrfneIYAAyaepdadFDALaaeqgELQEIIDAadawdldsqleiamdalrcppwda 159
|
170 180 190
....*....|....*....|....*....|...
gi 296439455 1336 PVKTLSEGIKRK--LCFVLsiLGNPSVVLLDEP 1366
Cdd:PRK11819 160 KVTKLSGGERRRvaLCRLL--LEKPDMLLLDEP 190
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1213-1419 |
1.58e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 54.27 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1213 FSTRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTK-----PTAGVVVLQGSRASVRQQHDNSLKflgycP 1287
Cdd:PRK14258 15 FYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIYERRVNLNRLR-----R 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 QENSLWPK---LTMKEHLELYAAVKGLGKEdAALSISRLVE-ALK-------LQEQLKAPVKTLSEGIKRKLCFVLSILG 1356
Cdd:PRK14258 89 QVSMVHPKpnlFPMSVYDNVAYGVKIVGWR-PKLEIDDIVEsALKdadlwdeIKHKIHKSALDLSGGQQQRLCIARALAV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1357 NPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1222-1398 |
2.01e-07 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 55.89 E-value: 2.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKmITGC-TKPTAGVVVLQG---------SRASVRQQHdnslkfLGYCPQENS 1291
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGClDKPTSGTYRVAGqdvatldadALAQLRREH------FGFIFQRYH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMD 1371
Cdd:PRK10535 97 LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALD 176
|
170 180
....*....|....*....|....*....
gi 296439455 1372 PEGQQQMWQILQATvknKERG--TLLTTH 1398
Cdd:PRK10535 177 SHSGEEVMAILHQL---RDRGhtVIIVTH 202
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1224-1421 |
2.05e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 55.48 E-value: 2.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1224 NVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTkPTAGVVVLQG------------SRASVRQQHDNSLKFLGYCPQEnS 1291
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLL-PSPPVVYPSGdirfhgesllhaSEQTLRGVRGNKIAMIFQEPMV-S 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQE---QLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:PRK15134 105 LNPLHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIADEPT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1368 TGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGtlRCI 1421
Cdd:PRK15134 185 TALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG--RCV 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1210-1401 |
2.19e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 55.66 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1210 KSCFSTR--KKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGV-VVLQGSRASVRQqhdnSLKFLGYC 1286
Cdd:PLN03211 70 KISDETRqiQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTgTILANNRKPTKQ----ILKRTGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1287 PQENSLWPKLTMKEHL---ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPV-----KTLSEGIKRKLCFVLSILGNP 1358
Cdd:PLN03211 146 TQDDILYPHLTVRETLvfcSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIgnsfiRGISGGERKRVSIAHEMLINP 225
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 296439455 1359 SVVLLDEPFTGMDPEGQQQMWQILqATVKNKERGTLLTTHYMS 1401
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTL-GSLAQKGKTIVTSMHQPS 267
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1221-1417 |
2.49e-07 |
|
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: 52.86 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSrasvrqqhdnslkfLGYCPQ----------EN 1290
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQepwiqngtirEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 SLWPKlTMKEhlELYAAVkglgkedaalsisrlVEALKLQEQLKAPVK-----------TLSEGIKRKLCFVLSILGNPS 1359
Cdd:cd03250 86 ILFGK-PFDE--ERYEKV---------------IKACALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1360 VVLLDEPFTGMDPEGQQQMWQ--ILQATVKNKERgtLLTTHYMSEAEAvCDRMAMMVSGT 1417
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTR--ILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1214-1419 |
2.62e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 55.22 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1214 STRKKKIaiRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPT-AGVVVLQGSRASVRQQHDNSLKFLGYCPQE--- 1289
Cdd:TIGR02633 270 NPHRKRV--DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDrkr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLWPKLTMKEHLELYAAVK--GLGKEDAALSISRLVEALKlQEQLKA-----PVKTLSEGIKRKLCFVLSILGNPSVVL 1362
Cdd:TIGR02633 348 HGIVPILGVGKNITLSVLKSfcFKMRIDAAAELQIIGSAIQ-RLKVKTaspflPIGRLSGGNQQKAVLAKMLLTNPRVLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1363 LDEPFTGMDPEGQQQMWQILQATVKnkeRGT--LLTTHYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:TIGR02633 427 LDEPTRGVDVGAKYEIYKLINQLAQ---EGVaiIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
937-1130 |
2.75e-07 |
|
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: 54.32 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 937 IFLLLITNCVSpFIGMSSISDYKKNVQSQLWISGLWPSAYWCGQALVDIPLYFLILfsihLIYYFIFLGFQLSWELMFVL 1016
Cdd:pfam12698 167 ILMIIILIGAA-IIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQL----LIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1017 VVCIIGCAVSLIFLTYVLSFIFRKWRKNNGFwSFGFFIILICVSTIMVSTQYEKLNLILCMIFIPSFTlLGYVMLLIQLd 1096
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSI-IGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFS-PIDGLLRLIY- 318
|
170 180 190
....*....|....*....|....*....|....
gi 296439455 1097 fmrnldsldnriNEVNKTILLTTLIPYLQSVIFL 1130
Cdd:pfam12698 319 ------------GDSLWEIAPSLIILLLFAVVLL 340
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1218-1403 |
2.94e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.84 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASvRQQHDNSLKFLGYCPQENSLWPKLT 1297
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASKEVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 MKE--------HLELYAAVKglgKEDAAlSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTG 1369
Cdd:PRK10253 98 VQElvargrypHQPLFTRWR---KEDEE-AVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 296439455 1370 MDPEGQQQMWQILQATvkNKERGTLLTT--HYMSEA 1403
Cdd:PRK10253 174 LDISHQIDLLELLSEL--NREKGYTLAAvlHDLNQA 207
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1219-1278 |
3.26e-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: 54.94 E-value: 3.26e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLqGSR---ASVRQQHDN 1278
Cdd:TIGR03719 335 KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETvklAYVDQSRDA 396
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1221-1416 |
3.30e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 54.83 E-value: 3.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGcTKPTA---GVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLT 1297
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1298 MKEHLELYAAVKGLGKEDAALSISRLVEALKLQEQLKA-----PVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMdp 1372
Cdd:TIGR02633 95 VAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDAdnvtrPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 1373 egQQQMWQILQATVKN-KERGT--LLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:TIGR02633 173 --TEKETEILLDIIRDlKAHGVacVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
390-559 |
3.55e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 390 AIRIRNVIKEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMeEIRK 469
Cdd:PLN03130 1237 SIKFEDVVLRYRPELPPV--LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLM-DLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 470 NIGFCPQFNFQFDFlTVRENLRVFAKIK------GIQPKEVEQEVKRIIMELDMQSIQDiiAKKLSGGQKRKLTLGIAIL 543
Cdd:PLN03130 1314 VLGIIPQAPVLFSG-TVRFNLDPFNEHNdadlweSLERAHLKDVIRRNSLGLDAEVSEA--GENFSVGQRQLLSLARALL 1390
|
170
....*....|....*.
gi 296439455 544 GDPQVLLLDEPTAGLD 559
Cdd:PLN03130 1391 RRSKILVLDEATAAVD 1406
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1192-1267 |
3.65e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 53.82 E-value: 3.65e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1192 EEPVITASCLHKeYYETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG 1267
Cdd:PRK11308 2 QQPLLQAIDLKK-HYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQG 76
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1219-1437 |
3.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 53.13 E-value: 3.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGC-----TKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLW 1293
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1294 PKLTMKEHLELYAAVKGLGKEDaalSISRLVEAL--------KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1365
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKR---EIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1366 PFTGMDPEGQQQMWQILqaTVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHL----KNKFGRDYLL 1437
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLI--TELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
420-559 |
5.15e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 5.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSGLSVSTEGSATiyntqlSEIT----DMEEIRK----NIGFCPQFNFQFDFLTVRENLR 491
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE------GVITydgiTPEEIKKhyrgDVVYNAETDVHFPHLTVGETLD 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 492 VFAKIKGIQ--PKEVEQEVKR-----IIMELDMQSI-------QDIIaKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAG 557
Cdd:TIGR00956 161 FAARCKTPQnrPDGVSREEYAkhiadVYMATYGLSHtrntkvgNDFV-RGVSGGERKRVSIAEASLGGAKIQCWDNATRG 239
|
..
gi 296439455 558 LD 559
Cdd:TIGR00956 240 LD 241
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1194-1409 |
5.68e-07 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 52.50 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1194 PVITASCLHKEYYETKkscfstrkkkiAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVR 1273
Cdd:COG4598 7 PALEVRDLHKSFGDLE-----------VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1274 QQHDNSLKF------------LGYCPQENSLWPKLTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTL 1340
Cdd:COG4598 76 PDRDGELVPadrrqlqrirtrLGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1341 SEG------IKRKLCFvlsilgNPSVVLLDEPFTGMDPEGQQQMWQILQATVKnKERGTLLTTHYMSEAEAVCDR 1409
Cdd:COG4598 156 SGGqqqraaIARALAM------EPEVMLFDEPTSALDPELVGEVLKVMRDLAE-EGRTMLVVTHEMGFARDVSSH 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1220-1411 |
6.64e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 52.48 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1220 IAIRNVSFCVKKGEVLGLLGHNGAGKSTSIK-------MITGCTkpTAGVVVLQGSR--------ASVRQQhdnslkfLG 1284
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFR--VEGKVTFHGKNlyapdvdpVEVRRR-------IG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1285 YCPQENSLWPKlTMKEHLELYAAVKGL-GKEDAALSISRLVEAL--KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVV 1361
Cdd:PRK14243 95 MVFQKPNPFPK-SIYDNIAYGARINGYkGDMDELVERSLRQAALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1362 LLDEPFTGMDPEGQQQMWQILQATvknKERGTL-LTTHYMSEAEAVCDRMA 1411
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHEL---KEQYTIiIVTHNMQQAARVSDMTA 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1215-1416 |
6.74e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHD---NSLKFLGYCPQENS 1291
Cdd:PRK10982 257 TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainHGFALVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMkEHLELYAAVKGLGKEDAALSISRL-------VEALKLQE-QLKAPVKTLSEGIKRKLCFVLSILGNPSVVLL 1363
Cdd:PRK10982 337 IYAYLDI-GFNSLISNIRNYKNKVGLLDNSRMksdtqwvIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1364 DEPFTGMDPEGQQQMWQILQATVKnKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAK-KDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
410-567 |
7.45e-07 |
|
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: 52.55 E-value: 7.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntqlseitdmeEIRKN--IGFCPQFNFQFDFlTVR 487
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG----------------KIKHSgrISFSSQFSWIMPG-TIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENLrvfakIKGIQPKEVEQE--VKRIIMELDMQSIQD----IIAK---KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGL 558
Cdd:cd03291 116 ENI-----IFGVSYDEYRYKsvVKACQLEEDITKFPEkdntVLGEggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
....*....
gi 296439455 559 DPFSRHRVW 567
Cdd:cd03291 191 DVFTEKEIF 199
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1221-1416 |
9.57e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 9.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSLKFLGYCPQENSLWPKLTMKE 1300
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1301 HL----ELYAAVKGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEG------IKRKLCFvlsilgNPSVVLLDEPFTGM 1370
Cdd:PRK10762 99 NIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 296439455 1371 -DPEGQQQMWQILQatVKNKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK10762 173 tDTETESLFRVIRE--LKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1195-1278 |
1.25e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.20 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1195 VITASCLHKEYYEtkkscfstrkkKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLqGSR---AS 1271
Cdd:PRK11819 324 VIEAENLSKSFGD-----------RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETvklAY 391
|
....*..
gi 296439455 1272 VRQQHDN 1278
Cdd:PRK11819 392 VDQSRDA 398
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1221-1416 |
1.35e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.03 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKP---TAGVVVLQGSRA-SVRQQHDNSLK-------FlgycpQE 1289
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlNLPEKELNKLRaeqismiF-----QD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 --NSLWPKLTMKEHL-ELYAAVKGLGKEDAALSISRLVEALKLQEQLKA----PvKTLSEGIKRKLCFVLSILGNPSVVL 1362
Cdd:PRK09473 106 pmTSLNPYMRVGEQLmEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRmkmyP-HEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1363 LDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAG 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1230-1366 |
1.35e-06 |
|
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: 52.86 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1230 KKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV--------VLQGSRASVRQQH-----DNSLKfLGYCPQENSLWPKl 1296
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdeVLKRFRGTELQDYfkklaNGEIK-VAHKPQYVDLIPK- 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1297 tmkehlelyaAVKG-----LGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:COG1245 175 ----------VFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1218-1398 |
1.37e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1218 KKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGctKPTAGVVVlQGSRASVRQQHDNSL-KFLGYCPQENSLWPKL 1296
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVIT-GGDRLVNGRPLDSSFqRSIGYVQQQDLHLPTS 851
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLELYAAV---KGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGI----KRKLCFVLSILGNP-SVVLLDEPFT 1368
Cdd:TIGR00956 852 TVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPkLLLFLDEPTS 931
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 1369 GMDpegQQQMWQILQATVK--NKERGTLLTTH 1398
Cdd:TIGR00956 932 GLD---SQTAWSICKLMRKlaDHGQAILCTIH 960
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
415-612 |
1.47e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.71 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 415 FDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGS--------ATIYNTQLSEITDMEEIRKNIgfcpqfnfqfDFLTV 486
Cdd:PRK10938 24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQRNNT----------DMLSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 487 RENL--RVFAKIkgIQpKEVEQEVKriIMELDMQ-SIQDIIA---KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDP 560
Cdd:PRK10938 94 GEDDtgRTTAEI--IQ-DEVKDPAR--CEQLAQQfGITALLDrrfKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 561 FSR----HRVWSLLKEHKVDRLIL--FST--QFMDEADILADRKVFLSNGKLKCAGSSLF 612
Cdd:PRK10938 169 ASRqqlaELLASLHQSGITLVLVLnrFDEipDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-610 |
1.54e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 53.24 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSAtiyntqLSEitdmeeirKNIGFCPQFNFQFDfLTVREN 489
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV------WAE--------RSIAYVPQQAWIMN-ATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKgiqPKEVEQEVKRIIMELDMQSI----QDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFS 562
Cdd:PTZ00243 741 ILFFDEED---AARLADAVRVSQLEADLAQLggglETEIGEKgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHV 817
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 563 RHRVwsllkehkVDRLILFS----TQFMDEADI----LADRKVFLSNGKLKCAGSS 610
Cdd:PTZ00243 818 GERV--------VEECFLGAlagkTRVLATHQVhvvpRADYVVALGDGRVEFSGSS 865
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1229-1366 |
1.71e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 52.50 E-value: 1.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsrasvrqqhDNSLKfLGYCPQENSLWPKLTMKEHLElyaav 1308
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV-------------DPELK-ISYKPQYIKPDYDGTVEDLLR----- 422
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1309 KGLGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK13409 423 SITDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1216-1418 |
1.76e-06 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 52.34 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG---SRASVRQQHDNSlkfLGYCPQE--- 1289
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGediTGLSPRERRRLG---VAYIPEDrlg 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1290 NSLWPKLTMKEHLelyaAVKGLGKEDAA----LSISRLVE-ALKLQEQ-------LKAPVKTLSEGIKRKlcFVLS--IL 1355
Cdd:COG3845 345 RGLVPDMSVAENL----ILGRYRRPPFSrggfLDRKAIRAfAEELIEEfdvrtpgPDTPARSLSGGNQQK--VILAreLS 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1356 GNPSVVLLDEPFTGMDPEGQQQMWQILqatVKNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:COG3845 419 RDPKLLIAAQPTRGLDVGAIEFIHQRL---LELRDAGAavLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1221-1267 |
1.79e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 51.33 E-value: 1.79e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG 1267
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDD 74
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1215-1372 |
1.82e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 1.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR--ASVRQQHDNSLKFLGYCPQENSL 1292
Cdd:PRK11831 16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENipAMSRSRLYTVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLT--------MKEHLELYAAVkglgkedAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLD 1364
Cdd:PRK11831 96 FTDMNvfdnvaypLREHTQLPAPL-------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFD 168
|
....*...
gi 296439455 1365 EPFTGMDP 1372
Cdd:PRK11831 169 EPFVGQDP 176
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1229-1276 |
2.36e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.49 E-value: 2.36e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQH 1276
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY 69
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
410-559 |
2.52e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.61 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsatiyntqlseitdmeEIRKN--IGFCPQFNFQFDFlTVR 487
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG----------------KIKHSgrISFSPQTSWIMPG-TIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 488 ENL---------RVFAKIKGIQPKE----VEQEVKRIIMELDMqsiqdiiakKLSGGQKRKLTLGIAILGDPQVLLLDEP 554
Cdd:TIGR01271 505 DNIifglsydeyRYTSVIKACQLEEdialFPEKDKTVLGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSP 575
|
....*
gi 296439455 555 TAGLD 559
Cdd:TIGR01271 576 FTHLD 580
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
403-604 |
2.91e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.16 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 403 KTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL---SVSTEGSATIYNTQLSEITDmeeiRKNIGFCPQFNF 479
Cdd:PLN03140 174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKldpSLKVSGEITYNGYRLNEFVP----RKTSAYISQNDV 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 QFDFLTVRENLRVFAKIKG-------------------IQP-KEVEQEVKRIIME--------------LDMQSIQDIIA 525
Cdd:PLN03140 250 HVGVMTVKETLDFSARCQGvgtrydllselarrekdagIFPeAEVDLFMKATAMEgvksslitdytlkiLGLDICKDTIV 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 526 -----KKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLILFS-TQFMDEADILADRKV 597
Cdd:PLN03140 330 gdemiRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQivHLTEATVLMSlLQPAPETFDLFDDII 409
|
....*..
gi 296439455 598 FLSNGKL 604
Cdd:PLN03140 410 LLSEGQI 416
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1216-1419 |
3.65e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 3.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTK-PTAGVVVLQGSRASVRQQHDNSLKFLGYCPQE---NS 1291
Cdd:PRK13549 273 PHIKR-VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPEDrkrDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLEL--YAAVKGLGKEDAAL---SISRLVEALKLQ-EQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1365
Cdd:PRK13549 352 IVPVMGVGKNITLaaLDRFTGGSRIDDAAelkTILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1366 PFTGMDPEGQQQMWQILQATVKnkeRGT--LLTTHYMSEAEAVCDRMAMMVSGTLR 1419
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLINQLVQ---QGVaiIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
393-603 |
3.73e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.27 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 393 IRNVIKEYNGktgkVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKNIG 472
Cdd:PRK10982 1 MSNISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 473 FCPQFNFQFDFLTVRENL---RVFAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVL 549
Cdd:PRK10982 77 MVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 550 LLDEPTAGLDPFSRHRVWSLLKEHKvDR--LILFSTQFMDEADILADRKVFLSNGK 603
Cdd:PRK10982 157 IMDEPTSSLTEKEVNHLFTIIRKLK-ERgcGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
919-1090 |
4.77e-06 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 49.19 E-value: 4.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 919 TSFSRDDIVLDLGFIDGSIFLLLITNCVSPFIGMSSISDYKKNVQSQLWISGL-WPSAYWCGQALVDIPLYFLILFSIHL 997
Cdd:pfam01061 32 TLFGNLGNQQGGLNRPGLLFFSILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 998 IYYFIFlGFQLSWELMFvlvvciigcavsLIFLTYVLSFIFrkwrknngFWSFGFFIILICVSTIMVSTqyeklnlILCM 1077
Cdd:pfam01061 112 IVYFMV-GLPPSAGRFF------------LFLLVLLLTALA--------ASSLGLFISALAPSFEDASQ-------LGPL 163
|
170
....*....|...
gi 296439455 1078 IFIPSFTLLGYVM 1090
Cdd:pfam01061 164 VLLPLLLLSGFFI 176
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
398-602 |
4.98e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 49.19 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 398 KEYNGKTGKVeaLQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIyntqlseitdmeEIRKNigfcpqf 477
Cdd:COG2401 36 VELRVVERYV--LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV------------DVPDN------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 478 nfQFDfltvrenlRVFAKIKGIQPKEVEQEVKRIimeLDMQSIQDIIA-----KKLSGGQKRKLTLGIAILGDPQVLLLD 552
Cdd:COG2401 95 --QFG--------REASLIDAIGRKGDFKDAVEL---LNAVGLSDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 553 EPTAGLDP-FSR---HRVWSLLKEHKVdRLILFSTQFMDEADILADRKVFLSNG 602
Cdd:COG2401 162 EFCSHLDRqTAKrvaRNLQKLARRAGI-TLVVATHHYDVIDDLQPDLLIFVGYG 214
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1222-1430 |
5.20e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsRASVRqqhdnslkfLGYCPQENSLWPKlTMKEH 1301
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----KHSGR---------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LelyaaVKGLGKEDaaLSISRLVEALKLQEQL-KAPVK----------TLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:TIGR01271 507 I-----IFGLSYDE--YRYTSVIKACQLEEDIaLFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 296439455 1371 DPEGQQQMWQ-ILQATVKNKERgtLLTTHYMSEAEAVcDRMAMMVSGTLRCIGSIQHLKNK 1430
Cdd:TIGR01271 580 DVVTEKEIFEsCLCKLMSNKTR--ILVTSKLEHLKKA-DKILLLHEGVCYFYGTFSELQAK 637
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1229-1366 |
5.52e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.96 E-value: 5.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV--------VLQGSRASVRQQH-----DNSLKfLGYCPQENSLWPK 1295
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRFRGTELQNYfkklyNGEIK-VVHKPQYVDLIPK 174
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1296 ltmkehlelyaAVKG-----LGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK13409 175 -----------VFKGkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
410-573 |
8.66e-06 |
|
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: 47.53 E-value: 8.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGsaTIyntqlseitDMEEiRKNIGFCPQFNFqFDFLTVREN 489
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG--RI---------GMPE-GEDLLFLPQRPY-LPLGTLREQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LrvfakikgIQPKEveqevkriimeldmqsiqdiiaKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSL 569
Cdd:cd03223 84 L--------IYPWD----------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQL 133
|
....
gi 296439455 570 LKEH 573
Cdd:cd03223 134 LKEL 137
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
380-559 |
8.94e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 8.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPEFhGKEAIRIRNVIKEYNGKTgkveALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNT-QL 458
Cdd:PRK11819 315 PPGPRL-GDKVIEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGETvKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 459 S-----------------EITDMEEIRKnIG--------FCPQFNFqfdfltvrenlrvfakiKGiqpkeveqevkriim 513
Cdd:PRK11819 390 AyvdqsrdaldpnktvweEISGGLDIIK-VGnreipsraYVGRFNF-----------------KG--------------- 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 514 eldmqSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:PRK11819 437 -----GDQQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1229-1371 |
9.11e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 9.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1229 VKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV--------VLQGSRASVRQQH-----DNSLKFLgYCPQENSLWPK 1295
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEFRGSELQNYftkllEGDVKVI-VKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 ltmkehlelyaAVKG-----LGKEDAALSISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:cd03236 102 -----------AVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
.
gi 296439455 1371 D 1371
Cdd:cd03236 171 D 171
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1216-1418 |
1.14e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.05 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1216 RKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG-CTKPTA-------GVVVLQGS-------------RASVRQ 1274
Cdd:PRK13547 11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEplaaidaprlarlRAVLPQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1275 QHDNSLKF-------LGYCPQENslwpKLTMKEHLELYAAVKGLGKEDAALSISRlvealklqeqlkaPVKTLSEGIKRK 1347
Cdd:PRK13547 91 AAQPAFAFsareivlLGRYPHAR----RAGALTHRDGEIAWQALALAGATALVGR-------------DVTTLSGGELAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1348 LCF--VLSIL-------GNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTL 1418
Cdd:PRK13547 154 VQFarVLAQLwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAI 233
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1239-1373 |
1.24e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.56 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1239 GHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQhdnslKFLGYCPQENSLWPKLTMKEHLELYAAVKglgkeDAAL 1318
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK-----PYCTYIGHNLGLKLEMTVFENLKFWSEIY-----NSAE 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1319 SISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPE 1373
Cdd:PRK13541 103 TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1222-1422 |
1.24e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 48.68 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRQQHDNSL------KFLGYCPQENSLWPK 1295
Cdd:PRK14267 20 IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEEARVEGEVRLFGRNIYSPDVdpievrREVGMVFQYPNPFPH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1296 LTMKEHLELYAAVKGLGKEDAALSiSRLVEALK-------LQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFT 1368
Cdd:PRK14267 100 LTIYDNVAIGVKLNGLVKSKKELD-ERVEWALKkaalwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 296439455 1369 GMDPEGQQQMWQILQATvkNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIG 1422
Cdd:PRK14267 179 NIDPVGTAKIEELLFEL--KKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1222-1371 |
1.25e-05 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 48.70 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVvlqgsRASVRqqhdnslkfLGYCPQENSLWPKlTMKEH 1301
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----KHSGR---------ISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1302 LelyaaVKGLGKEDaaLSISRLVEALKLQEQL-KAPVK----------TLSEGIKRKLCFVLSILGNPSVVLLDEPFTGM 1370
Cdd:cd03291 118 I-----IFGVSYDE--YRYKSVVKACQLEEDItKFPEKdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
.
gi 296439455 1371 D 1371
Cdd:cd03291 191 D 191
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1232-1382 |
1.66e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1232 GEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVL-QGSRASVRQQHdnSLKFLGycPQENSLwpkltmkEHLelyaavkg 1310
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYFAQH--QLEFLR--ADESPL-------QHL-------- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1311 lgkedaalsiSRLVEAlKLQEQLK--------------APVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQ 1376
Cdd:PRK10636 399 ----------ARLAPQ-ELEQKLRdylggfgfqgdkvtEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQ 467
|
....*.
gi 296439455 1377 QMWQIL 1382
Cdd:PRK10636 468 ALTEAL 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
380-605 |
1.81e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 380 PVSPEFHGKEAIRIRNvIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGL-------SVSTEGS-A 451
Cdd:PRK13549 249 PREPHTIGEVILEVRN-LTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAypgrwegEIFIDGKpV 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 452 TIYNTQLS---EITDMEEIRKNIGFCPQfnfqfdfLTVREN-----LRVFAKIKGI-QPKE---VEQEVKRiiMELDMQS 519
Cdd:PRK13549 328 KIRNPQQAiaqGIAMVPEDRKRDGIVPV-------MGVGKNitlaaLDRFTGGSRIdDAAElktILESIQR--LKVKTAS 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 520 IQDIIAKkLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEhKVDR---LILFSTQfMDEADILADRK 596
Cdd:PRK13549 399 PELAIAR-LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQ-LVQQgvaIIVISSE-LPEVLGLSDRV 475
|
....*....
gi 296439455 597 VFLSNGKLK 605
Cdd:PRK13549 476 LVMHEGKLK 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1221-1254 |
1.84e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.16 E-value: 1.84e-05
10 20 30
....*....|....*....|....*....|....
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG 1254
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG 53
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
397-559 |
2.23e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.86 E-value: 2.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 397 IKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLS--VSTEGSATIYNTQLSEITDMEEIRKNIGFC 474
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGIFMA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 475 PQF-------NFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRIIMELDMQsiQDIIAKKL----SGGQ-KRKLTLGIAI 542
Cdd:PRK09580 84 FQYpveipgvSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMP--EDLLTRSVnvgfSGGEkKRNDILQMAV 161
|
170
....*....|....*..
gi 296439455 543 LgDPQVLLLDEPTAGLD 559
Cdd:PRK09580 162 L-EPELCILDESDSGLD 177
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1192-1263 |
2.31e-05 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 47.61 E-value: 2.31e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 296439455 1192 EEPVITASCLHKeYYETKKSCfstrkkkiaiRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV 1263
Cdd:PRK11701 3 DQPLLSVRGLTK-LYGPRKGC----------RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1234-1424 |
3.29e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.95 E-value: 3.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1234 VLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLqGSRASVRQQHDNSL----KFLGYCPQENSLWPKLTMKEHLeLYaavk 1309
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVL-NGRVLFDAEKGICLppekRRIGYVFQDARLFPHYKVRGNL-RY---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1310 GLGKEDAALsISRLVEALKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNK 1389
Cdd:PRK11144 100 GMAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178
|
170 180 190
....*....|....*....|....*....|....*
gi 296439455 1390 ERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSI 1424
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
377-580 |
3.32e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.87 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 377 SFEPVSPEFHGKEAIRIRN----VIKEYNGKTGKVEALQGIF---------------FDIYEGQITAILGHNGAGKSTLL 437
Cdd:PTZ00265 1132 SFEKYYPLIIRKSNIDVRDnggiRIKNKNDIKGKIEIMDVNFryisrpnvpiykdltFSCDSKKTTAIVGETGSGKSTVM 1211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 438 NIL-----------------------------------------SGLSVSTEGS----ATIYNTQLSEITD--------M 464
Cdd:PTZ00265 1212 SLLmrfydlkndhhivfknehtndmtneqdyqgdeeqnvgmknvNEFSLTKEGGsgedSTVFKNSGKILLDgvdicdynL 1291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKNIGFCPQFNFQFdfltvreNLRVFAKIKGIQPKEVEQEVKRI---------IMELDMQSIQDI--IAKKLSGGQK 533
Cdd:PTZ00265 1292 KDLRNLFSIVSQEPMLF-------NMSIYENIKFGKEDATREDVKRAckfaaidefIESLPNKYDTNVgpYGKSLSGGQK 1364
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 296439455 534 RKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKE--HKVDRLIL 580
Cdd:PTZ00265 1365 QRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDikDKADKTII 1413
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1225-1365 |
3.59e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 3.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1225 VSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG------SRASVRQQHdnSLKFLGYcpqenslwpkltm 1298
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGqpvtadNREAYRQLF--SAVFSDF------------- 415
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 296439455 1299 keHL--ELYaavkGLGKEDAALSISRLVEALKLQEQLKapVKT-------LSEGIKRKLCFVLSILGNPSVVLLDE 1365
Cdd:COG4615 416 --HLfdRLL----GLDGEADPARARELLERLELDHKVS--VEDgrfsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1212-1419 |
4.19e-05 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 48.04 E-value: 4.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1212 CFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRASVRqqhdnslkflgycpqens 1291
Cdd:PRK10522 329 TFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE------------------ 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 lwpklTMKEHLELYAAV--------KGLGKE----DAALSISRLvEALKLQEQLK------APVKtLSEGIKRKLCFVLS 1353
Cdd:PRK10522 391 -----QPEDYRKLFSAVftdfhlfdQLLGPEgkpaNPALVEKWL-ERLKMAHKLEledgriSNLK-LSKGQKKRLALLLA 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1354 ILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTH---YMSEAeavcDRMAMMVSGTLR 1419
Cdd:PRK10522 464 LAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQLS 528
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
527-603 |
4.42e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 48.16 E-value: 4.42e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 527 KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHK--VDRLILFSTQFMDEADILADRKVFLSNGK 603
Cdd:PRK15134 156 QLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqeLNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
|
| RloC |
COG4694 |
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis]; |
420-536 |
4.85e-05 |
|
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
Pssm-ID: 443729 [Multi-domain] Cd Length: 692 Bit Score: 48.19 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSglSVSTEGSATIYNTQLSEITDMEEIRKNIgfcpqFNFQFDFltVRENLRVFAKIKGI 499
Cdd:COG4694 24 KKLNLIYGENGSGKSTLSRILR--SLELGDTSSEVIAEFEIEAGGSAPNPSV-----RVFNRDF--VEENLRSGEEIKGI 94
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 296439455 500 -----QPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKL 536
Cdd:COG4694 95 ftlgeENIELEEEIEELEKEIEDLKKELDKLEKELKEAKKAL 136
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
410-566 |
8.13e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 46.36 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSG--------LSVSTEGSATIYNTQLSEI--TDMEEIRKNIGFCPQFNF 479
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgggapRGARVTGDVTLNGEPLAAIdaPRLARLRAVLPQAAQPAF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 480 QFdflTVRENLRV----FAKIKGIQPKEVEQEVKRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAI---------LGDP 546
Cdd:PRK13547 97 AF---SAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180
....*....|....*....|
gi 296439455 547 QVLLLDEPTAGLDPFSRHRV 566
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRL 193
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
312-584 |
8.25e-05 |
|
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: 46.61 E-value: 8.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 312 TFFILAFDTLFYLIFTLYFERVLPDKDGHGDSPLFFL-------KSSFWSKHQNTHHEIFENEINPEHSSDDSFEPVSPE 384
Cdd:pfam13304 13 SNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLLngidpkePIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 385 FHGKEAIRIRNVIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDM 464
Cdd:pfam13304 93 LLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 465 EEIRKnigfcpqFNFQFDFLTVRENLRVFAKIKGIQPKEVEQEVKRI--------IMELDMQSIQDIIAKKLSGGQKRKL 536
Cdd:pfam13304 173 ADLAL-------FPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVddrlrergLILLENGGGGELPAFELSDGTKRLL 245
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 296439455 537 TLGIAILGDPQ---VLLLDEPTAGLDPFSRHRVWSLLKEHKVDRL-ILFSTQ 584
Cdd:pfam13304 246 ALLAALLSALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
396-590 |
9.08e-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: 45.40 E-value: 9.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 396 VIKEYNGKTGKVEALQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITDMEEIRKN---IG 472
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNrysVA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 473 FCPQFNFQFDfLTVRENLRVFAKIKgiqpkevEQEVKRIIMELDMQSIQDII-----------AKKLSGGQKRKLTLGIA 541
Cdd:cd03290 83 YAAQKPWLLN-ATVEENITFGSPFN-------KQRYKAVTDACSLQPDIDLLpfgdqteigerGINLSGGQRQRICVARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 296439455 542 ILGDPQVLLLDEPTAGLD-PFSRHR----VWSLLKEHKvdRLILFST---QFMDEAD 590
Cdd:cd03290 155 LYQNTNIVFLDDPFSALDiHLSDHLmqegILKFLQDDK--RTLVLVThklQYLPHAD 209
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1221-1430 |
9.42e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 46.44 E-value: 9.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKP----TAGVVVLQG---SRASVRQQ-----HDNSLKFlgycpQ 1288
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGidlLKLSPRERrkiigREIAMIF-----Q 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1289 E--NSLWPKLTMKEHLE---LYAAVKGLGKEDAALSISRLVEAL------KLQEQLKAPVKTLSEGIKRKLCFVLSILGN 1357
Cdd:COG4170 97 EpsSCLDPSAKIGDQLIeaiPSWTFKGKWWQRFKWRKKRAIELLhrvgikDHKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1358 PSVVLLDEPFTGMDPEGQQQMWQILQATvkNKERGT--LLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKNK 1430
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARL--NQLQGTsiLLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
410-559 |
1.06e-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: 47.25 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEItDMEEIRKNIGFCPQFNFQFDFlTVREN 489
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKI-GLHDLRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 490 LRVFAKIKgiqpkevEQEVkriIMELDMQSIQDIIA--------------KKLSGGQKRKLTLGIAILGDPQVLLLDEPT 555
Cdd:TIGR00957 1380 LDPFSQYS-------DEEV---WWALELAHLKTFVSalpdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEAT 1449
|
....
gi 296439455 556 AGLD 559
Cdd:TIGR00957 1450 AAVD 1453
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
422-570 |
1.23e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.86 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 422 ITAILGHNGAGKSTLLNILSGLSVSTEGSATIYNTQLSEITD--MEEIRKNIGFCPQfnfqfdfLTVRENLRVFAKIKgi 499
Cdd:PRK13541 28 ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKpyCTYIGHNLGLKLE-------MTVFENLKFWSEIY-- 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 296439455 500 qpkeveQEVKRIIMELDMQSIQDIIAKK---LSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLL 570
Cdd:PRK13541 99 ------NSAETLYAAIHYFKLHDLLDEKcysLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
525-573 |
2.49e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 45.57 E-value: 2.49e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 296439455 525 AKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEH 573
Cdd:COG4178 483 DQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREE 531
|
|
| MdoB |
COG1368 |
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope ... |
987-1134 |
2.53e-04 |
|
Phosphoglycerol transferase MdoB/OpgB, AlkP superfamily [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440979 [Multi-domain] Cd Length: 576 Bit Score: 45.41 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 987 LYFLILFSIHLIYYFIFLGFQLSWELMFVLVVCIIGCAVSLIFLTYVLSFIFRKWRKNNGFWSFGFFIILICVSTIMVST 1066
Cdd:COG1368 3 LLFLLLLSLRLVFLLFNFDLSLGEILQAFLYGLRFILYLLLLLLLLLLLLLPLLFRRPKLRWIYLLLVLLLLLLLLVADI 82
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1067 QYeklnlilcmifipsFTLLGYVMLLIQLDFMRNLDSLDNRINEVNKTILLTTLIPYLQSVIFLFVIR 1134
Cdd:COG1368 83 LY--------------YRFFGDRLNFSDLDYLGDTGEVLGSLLSSYDLLLLLDLLLLLLLLLLLYRLL 136
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1219-1435 |
3.88e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 3.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTS----IKMItgctkPTAGVVVLQGS---------------RASVRQQHDNS 1279
Cdd:PRK15134 299 NVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLI-----NSQGEIWFDGQplhnlnrrqllpvrhRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1280 lkflgycpqenSLWPKLTMKEHLElyaavKGLGKEDAALSIS----RLVEAlkLQEQLKAPV------KTLSEGIKRKLC 1349
Cdd:PRK15134 374 -----------SLNPRLNVLQIIE-----EGLRVHQPTLSAAqreqQVIAV--MEEVGLDPEtrhrypAEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1350 FVLSILGNPSVVLLDEPFTGMDPEGQQQMWQILQATVKNKERGTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGSIQHLKN 1429
Cdd:PRK15134 436 IARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
....*.
gi 296439455 1430 KFGRDY 1435
Cdd:PRK15134 516 APQQEY 521
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1219-1418 |
4.79e-04 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 44.84 E-value: 4.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTkPTAGVVVLQG------SRASVRQQhdnsLKFLGycpqENSL 1292
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGielrelDPESWRKH----LSWVG----QNPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1293 WPKLTMKEHLElyaavkgLGKEDA-------ALSISRLVEALKLQEQ-LKAPVK----TLSEGIKRKLCFVLSILGNPSV 1360
Cdd:PRK11174 434 LPHGTLRDNVL-------LGNPDAsdeqlqqALENAWVSEFLPLLPQgLDTPIGdqaaGLSVGQAQRLALARALLQPCQL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 296439455 1361 VLLDEPFTGMDPEGQQQMWQILQATVKNKErgTLLTTHYMSEAEAvCDRMAMMVSGTL 1418
Cdd:PRK11174 507 LLLDEPTASLDAHSEQLVMQALNAASRRQT--TLMVTHQLEDLAQ-WDQIWVMQDGQI 561
|
|
| NosY |
COG1277 |
ABC-type transport system involved in multi-copper enzyme maturation, permease component ... |
177-272 |
4.86e-04 |
|
ABC-type transport system involved in multi-copper enzyme maturation, permease component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440888 [Multi-domain] Cd Length: 201 Bit Score: 42.88 E-value: 4.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 177 WLSWGLTYICFIFIMSIFMALVITSIPIVFHTGFMVIFTLY---SLYGLSLIALAFLMSVLIRKPMLAGLAGF-LFTVFW 252
Cdd:COG1277 100 FLGALLVLLLALLITFLLALLLGLLLFGSPPPDLGAILGFYlglLLLGLAFLAIGLFISALTRNQIVAAILAIaLWLLLV 179
|
90 100
....*....|....*....|
gi 296439455 253 GCLGFTVlyrqLPLSLGWVL 272
Cdd:COG1277 180 ILLAWIV----LFLALAYLR 195
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1221-1254 |
5.47e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 5.47e-04
10 20 30
....*....|....*....|....*....|....
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG 1254
Cdd:NF040905 16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
420-602 |
6.57e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.98 E-value: 6.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 420 GQITAILGHNGAGKSTLLNILSGLSVSTEGSAtiyntqlsEITDMEEIRknigfcpqfnfqfdfltvrenlrvfakikgi 499
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGV--------IYIDGEDIL------------------------------- 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 500 qpkeveqevkRIIMELDMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLL-------KE 572
Cdd:smart00382 43 ----------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrllllLK 112
|
170 180 190
....*....|....*....|....*....|....*
gi 296439455 573 HKVDRLILFSTQFMDEAD-----ILADRKVFLSNG 602
Cdd:smart00382 113 SEKNLTVILTTNDEKDLGpallrRRFDRRIVLLLI 147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1215-1431 |
7.48e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1215 TRKKKIaIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCT----KPTAGVVVLQGsrasvRQQHDNSLKFLG---YCP 1287
Cdd:TIGR00956 71 TKTFDI-LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTdgfhIGVEGVITYDG-----ITPEEIKKHYRGdvvYNA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1288 QENSLWPKLTMKEHLELYAA-------VKGLGKEDAALSISRLVEA---LKLQEQLKAP---VKTLSEGIKRKLCFVLSI 1354
Cdd:TIGR00956 145 ETDVHFPHLTVGETLDFAARcktpqnrPDGVSREEYAKHIADVYMAtygLSHTRNTKVGndfVRGVSGGERKRVSIAEAS 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1355 LGNPSVVLLDEPFTGMDPEGQQQMWQILQaTVKNKERGTLLTTHYMSEAEA--VCDRMAMMVSGTLRCIGSIQHLKNKF 1431
Cdd:TIGR00956 225 LGGAKIQCWDNATRGLDSATALEFIRALK-TSANILDTTPLVAIYQCSQDAyeLFDKVIVLYEGYQIYFGPADKAKQYF 302
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
527-559 |
8.99e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.62 E-value: 8.99e-04
10 20 30
....*....|....*....|....*....|...
gi 296439455 527 KLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLD 559
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPTRGID 436
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
523-594 |
1.21e-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: 41.19 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 523 IIAKKLSGGQKRKLT----LGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRLILFST----QFMDEADILAD 594
Cdd:cd03227 73 FTRLQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVIthlpELAELADKLIH 152
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1191-1269 |
1.46e-03 |
|
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: 43.13 E-value: 1.46e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 1191 EEEPVITASCLHKEYYETKKSCFSTRKKKIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTkPTAGVVVLQGSR 1269
Cdd:COG4172 271 DAPPLLEARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQD 348
|
|
| MFS_1 |
pfam07690 |
Major Facilitator Superfamily; |
136-288 |
1.48e-03 |
|
Major Facilitator Superfamily;
Pssm-ID: 429598 [Multi-domain] Cd Length: 344 Bit Score: 42.79 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 136 FHFTCLVSFSSFIYFASLNVARERGKFKKLM---TVMGLRESAFWLSWGLTYICFIFIMSIFMALVITSIPI---VFHTG 209
Cdd:pfam07690 154 FLILAILSLLAAVLLLLPRPPPESKRPKPAEearLSLIVAWKALLRDPVLWLLLALLLFGFAFFGLLTYLPLyqeVLGLS 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 210 FMVIFTLYSLYGLSLIALAFLMSVLIRK----PMLAGLAGFLFTVFWGCLGFTvlyrqLPLSLGWVLSLLSPFAFTAGMA 285
Cdd:pfam07690 234 ALLAGLLLGLGGLLGAIGRLLLGRLSDRlgrrRRLLLALLLLILAALGLLLLS-----LTLSSLWLLLALLLLGFGFGLV 308
|
...
gi 296439455 286 QIT 288
Cdd:pfam07690 309 FPA 311
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
403-442 |
1.73e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 41.61 E-value: 1.73e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 296439455 403 KTGK-VEALQGIFfdiyEGQITAILGHNGAGKSTLLNILSG 442
Cdd:cd01854 71 KTGEgLDELRELL----KGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1221-1416 |
1.76e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.79 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSR---ASVRQQHDN-------SLKFLGYCPQEN 1290
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEidfKSSKEALENgismvhqELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1291 SLW----PKLTM-KEHLELYAAVKGLGKEdaalsisrlveaLKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDE 1365
Cdd:PRK10982 93 NMWlgryPTKGMfVDQDKMYRDTKAIFDE------------LDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 296439455 1366 PFTGMDPEGQQQMWQILQatvKNKERG--TLLTTHYMSEAEAVCDRMAMMVSG 1416
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIR---KLKERGcgIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1209-1267 |
1.95e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 42.39 E-value: 1.95e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1209 KKSCFSTRKKKI-AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQG 1267
Cdd:PRK15079 23 GKQWFWQPPKTLkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLG 82
|
|
| UhpC |
COG2271 |
Sugar phosphate permease [Carbohydrate transport and metabolism]; |
156-330 |
2.07e-03 |
|
Sugar phosphate permease [Carbohydrate transport and metabolism];
Pssm-ID: 441872 [Multi-domain] Cd Length: 363 Bit Score: 42.16 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 156 ARERGkfkklmTVMGLRESAFWLSWGLTYICFIFIMSIF---MALVITSIPIVF-------HTGFMVIFTLYSLYGLSLI 225
Cdd:COG2271 129 PKERG------RALGIFNAGGPLGGALAPPLLGWLLAAFgwrAAFLILGLPGLLlallrfwLLALAYFLVYFALYGFLTW 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 226 ALAFLMSVLIRKPMLAGLAGFLFTVFW--GCLGFTVLYRQLPLSLGWVLsLLSPFAFTAGMAQITHLDNYLSGVIFPdps 303
Cdd:COG2271 203 LPTYLVEVRGLSLAQAGLLLSLPFLAGivGSLLGGWLSDRLGRRRKLVL-AIGLLLAALALLLLALLPSPALAIALL--- 278
|
170 180
....*....|....*....|....*..
gi 296439455 304 gdsykMIATFFILAFDTLFYLIFTLYF 330
Cdd:COG2271 279 -----FLAGFGLGGAFGLLWALAAELF 300
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1174-1396 |
3.11e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 42.24 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1174 VQAERVQ--AANALTAPNLEEEPVITASCLHKEYYETKKSCFSTRKK-KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIK 1250
Cdd:TIGR00957 1251 VAVERLKeySETEKEAPWQIQETAPPSGWPPRGRVEFRNYCLRYREDlDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTL 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1251 MITGCTKPTAGVVVLQGSRASVRQQHDnsLKF-LGYCPQENSLWPKlTMKEHLELYAAvkgLGKEDA--ALSISRL---V 1324
Cdd:TIGR00957 1331 GLFRINESAEGEIIIDGLNIAKIGLHD--LRFkITIIPQDPVLFSG-SLRMNLDPFSQ---YSDEEVwwALELAHLktfV 1404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 296439455 1325 EAL--KLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEPFTGMDPEGQqqmwQILQATVKNK-ERGTLLT 1396
Cdd:TIGR00957 1405 SALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD----NLIQSTIRTQfEDCTVLT 1475
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1221-1423 |
3.28e-03 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 41.75 E-value: 3.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1221 AIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVVVLQGSRAsvrqqhdNSLK---------FLGYcpqenS 1291
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-------NELEpadrdiamvFQNY-----A 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1292 LWPKLTMKEHLElYA-AVKGLGKEDaalsISRLVEA----LKLQEQLKAPVKTLSEGIKRKLCFVLSILGNPSVVLLDEP 1366
Cdd:PRK11650 87 LYPHMSVRENMA-YGlKIRGMPKAE----IEERVAEaariLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEP 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1367 FTGMDPEGQQQM---WQILQATVKNKergTLLTTHYMSEAEAVCDRMAMMVSGTLRCIGS 1423
Cdd:PRK11650 162 LSNLDAKLRVQMrleIQRLHRRLKTT---SLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
516-604 |
3.50e-03 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 40.84 E-value: 3.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 516 DMQSIQDIIAKKLSGGQKRKLTLGIAILGDPQVLLLDEPTAGLDPFSRHRVWSLLKEHKVDRL--ILFSTQFMDEADILA 593
Cdd:PRK10418 129 NAARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARLA 208
|
90
....*....|.
gi 296439455 594 DRKVFLSNGKL 604
Cdd:PRK10418 209 DDVAVMSHGRI 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1219-1263 |
4.89e-03 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 4.89e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 296439455 1219 KIAIRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITGCTKPTAGVV 1263
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
419-447 |
5.92e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 39.45 E-value: 5.92e-03
10 20 30
....*....|....*....|....*....|
gi 296439455 419 EGQITAILGHNGAGKSTLLN-ILSGLSVST 447
Cdd:pfam03193 105 KGKTTVLAGQSGVGKSTLLNaLLPELDLRT 134
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
410-560 |
6.43e-03 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 41.30 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 410 LQGIFFDIYEGQITAILGHNGAGKSTLLNILSGLsVSTEGSATIYNTQLSEITDMEEIRKNIGFCPQFNFQFDFlTVREN 489
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRM-VEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQN 1403
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 296439455 490 LRVFAKikgIQPKEVEQEVKRIIMELDMQSIQD-IIAKKLSG------GQKRKLTLGIAILG-DPQVLLLDEPTAGLDP 560
Cdd:PTZ00243 1404 VDPFLE---ASSAEVWAALELVGLRERVASESEgIDSRVLEGgsnysvGQRQLMCMARALLKkGSGFILMDEATANIDP 1479
|
|
| 7tm_TAS2R |
cd13950 |
mammalian taste receptors type 2, member of the seven-transmembrane G protein-coupled receptor ... |
896-1093 |
6.72e-03 |
|
mammalian taste receptors type 2, member of the seven-transmembrane G protein-coupled receptor superfamily; This group represents a family of mammalian taste receptors (TAS2Rs), which function as bitter taste receptors. The human TAS2R family contains about 25 functional members, which are glycoproteins and have the ability to form both homomeric and heteromeric receptor complexes. Five basic tastes are perceived by animals: bitter, sweet, sour, salty, and umami (the taste of glutamate, MSG). Among these, sour and salty are mediated by ion channels, while the perception of umami and sweet tastes is mediated by the TAS1R taste receptors, which belong to the class C GPCR family. The TAS2Rs in humans have a short extracellular N-terminus and the ligand binds within the transmembrane domain, whereas the TAS1Rs have a large N-terminal extracellular domain composed of the Venus flytrap module that forms the orthosteric (primary) ligand binding site. Signal transduction of bitter taste involves binding of bitter compounds to TAS2Rs linked to the alpha-subunit of gustducin, a heterotrimeric G protein expressed in taste receptor cells. This G-alpha subunit stimulates phosphodiesterase and decreases cAMP and cGMP levels. Further steps in the signaling cascade is still unknown. The beta-gamma-subunit of gustducin also mediates bitter taste transduction by activating phospholipase C, which leads to an increased formation of IP3 (inositol triphosphate) and DAG (diacylglycerol), thereby causing release of Ca2+ from intracellular stores and enhanced neurotransmitter release.
Pssm-ID: 320088 Cd Length: 288 Bit Score: 40.24 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 896 LMGIVSNALMGIFNFTELIQMESTSFSrDDIVLDLGFidgSIFLLLIT----NCVSPFIGMSSISDYKKNVQSQLWISGL 971
Cdd:cd13950 11 LIGILGNGFIVLVNCIDWIKSRKLSSI-DFILTSLAI---SRIGLLWTiilnSILSVFYPDIYLSGNVLRTLDILWMFLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 972 WPSAyWCGQAL-VdipLYFLIL--FSIHLiyyFIFLGFQLSWELMFVLVVCIIGCAVSLIFLTYVLSFIFRKWRKNNGFW 1048
Cdd:cd13950 87 HSSL-WFATCLsV---FYCLKIanFSHPF---FLWLKWRINRVVPWLLLGSLLISLLISLPIVWVIYSVYQNNSKEESNN 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 296439455 1049 SFGFFiilicvstiMVSTQYEKLNLILCMIFIPSFTL-LGYVMLLI 1093
Cdd:cd13950 160 TSKFQ---------VKKTSYFYSFILLNLGSLIPFILsLISFFLLI 196
|
|
| MFS_FucP_MFSD4_like |
cd17333 |
Bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein ... |
183-330 |
9.46e-03 |
|
Bacterial fucose permease, eukaryotic Major facilitator superfamily domain-containing protein 4, and similar proteins; This family is composed of bacterial L-fucose permease (FucP), eukaryotic Major facilitator superfamily domain-containing protein 4 (MFSD4) proteins, and similar proteins. L-fucose permease facilitates the uptake of L-fucose across the boundary membrane with the concomitant transport of protons into the cell; it can also transport L-galactose and D-arabinose. The MFSD4 subfamily consists of two vertebrate members: MFSD4A and MFSD4B. The function of MFSD4A is unknown. MFSD4B is more commonly know as Sodium-dependent glucose transporter 1 (NaGLT1), a primary fructose transporter in rat renal brush-border membranes that also facilitates sodium-independent urea uptake. The FucP/MFSD4 family belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.
Pssm-ID: 340891 [Multi-domain] Cd Length: 372 Bit Score: 40.00 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 183 TYICFI--FIMSIFMALVITSIPIVFHTGF----MVIFTLYSLYGLSLIALAFLMSVLIRKPMLA------GLAGFLFTV 250
Cdd:cd17333 1 LYISFFsnGLTDALLGILGPSLEEAFNLNVadvsVIFSSQNAGYLIGSLLAGFLMKRLGRRRTLIlgllliSLALALIFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 251 FWGCLGFTVLYRQLPLSLGWVLSLLSPFAFTAG------MAQITHLDNYLSGVIFPdpsgdsykMIATFFI---LAFDTL 321
Cdd:cd17333 81 TPSIYLFVVLMFLAGLGAGILDTGANTFVGALFeessatRLNVLHGFFGLGALIGP--------LIATSLLtseLSWSWA 152
|
....*....
gi 296439455 322 FYLIFTLYF 330
Cdd:cd17333 153 YLIIGLIYL 161
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1222-1399 |
9.72e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 39.63 E-value: 9.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1222 IRNVSFCVKKGEVLGLLGHNGAGKSTSIKMITG--CTKPTAGVVVLQGSRASVRQQHDNSLK--FLGY-CPQEnslWPKL 1296
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLgiFLAFqYPIE---IPGV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 296439455 1297 TMKEHLEL-YAAVK---GLGKEDAALSISRLVEALKL----QEQLKAPV-KTLSEGIKRKLCFVLSILGNPSVVLLDEPF 1367
Cdd:CHL00131 100 SNADFLRLaYNSKRkfqGLPELDPLEFLEIINEKLKLvgmdPSFLSRNVnEGFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190
....*....|....*....|....*....|..
gi 296439455 1368 TGMDPEGQQQMWQILQaTVKNKERGTLLTTHY 1399
Cdd:CHL00131 180 SGLDIDALKIIAEGIN-KLMTSENSIILITHY 210
|
|
| |
