|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
107-1618 |
4.00e-139 |
|
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: 477.97 E-value: 4.00e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 107 EEYASEKELLASSLS--KPSNF-VGVVFKDV----------MSYELRFFPDMV----PVSSVYMDSRAGCSKSCDAAQYW 169
Cdd:TIGR01257 526 ESYDDEVQLTQRALSllEENRFwAGVVFPDMypwtsslpphVKYKIRMDIDVVektnKIKDRYWDSGPRADPVEDFRYIW 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 170 SsGFTALQASIDAAI----IQLKTNVSLWRELESTKAVIMGEAAVVEIDTFPrgvilIYLVIAFSPFGYFLAIHIVAEKE 245
Cdd:TIGR01257 606 G-GFAYLQDMVEQGItrsqMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFP-----IFMVLAWIYSVSMTVKSIVLEKE 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 246 KRLKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATASSLFPQSSSIVIFLLFFLYGLSSVFFALMLTPLFKKSK 325
Cdd:TIGR01257 680 LRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKAS 759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 326 HVGVVEFFVTVVFGFVGLLIVL----VESFPRSLVWLFSPLcqcAFLIGIAQVMHLEDFNEGALFSSLTEGP-----YPL 396
Cdd:TIGR01257 760 LAAACSGVIYFTLYLPHILCFAwqdrMTADLKTAVSLLSPV---AFGFGTEYLVRFEEQGLGLQWSNIGNSPlegdeFSF 836
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 397 IITLTMLALDSVFYALLAVYLDQVIPGEFGLRRSSLYFLKPSYW------SKNKRNYKELSEgNINGNISLNEIVEPVSS 470
Cdd:TIGR01257 837 LLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggegcSTREERALEKTE-PLTEEMEDPEHPEGIND 915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 471 EFIGKE------AIRISGIQKAYRKKNETVEALRNLSFdiYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhr 544
Cdd:TIGR01257 916 SFFERElpglvpGVCVKNLVKIFEPSGRPAVDRLNITF--YENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG-- 991
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 545 vSEIDEMFEA-RKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKL 623
Cdd:TIGR01257 992 -KDIETNLDAvRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSK 703
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 704 WGIGYRLSMY------------IDRYCATES--------------------------LSSLVRQHIPAAALLQQNDQQIV 745
Cdd:TIGR01257 1151 FGTGFYLTLVrkmkniqsqrggCEGTCSCTSkgfstrcparvdeitpeqvldgdvneLMDLVYHHVPEAKLVECIGQELI 1230
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 746 YSLPFKDMDK--FSGLFSALD-IHSNLGVISYGVSMTTLEDVFLKLEVEAEIDQAdYSVFTQQPREE-------ETDSKS 815
Cdd:TIGR01257 1231 FLLPNKNFKQraYASLFRELEeTLADLGLSSFGISDTPLEEIFLKVTEDADSGSL-FAGGAQQKRENanlrhpcSGPTEK 1309
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 816 FDEMEQSLLILS----------------ETKASLVST---MSLWKQQVSTIAKFHFLSLKRESKSVRSVLLLLLIFFAVQ 876
Cdd:TIGR01257 1310 AGQTPQASHTCSpgqpaahpegqpppepEDPGVPLNTgarLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALM 1389
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 877 I-----------------FMFLVHHSFKNAVVP----IKLVPDLYFLKPGDKPHKYKTSLLLQ----NS----TDSDIND 927
Cdd:TIGR01257 1390 LsiiippfgeypaltlhpWMYGQQYTFFSMDEPnsehLEVLADVLLNKPGFGNRCLKEEWLPEypcgNStpwkTPSVSPN 1469
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 928 LIDFFTQQNIIVAMFNDSDYVSA---------APHSA-----------ALNVVQSEKDY--------VFTAVFNSTMVYS 979
Cdd:TIGR01257 1470 ITHLFQKQKWTAAHPSPSCRCSTrekltmlpeCPEGAgglpppqrtqrSTEILQDLTDRnisdflvkTYPALIRSSLKSK 1549
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 980 ----------------LPV-----------------MMNIISN-----------YYLYHLNVTDTIQIW----------- 1004
Cdd:TIGR01257 1550 fwvneqryggisiggkLPAipitgealvgflsdlgqMMNVSGGpvtreaskempDFLKHLETEDNIKVWfnnkgwhalvs 1629
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1005 ----------------------------STPF------IQEITDIVFKVElyfqaALLGIIV----TAMPPYFAMENAEN 1046
Cdd:TIGR01257 1630 flnvahnailraslpkdrdpeeygitviSQPLnltkeqLSEITVLTTSVD-----AVVAICVifamSFVPASFVLYLIQE 1704
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1047 HKIKAYTQLKLSGLLPSAYWIGQAVVDIPLFFVVLTLMLGSLFAFHHGLYFYPVKFLAVVFCLIAYVPSVILFTYIASFT 1126
Cdd:TIGR01257 1705 RVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFL 1784
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1127 FKkilntkefwsfiysVTALACVAVTEITFFLGYGVTAVfhyTFC---------------------IAIPIYPLLGCLIS 1185
Cdd:TIGR01257 1785 FD--------------VPSTAYVALSCANLFIGINSSAI---TFVlelfennrtllrfnamlrkllIVFPHFCLGRGLID 1847
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1186 F-----IKGSWKNIPKtENAYNP--WDRL---LVAVIMPYLQCVLWIFLLQHYEKkhggrsirkdpLFRALSQKAKhkkf 1255
Cdd:TIGR01257 1848 LalsqaVTDVYAQFGE-EHSANPfqWDLIgknLVAMAVEGVVYFLLTLLIQHHFF-----------LSRWIAEPAK---- 1911
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1256 pEPPIneDEDEDVKAERLKVkeLMGcqcceekpaimvynlhkeyDDKKDFLHSRKTTKV-------ATKYVSFCVKKGEI 1328
Cdd:TIGR01257 1912 -EPIF--DEDDDVAEERQRI--ISG-------------------GNKTDILRLNELTKVysgtsspAVDRLCVGVRPGEC 1967
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1329 LGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEStKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGD 1408
Cdd:TIGR01257 1968 FGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEE 2046
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1409 MKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKnKKRAALL 1488
Cdd:TIGR01257 2047 IEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR-EGRAVVL 2125
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1489 TTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKLKDWIENL--EIDRLQREIQYIFPNASRQESFSSI 1566
Cdd:TIGR01257 2126 TSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKDDLlpDLNPVEQFFQGNFPGSVQRERHYNM 2205
|
1770 1780 1790 1800 1810
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1567 LAYKIPKedvQSLSQSFAKLEEAKHTFAIEEYSFSQATLEQVFVELTKEQEE 1618
Cdd:TIGR01257 2206 LQFQVSS---SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTE 2254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
478-701 |
3.04e-84 |
|
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: 275.15 E-value: 3.04e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03263 1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSIFLK 701
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1290-1521 |
7.80e-83 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 270.92 E-value: 7.80e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYddkkdflhsRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:cd03263 1 LQIRNLTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DEStKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03263 72 AAR-QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLK 1521
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1294-1524 |
2.61e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 229.95 E-value: 2.61e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSNEDDEST 1373
Cdd:COG1131 5 GLTKRYGDK-----------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGE-DVARDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQV 1453
Cdd:COG1131 73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1454 TLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:COG1131 153 LILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
478-696 |
4.75e-68 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 229.18 E-value: 4.75e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLlSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1290-1526 |
2.75e-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: 195.85 E-value: 2.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:COG4555 2 IEVENLSKKYGKVP-----------ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKcMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:COG4555 71 EARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGK 1526
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
478-691 |
4.86e-56 |
|
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: 192.23 E-value: 4.86e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVseIDEMFEARKM 557
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLsilasvkgipanniiqevqkvlldldmqaikdnqakKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGML 691
Cdd:cd03230 119 LDEPTSGLDPESRREFWELLRELKKEGKTILlSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1290-1521 |
3.09e-55 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 191.81 E-value: 3.09e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSNED 1369
Cdd:cd03265 1 IEVENLVKKYGDF-----------EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH-DVVREP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLK 1521
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1314-1613 |
1.98e-54 |
|
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: 192.60 E-value: 1.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSnEDDESTKCMGYCPQTNPLWPDITLQE 1393
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-EPRKVRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWR 1473
Cdd:TIGR01188 86 NLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1474 AIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGyFLEIKLKDWIE-NLEIDRLQREIQY 1552
Cdd:TIGR01188 166 YIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD-TLESRPRDIQSlKVEVSMLIAELGE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1553 IFPNASRQESFSSILAYKIPKEDVQsLSQSFAKLEEAKHTfaIEEYSFSQATLEQVFVELT 1613
Cdd:TIGR01188 244 TGLGLLAVTVDSDRIKILVPDGDET-VPEIVEAAIRNGIR--IRSISTERPSLDDVFLKLT 301
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
478-696 |
1.42e-50 |
|
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: 179.28 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRaLKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
478-695 |
8.22e-50 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 175.84 E-value: 8.22e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGqITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03264 74 IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03264 154 VDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1294-1511 |
4.57e-49 |
|
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: 172.20 E-value: 4.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSNEDDEST 1373
Cdd:cd03230 5 NLSKRYGKKT-----------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV--LGKDIKKEPEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 K-CMGYCPQTNPLWPDITLQEHFeiygavkgmssgdmkevisritkaldlkehlqktvkKLPAGIKRKLCFALSMLGNPQ 1452
Cdd:cd03230 72 KrRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
489-701 |
1.90e-48 |
|
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: 172.55 E-value: 1.90e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKMIGICPQSDMNF 568
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03265 86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 649 SRHIVWNLL-KYRKANRVTVF-STHFMDEADILADRKAVISQGMLKCVGSSIFLK 701
Cdd:cd03265 166 TRAHVWEYIeKLKEEFGMTILlTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1292-1618 |
5.44e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.98 E-value: 5.44e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGSHSNEDDe 1371
Cdd:COG4152 4 LKGLTKRFGDKT-----------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD--GEPLDPED- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1372 sTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:COG4152 70 -RRRIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1452 QVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFlE 1531
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIR-ELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL-R 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1532 IKLK---DWIENLeidrlqreiqyifPNASRQESFSSILAYKIPKE-DVQSLsqsfakLEEAKHTFAIEEYSFSQATLEQ 1607
Cdd:COG4152 227 LEADgdaGWLRAL-------------PGVTVVEEDGDGAELKLEDGaDAQEL------LRALLARGPVREFEEVRPSLNE 287
|
330
....*....|.
gi 27368659 1608 VFVELTKEQEE 1618
Cdd:COG4152 288 IFIEVVGEKAE 298
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1289-1588 |
1.44e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 167.96 E-value: 1.44e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDK----------KDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIf 1358
Cdd:COG4586 1 IIEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1359 lgdygshsneddestKCMGYCP----------------QTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDL 1422
Cdd:COG4586 80 ---------------RVLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1423 KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAfkNKKRAA--LLTTHYMEEAEAVC 1500
Cdd:COG4586 145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEALC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1501 DRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKLKDWIENLEIDRLQREIQYIFPNA----SRQESFSSILAYKIPKEDV 1576
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGEVIEREGNRVrlevDPRESLAEVLARLLARYPV 302
|
330
....*....|..
gi 27368659 1577 QSLSQSFAKLEE 1588
Cdd:COG4586 303 RDLTIEEPPIEE 314
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
478-695 |
2.81e-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: 160.23 E-value: 2.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRqLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1312-1515 |
8.32e-43 |
|
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: 155.90 E-value: 8.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1312 TKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshSNEDDESTKCMGYCPQTNPLWPDITL 1391
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG----KPLDIAARNRIGYLPEERGLYPKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 1472 WRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03269 168 KDVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
487-689 |
8.36e-43 |
|
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: 155.70 E-value: 8.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-SD 565
Cdd:cd03225 7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGLVFQnPD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 MNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03225 86 DQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27368659 646 DPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03225 166 DPAGRRELLELLKKLKAEGKTiIIVTHDLDLLLELADRVIVLEDG 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
478-696 |
1.16e-42 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 155.95 E-value: 1.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKM 557
Cdd:COG1122 1 IELENLSFSY---PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQS--DMNFDvLTVEE-------NLsilasvkGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GI 627
Cdd:COG1122 77 VGLVFQNpdDQLFA-PTVEEdvafgpeNL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIaGV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 628 AVLgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1122 149 LAM-EPEVLVLDEPTAGLDPRGRRELLELLKrLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
478-687 |
1.80e-42 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 155.32 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfEARKM 557
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVIS 687
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLdiWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1290-1512 |
3.24e-41 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 151.19 E-value: 3.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGeILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSNED 1369
Cdd:cd03264 1 LQLENLTKRYGKKR-----------ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQ-DVLKQP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03264 68 QKLRRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1450 NPQVTLLDEPSTGMDPRAkqhmwraiRTAFKN------KKRAALLTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:cd03264 148 DPSILIVDEPTAGLDPEE--------RIRFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
478-691 |
4.81e-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: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKM 557
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIiqevQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQGML 691
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLiSSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
478-689 |
6.12e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 150.72 E-value: 6.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--- 554
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQSdmnF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:cd03255 81 RRHIGFVFQS---FnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 632 NPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1290-1515 |
2.34e-40 |
|
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: 149.06 E-value: 2.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:cd03266 2 ITADALTKRFRDVK-------KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKcMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03266 75 EARRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1290-1511 |
6.08e-40 |
|
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: 148.63 E-value: 6.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYD----------DKKDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1360 GDYGSHSNEDDESTK---CMGycpQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAG 1436
Cdd:cd03267 81 AGLVPWKRRKKFLRRigvVFG---QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1437 IKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03267 158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
478-688 |
1.02e-39 |
|
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: 146.86 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRkkNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARkm 557
Cdd:COG4133 3 LEAENLSCRRG--ERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIiqEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHfmDEADILADRKAVISQ 688
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAaHLARGGAVLLTTH--QPLELAAARVLDLGD 204
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
475-691 |
1.51e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 144.03 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 475 KEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA 554
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 ---RKMIGICPQSdmnF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG1136 82 rlrRRHIGFVFQF---FnllPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADIlADRKAVISQGML 691
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
479-689 |
4.54e-38 |
|
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: 140.07 E-value: 4.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMI 558
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-LEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd00267 76 GYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTViIVTHDPELAELAADRVIVLKDG 156
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1288-1510 |
5.38e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 145.33 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1288 PAIMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSN 1367
Cdd:PRK13537 6 APIDFRNVEKRYGDK-----------LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKcMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSM 1447
Cdd:PRK13537 75 ARHARQR-VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1448 LGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKrAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1081-1626 |
1.42e-37 |
|
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: 155.56 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1081 LTLMLGSLFAFHHGLYFYPVKFLAVVFcLIAYVPSVILFTYIASFTFKKilntkefwsfiySVTALACVAVTEITFFLGY 1160
Cdd:TIGR01257 710 MSIFLLTIFIMHGRILHYSDPFILFLF-LLAFSTATIMQCFLLSTFFSK------------ASLAAACSGVIYFTLYLPH 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1161 --------GVTAVFHYTFCIAIPIYPLLGC--LISF----IKGSWKNIPKTENAYNPWDRLLVAVIMP-----------Y 1215
Cdd:TIGR01257 777 ilcfawqdRMTADLKTAVSLLSPVAFGFGTeyLVRFeeqgLGLQWSNIGNSPLEGDEFSFLLSMKMMLldaalygllawY 856
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1216 LQCVL---------WIFLLQH-YEKKHGGRSIRKDplfRALSQKAKHKKFPEPPINEDEDEDVKAERlkvkELMGCQcce 1285
Cdd:TIGR01257 857 LDQVFpgdygtplpWYFLLQEsYWLGGEGCSTREE---RALEKTEPLTEEMEDPEHPEGINDSFFER----ELPGLV--- 926
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1286 ekPAIMVYNLHKEYDdkkdflhsrKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSH 1365
Cdd:TIGR01257 927 --PGVCVKNLVKIFE---------PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1366 SNEDdESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFAL 1445
Cdd:TIGR01257 996 TNLD-AVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAI 1074
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1446 SMLGNPQVTLLDEPSTGMDPRAKQHMWRAIrtaFKNKK-RAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:TIGR01257 1075 AFVGDAKVVVLDEPTSGVDPYSRRSIWDLL---LKYRSgRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCF 1151
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1525 GKGYFLEIKLKdwIENLEIDRLQRE-------------------------------------IQYIFPNASRQESFSSIL 1567
Cdd:TIGR01257 1152 GTGFYLTLVRK--MKNIQSQRGGCEgtcsctskgfstrcparvdeitpeqvldgdvnelmdlVYHHVPEAKLVECIGQEL 1229
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1568 AYKIPKEDVQ--SLSQSFAKLEEAKHTFAIEEYSFSQATLEQVFVELTkeqeeEDNSCGTL 1626
Cdd:TIGR01257 1230 IFLLPNKNFKqrAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVT-----EDADSGSL 1285
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1289-1509 |
1.72e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 144.97 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDygSHSN 1367
Cdd:PRK13536 41 AIDLAGVSKSYGDK-----------AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLGV--PVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSM 1447
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1448 LGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKrAALLTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
477-689 |
3.02e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 3.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 637 LLDEPTAGMDPCSRHIVWN-LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG1116 161 LMDEPFGALDALTRERLQDeLLRLWQETGKTVlFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
478-689 |
3.34e-37 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 140.71 E-value: 3.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:cd03261 1 IELRGLTKSFGGR--TV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKK---LSGGQKRKLSLGIAVLGN 632
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIRE--IVLEKLEAVGLRGAEDLYpaeLSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLiRSLKKELGLTSIMvTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-643 |
1.02e-36 |
|
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: 136.24 E-value: 1.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEaRKMIGICPQSDMNFDVLTVEEN 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 577 LSILASVKGIPANNIIQEVQKVLLDLDMQAIKD----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
5.89e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.35 E-value: 5.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARK 556
Cdd:PRK13536 41 AIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDmNFDV-LTVEENLSILASVKGIPANNIiQEVQKVLLDL-DMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK13536 115 RIGVVPQFD-NLDLeFTVRENLLVFGRYFGMSTREI-EAVIPSLLEFaRLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTIlLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1290-1512 |
2.06e-35 |
|
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: 134.65 E-value: 2.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSNED 1369
Cdd:cd03268 1 LKTNDLTKTYGKKR-----------VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF--DGKSYQKN 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRItkalDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03268 68 IEALRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDEVLDVV----GLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELIL-SLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
497-691 |
7.91e-35 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 133.02 E-value: 7.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEARKMIGICPQ-SDMNFDvlTV 573
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--EIYldGKPLSAMP-PPEWRRQVAYVPQePALWGG--TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSILASVKGIPANniIQEVQKVL--LDLDmQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:COG4619 91 RDNLPFPFQLRERKFD--RERALELLerLGLP-PDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 652 IVWNLLK-YRKANRVTVFS-THFMDEADILADRKAVISQGML 691
Cdd:COG4619 168 RVEELLReYLAEEGRAVLWvSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
478-689 |
9.15e-35 |
|
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: 132.64 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfEARKM 557
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 638 LDEPTAGMDPCSR-HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03259 154 LDEPLSALDAKLReELREELKELQRELGITtIYVTHDQEEALALADRIAVMNEG 207
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-689 |
1.08e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 135.24 E-value: 1.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARK 556
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQ-----SDMnfdvlTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:COG4152 72 RIGYLPEerglyPKM-----KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 632 NPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTViFSSHQMELVEELCDRIVIINKG 205
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
478-689 |
1.52e-34 |
|
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: 132.02 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 638 LDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
2.49e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.55 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARK 556
Cdd:PRK13537 7 PIDFRNVEKRYGDK--LV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDmNFDV-LTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13537 81 RVGVVPQFD-NLDPdFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILlTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
478-689 |
2.55e-34 |
|
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: 129.81 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDvLTVEENLsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03228 78 IAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-691 |
7.86e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 130.92 E-value: 7.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 475 KEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFea 554
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGIC--PQSDMNFDvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03267 93 LRRIGVVfgQKTQLWWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:cd03267 172 PEILFLDEPTIGLDVVAQENIRNFLKeYNRERGTTVlLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
478-689 |
1.14e-33 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 130.36 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFE-ARK 556
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKrARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEG 209
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
478-696 |
4.19e-33 |
|
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: 128.96 E-value: 4.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03295 1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
477-689 |
4.98e-33 |
|
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: 128.56 E-value: 4.98e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG1127 5 MIEVRNLTKSFGDR----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQSDMNFDVLTVEENLSI-LASVKGIPANNIIqevQKVLLDLDMQAIKDNQAKK---LSGGQKRKLSLGIAVL 630
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFpLREHTDLSEAEIR---ELVLEKLELVGLPGAADKMpseLSGGMRKRVALARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 631 GNPKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:COG1127 158 LDPEILLYDEPTAGLDPITSAVIDELiRELRDELGLTSVVvTHDLDSAFAIADRVAVLADG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1294-1510 |
1.59e-32 |
|
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: 124.28 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKDFLHsrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEST 1373
Cdd:cd00267 4 NLSFRYGGRTALDN-----------VSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQtnplwpditlqehfeiygavkgmssgdmkevisritkaldlkehlqktvkkLPAGIKRKLCFALSMLGNPQV 1453
Cdd:cd00267 73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1454 TLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLR-ELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
478-689 |
1.76e-32 |
|
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: 126.85 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEAR 555
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMN-FD-VLTVE----ENLSILASVKGIPANNIIQEVQKVLLDLDmQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:cd03257 82 KEIQMVFQDPMSsLNpRMTIGeqiaEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKkLQEELGLTLlFITHDLGVVAKIADRVAVMYAG 222
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
477-696 |
1.78e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.18 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARK 556
Cdd:PRK13632 7 MIKVENVSFSYP--NSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13632 84 KIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 636 LLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFS-THFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13632 164 IIFDESTSMLDPKGKReIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
478-689 |
4.15e-32 |
|
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: 125.62 E-value: 4.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-----EIdemf 552
Cdd:cd03224 1 LEVENLNAGYGK----SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphER---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 eARKMIGICPQSDMNFDVLTVEENLsILASVKGIPANN--IIQEVqkvlLDL--DMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:cd03224 73 -ARAGIGYVPEGRRIFPELTVEENL-LLGAYARRRAKRkaRLERV----YELfpRLKERRKQLAGTLSGGEQQMLAIARA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:cd03224 147 LMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILlVEQNARFALEIADRAYVLERG 208
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1319-1491 |
4.33e-32 |
|
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: 124.90 E-value: 4.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEStKCMGYCPQTNPLWPDITLQEHFEIY 1398
Cdd:COG4133 21 LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYR-RRLAYLGHADGLKPELTVRENLRFW 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMSSGDmkEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRtA 1478
Cdd:COG4133 100 AALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIA-A 176
|
170
....*....|...
gi 27368659 1479 FKNKKRAALLTTH 1491
Cdd:COG4133 177 HLARGGAVLLTTH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
478-689 |
4.64e-32 |
|
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: 125.77 E-value: 4.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQsdmNFDVL---TVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALL--RDINRelgLTiVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1319-1510 |
5.86e-32 |
|
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: 124.50 E-value: 5.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQtNPlwpD-----ITLQE 1393
Cdd:cd03225 20 ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQ-NP---DdqffgPTVEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 hfEI-YGAVK-GMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:cd03225 96 --EVaFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRREL 173
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1472 WRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03225 174 LELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1294-1515 |
5.92e-32 |
|
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: 124.55 E-value: 5.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSNEDDEST 1373
Cdd:cd03259 5 GLSKTYGSV-----------RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR-DVTGVPPERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KcMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQV 1453
Cdd:cd03259 73 N-IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1454 TLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03259 152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
478-691 |
1.19e-31 |
|
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: 124.22 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-----PSDGFASIYGHRVSEIDEMF 552
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 EA-RKMIGICPQSDMNFDvLTVEENLSILASVKGIPANNIIQE-VQKVLLDLDM-QAIKDNQ-AKKLSGGQKRKLSLGIA 628
Cdd:cd03260 77 LElRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1319-1518 |
2.55e-31 |
|
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: 123.60 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgshsNEDDESTKCM----GYCPQtNPlwpDI----- 1389
Cdd:COG1122 20 VSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK----DITKKNLRELrrkvGLVFQ-NP---DDqlfap 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1390 TLQEhfEI-YGAV-KGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFA--LSMlgNPQVTLLDEPSTGMDP 1465
Cdd:COG1122 92 TVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAgvLAM--EPEVLVLDEPTAGLDP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1466 RAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG1122 168 RGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
9.22e-31 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.51 E-value: 9.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQ-SDMNFDV-LTVEE----NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:COG1121 76 RIGYVPQrAEVDWDFpITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 631 GNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTIlVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-699 |
9.37e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 123.59 E-value: 9.37e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 475 KEAIRISGIQkaYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEA 554
Cdd:PRK13635 3 EEIIRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLgN 632
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIaGVLAL-Q 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKAN-RVTVFS-THFMDEAdILADRKAVISQGMLKCVG--SSIF 699
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGtpEEIF 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-689 |
1.85e-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: 128.10 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVSEIDEmFE 553
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 554 ARKMIGICPQSDMN-FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:COG1123 81 RGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTtvLLITHDLGVVAEIADRVVVMDDG 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1319-1461 |
3.21e-30 |
|
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: 117.36 E-value: 3.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEIY 1398
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1399 GAVKGMSSGDMKEVISRITKALDL----KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
474-689 |
3.56e-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: 3.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAYR-KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID- 549
Cdd:COG1123 257 AEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG--SILfdGKDLTKLSr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 550 -EMFEARKMIGICPQ--SDMNFDVLTVEENLS-ILASVKGIPANNIIQEVQKVL----LDLDMqaikdnqAKK----LSG 617
Cdd:COG1123 335 rSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAePLRLHGLLSRAERRERVAELLervgLPPDL-------ADRypheLSG 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 618 GQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 408 GQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdLQRELGLTyLFISHDLAVVRYIADRVAVMYDG 481
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
477-696 |
6.22e-30 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 120.15 E-value: 6.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR-ELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQS-DMNFDvLTVEE--------NLSILASvkgiPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:COG1120 76 RIAYVPQEpPAPFG-LTVRElvalgrypHLGLFGR----PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-671 |
9.67e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 118.13 E-value: 9.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemFEARKMI 558
Cdd:cd03226 1 RIENISFSYKKGTEI---LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GICPQ-SDMNFDVLTVEENLSIlaSVKGIPANNiiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLL--GLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STH 671
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIvITH 184
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1292-1516 |
1.42e-29 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 118.41 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYddkkdflhsrKTTKVaTKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYG-SHSNEDD 1370
Cdd:cd03218 3 AENLSKRY----------GKRKV-VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDiTKLPMHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1371 ESTKCMGYCPQTNPLWPDITLQEHfeIYGAVKGMssGDMKEVISRITKALdLKE-HLQKTVKK----LPAGIKRKLCFAL 1445
Cdd:cd03218 72 RARLGIGYLPQEASIFRKLTVEEN--ILAVLEIR--GLSKKEREEKLEEL-LEEfHITHLRKSkassLSGGERRRVEIAR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1446 SMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03218 147 ALATNPKFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1314-1519 |
2.33e-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: 2.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQ 1392
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVlFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 E-------HFEIYGAVKGMSSGDMKEVISRITKALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:cd03219 94 EnvmvaaqARTGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1463 MDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:cd03219 174 LNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
477-710 |
2.73e-29 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 126.49 E-value: 2.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEA 554
Cdd:COG2274 473 DIELENVSFRYP--GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--RILidGIDLRQID-PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQSDMNFDVlTVEENLSIlaSVKGIPANNIIQEVQKVLLD---------LDMQaIKDNqAKKLSGGQKRKLSL 625
Cdd:COG2274 548 RRQIGVVLQDVFLFSG-TIRENITL--GDPDATDEEIIEAARLAGLHdfiealpmgYDTV-VGEG-GSNLSGGQRQRLAI 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGSSIFLKSKW 704
Cdd:COG2274 623 ARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLADRIIVLDKGRIVEDGTHEELLARK 700
|
....*.
gi 27368659 705 GIGYRL 710
Cdd:COG2274 701 GLYAEL 706
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
477-691 |
3.22e-29 |
|
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: 117.98 E-value: 3.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK 556
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 --MIGICPQSDMNfDVLTVEENLSILASVKGIPanNIIQEVQKVLLDLDM-QAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:COG1124 81 vqMVFQDPYASLH-PRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 634 KILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKdLREERGLTyLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
477-696 |
3.24e-29 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 120.95 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDEmfeA 554
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG--EILigGRDVTDLPP---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 635 ILLLDEPTAGMDPCSRhivWNL---LKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG3839 154 VFLLDEPLSNLDAKLR---VEMraeIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
478-691 |
3.48e-29 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 117.08 E-value: 3.48e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:COG2884 2 IRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQsdmNF---DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:COG2884 79 RRIGVVFQ---DFrllPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNR 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADILADRKA---VISQGML 691
Cdd:COG2884 156 PELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiATH---DLELVDRMPKrvlELEDGRL 215
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
478-656 |
7.57e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.67 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFE-ARK 556
Cdd:COG1137 4 LEAENLVKSYGKR--TV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-MHKrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180
....*....|....*....|....
gi 27368659 637 LLDEPTAGMDPCS----RHIVWNL 656
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKIIRHL 182
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
496-676 |
7.85e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 125.62 E-value: 7.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemFEARKMIGICPQSdmnFDV---LT 572
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRRVGYMSQA---FSLygeLT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|....*.
gi 27368659 653 VWNLL-KYRKANRVTVF-STHFMDEA 676
Cdd:NF033858 436 FWRLLiELSREDGVTIFiSTHFMNEA 461
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1294-1520 |
8.57e-29 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 116.60 E-value: 8.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYG-SHSNEDDES 1372
Cdd:TIGR04406 6 NLIKSYKKRK-----------VVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDiTHLPMHERA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1373 TKCMGYCPQTNPLWPDITLQEHFEiygAVKGMSSGDMKEVISRITKALdLKEHLQKTVKKLPA-----GIKRKLCFALSM 1447
Cdd:TIGR04406 75 RLGIGYLPQEASIFRKLTVEENIM---AVLEIRKDLDRAEREERLEAL-LEEFQISHLRDNKAmslsgGERRRVEIARAL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1448 LGNPQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:TIGR04406 151 ATNPKFILLDEPFAGVDPIAVGDIKKIIKH-LKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
478-689 |
9.99e-29 |
|
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: 114.21 E-value: 9.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-SEIDEMFEARK 556
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANR-VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLgITVvLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
497-671 |
1.18e-28 |
|
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: 114.57 E-value: 1.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-GFASIYGHRVSeideMFEARKMIGICPQSDMNFDVLTVE 574
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLD----KRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSILASVKGIpanniiqevqkvlldldmqaikdnqakklSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVW 654
Cdd:cd03213 101 ETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*...
gi 27368659 655 NLLK-YRKANRVTVFSTH 671
Cdd:cd03213 152 SLLRrLADTGRTIICSIH 169
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
496-704 |
1.72e-28 |
|
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: 116.78 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEARKMIGIC---PQSDMnFDv 570
Cdd:TIGR04521 20 ALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDLRKKVGLVfqfPEHQL-FE- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 571 LTVEE-------NLsilasvkGIPANNIIQEVQKVL--LDLDmQAIKDNQAKKLSGGQKRKLSlgIA-VLG-NPKILLLD 639
Cdd:TIGR04521 98 ETVYKdiafgpkNL-------GLSEEEAEERVKEALelVGLD-EEYLERSPFELSGGQMRRVA--IAgVLAmEPEVLILD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 640 EPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS--IFLKSKW 704
Cdd:TIGR04521 168 EPTAGLDPKGRKEILDLFKrlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPreVFSDVDE 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
477-710 |
1.81e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 122.57 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4987 333 SLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED-DLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVlTVEENLSIlasvkgipANN------IIQEVQKVLLD---------LDMQAikDNQAKKLSGGQKR 621
Cdd:COG4987 410 RIAVVPQRPHLFDT-TLRENLRL--------ARPdatdeeLWAALERVGLGdwlaalpdgLDTWL--GEGGRRLSGGERR 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSIFLK 701
Cdd:COG4987 479 RLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELL 557
|
....*....
gi 27368659 702 SKWGIGYRL 710
Cdd:COG4987 558 AQNGRYRQL 566
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
478-695 |
2.45e-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: 114.27 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03301 74 IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03301 154 MDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
495-689 |
3.14e-28 |
|
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: 114.54 E-value: 3.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVE 574
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSILASVKGIPANNIIQEVqkvlLDLdMQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPcsrH 651
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEI----YEL-FPVLKEMLGRRggdLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP---S 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 652 IVWN----LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:TIGR03410 166 IIKDigrvIRRLRAEGGMAIlLVEQYLDFARELADRYYVMERG 208
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
477-689 |
3.96e-28 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 114.77 E-value: 3.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQsdmNFDV---LTVEEN--------LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKL 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 624 slGIA--VLGNPKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG3638 156 --AIAraLVQEPKLILADEPVASLDPKTARQVMDLL--RRIARedgITVvVNLHQVDLARRYADRIIGLRDG 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
477-689 |
6.69e-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: 117.12 E-value: 6.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEARK 556
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 -MIGICPQSDMNFDVLTVEEN----LsilaSVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLG--IAV 629
Cdd:COG3842 77 rNVGMVFQDYALFPHLTVAENvafgL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAraLAP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 630 lgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG3842 153 --EPRVLLLDEPLSALDAKLREEMREELRrLQRELGITfIYVTHDQEEALALADRIAVMNDG 212
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
478-689 |
9.06e-28 |
|
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: 113.30 E-value: 9.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---F--ASIYGHRVSEIdemf 552
Cdd:cd03219 1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlFdgEDITGLPPHEI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 eARKmiGIC-----PQSdmnFDVLTVEENLSI-------LASVKGIPANNIIQEVQKV--LLD-LDMQAIKDNQAKKLSG 617
Cdd:cd03219 73 -ARL--GIGrtfqiPRL---FPELTVLENVMVaaqartgSGLLLARARREEREARERAeeLLErVGLADLADRPAGELSY 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 618 GQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03219 147 GQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVlLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
495-691 |
1.06e-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: 112.63 E-value: 1.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfeaRKMIGICPQS-DMNFDV-LT 572
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQRrSIDRDFpIS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSiLASVKGIPANNII-----QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:cd03235 87 VRDVVL-MGLYGHKGLFRRLskadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27368659 648 CSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03235 166 KTQEDIYELLReLRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
490-701 |
1.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 114.51 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFAS---IYGHRVSEiDEMFEARKMIGICPQS-D 565
Cdd:PRK13640 16 PDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTA-KTVWDIREKVGIVFQNpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 MNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLGnPKILLLDEPTAG 644
Cdd:PRK13640 95 NQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE-PKIIILDESTSM 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 645 MDPCSRHIVWNLL-KYRKANRVTVFS-THFMDEADiLADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK13640 174 LDPAGKEQILKLIrKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGSpvEIFSK 233
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
477-696 |
1.74e-27 |
|
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: 112.82 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfeaRK 556
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILASVKGI----PANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRrlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
478-689 |
2.63e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.79 E-value: 2.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID--EMFE 553
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSG--SVLvdGVDLTALSerELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 554 ARKMIGICPQsdmNFDVL---TVEEN----LSILasvkGIPANNIIQEVQKvLLDL-DMQAIKDNQAKKLSGGQKRKlsL 625
Cdd:COG1135 80 ARRKIGMIFQ---HFNLLssrTVAENvalpLEIA----GVPKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQR--V 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 626 GIA-VL-GNPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1135 150 GIArALaNNPKVLLCDEATSALDPETTRSILDLLK--DINRelgLTiVLITHEMDVVRRICDRVAVLENG 217
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
477-696 |
3.73e-27 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 118.32 E-value: 3.73e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4988 336 SIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA-SWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDvLTVEENLSILASvkGIPANNIIQEVQKVLLD---------LDMQaIKDNqAKKLSGGQKRKLSLGI 627
Cdd:COG4988 412 QIAWVPQNPYLFA-GTIRENLRLGRP--DASDEELEAALEAAGLDefvaalpdgLDTP-LGEG-GRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGS 696
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1290-1510 |
4.84e-27 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 109.20 E-value: 4.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSN 1367
Cdd:cd03229 1 LELKNVSKRYGQKT-----------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKCMGYCPQTNPLWPDITlqehfeiygavkgmssgdmkeVISRITKALDlkehlqktvkklpAGIKRKLCFALSM 1447
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLT---------------------VLENIALGLS-------------GGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1448 LGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
494-647 |
9.72e-27 |
|
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: 110.46 E-value: 9.72e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKMIGICPQSDMNF 568
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirFDgeDITGLPPHRI-----ARLGIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLsILASVKGIPANNIIQEVQKVLlDL--DMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG0410 91 PSLTVEENL-LLGAYARRDRAEVRADLERVY-ELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLA 168
|
.
gi 27368659 647 P 647
Cdd:COG0410 169 P 169
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
479-695 |
1.10e-26 |
|
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: 108.29 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMI 558
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK-ELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GICPQsdmnfdvltveenlsilasvkgipanniiqevqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 639 DEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1314-1511 |
1.27e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 110.90 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsneDDESTKCMGycP------------Q 1381
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILF---------DGRDITGLP--PhriarlgiartfQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1382 TNPLWPDITLQEHFEIyGAVKGMSSG-------------DMKEVISRITKALD---LKEHLQKTVKKLPAGIKRKLCFAL 1445
Cdd:COG0411 87 NPRLFPELTVLENVLV-AAHARLGRGllaallrlprarrEEREARERAEELLErvgLADRADEPAGNLSYGQQRRLEIAR 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1446 SMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG0411 166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
478-689 |
1.41e-26 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 109.97 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDEMFEAR 555
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMNFDVLTVEEN-----LSILASVKGIPANNIIQEVQKVLLDLDMQAIKD---NQAKKLSGGQKRKLSLGI 627
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDkayQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-691 |
1.41e-26 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 109.31 E-value: 1.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFDIyEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVseideMFEARKMIGICP---------QSDMNFD 569
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTV-----LFDSRKKINLPPqqrkiglvfQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 570 VLTVEENlsILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:cd03297 89 HLNVREN--LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 650 RHIVWNLLKYRKA--NRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03297 167 RLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
488-671 |
1.76e-26 |
|
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: 109.28 E-value: 1.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGH-----RVSEIDEMfeaRKMIGICP 562
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGQilfngQPRKPDQF---QKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 563 QSDMNFDVLTVEENLSILASVKG--IPANNIIQEV--QKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|....
gi 27368659 639 DEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH 671
Cdd:cd03234 168 DEPTSGLDSFTALnLVSTLSQLARRNRIVILTIH 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-676 |
1.78e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 110.56 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKK--NETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR 555
Cdd:COG1101 2 LELKNLSKTFNPGtvNEKR-ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 K--------MIGICPQsdmnfdvLTVEENLSiLASVKG-----IPANNI--IQEVQKVL--LDLDMQAIKDNQAKKLSGG 618
Cdd:COG1101 81 YigrvfqdpMMGTAPS-------MTIEENLA-LAYRRGkrrglRRGLTKkrRELFRELLatLGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 619 QKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR-KANRVTVFS-THFMDEA 676
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMvTHNMEQA 212
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
489-689 |
2.22e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.59 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQS-DMN 567
Cdd:PRK13650 15 KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDIRHKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13650 94 FVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 648 CSR-HIVWNLLKYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13650 174 EGRlELIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNG 216
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
478-694 |
4.21e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 110.14 E-value: 4.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKN--ETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDE---MF 552
Cdd:PRK13637 3 IKIENLTHIYMEGTpfEKK-ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG--KIIIDGVDITDKkvkLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 EARKMIGIC---PQSDMnFDVlTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK13637 80 DIRKKVGLVfqyPEYQL-FEE-TIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGmlKCV 694
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKLADRIIVMNKG--KCE 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
478-696 |
5.27e-26 |
|
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: 108.09 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 638 LDEPTAGMDpcsrhivwnlLKYRKANRVT------------VFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03300 154 LDEPLGALD----------LKLRKDMQLElkrlqkelgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
488-695 |
5.92e-26 |
|
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: 109.27 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQS 564
Cdd:cd03294 31 LKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkELRELRrKKISMVFQS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:cd03294 111 FALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 645 MDPCSRHIVWN-LLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03294 191 LDPLIRREMQDeLLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
478-689 |
7.97e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 110.66 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQsdmNFDVL---TVEENLSILASVKGIPANNIIQEVQKvLLDL-DMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTE-LLELvGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 632 NPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLK--DINRelgLTiVLITHEMDVVKRICDRVAVIDAG 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1319-1518 |
9.78e-26 |
|
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: 108.21 E-value: 9.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSNEddESTKCMGYCPQTNPLWPDITLQE--- 1393
Cdd:COG1120 20 VSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrDLASLSRR--ELARRIAYVPQEPPAPFGLTVRElva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 -----HFeiyGAVKGMSSGDmKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK 1468
Cdd:COG1120 98 lgrypHL---GLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQ 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 1469 QHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG1120 174 LEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
478-696 |
1.10e-25 |
|
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: 104.82 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEMFEARKM 557
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 -IGICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03216 76 gIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAViFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
478-689 |
1.20e-25 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 110.24 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVSEIDEMFEARKm 557
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-NGRDLFTNLPPRERR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKvLLDL-DMQAIKD---NQakkLSGGQKRKLSLGIAVLGNP 633
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEE-LLELvQLEGLADrypSQ---LSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 634 KILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRrlHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
474-696 |
1.22e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 108.64 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAYRKKNETVE--ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEM 551
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 FEARKMIGICPQSDMNFDVLT-VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK13633 81 WDIRNKAGMVFQNPDNQIVATiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13633 161 MRPECIIFDEPTAMLDPSGRREVVNTIKelNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1289-1517 |
1.40e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.47 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEY-------DDKKDFLHSRKTTKVATKY----VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI 1357
Cdd:COG1134 4 MIEVENVSKSYrlyhepsRSLKELLLRRRRTRREEFWalkdVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1358 -------FLGDYGS--HsneddestkcmgycpqtnplwPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQK 1428
Cdd:COG1134 84 evngrvsALLELGAgfH---------------------PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1429 TVKKLPAGIKRKLCFALSMLGNPQVTLLDEP-STGmDP----RAKQHMwrairTAFKNKKRAALLTTHYMEEAEAVCDRV 1503
Cdd:COG1134 143 PVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DAafqkKCLARI-----RELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|....
gi 27368659 1504 AIMVSGQLRCIGTV 1517
Cdd:COG1134 217 IWLEKGRLVMDGDP 230
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
488-728 |
1.72e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 109.41 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeaRKMIGIcpqsdmn 567
Cdd:COG4586 29 RREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEF--ARRIGV------- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 fdV----------LTVEENLSILASVKGIPaNNIIQEVQKVLLD-LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG4586 100 --VfgqrsqlwwdLPAIDSFRLLKAIYRIP-DAEYKKRLDELVElLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKIL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVF-STHFMDeaDI--LADRKAVISQGMLKCVGSSIFLKSKWGIGYRLSM 712
Cdd:COG4586 177 FLDEPTIGLDVVSKEAIREFLKeYNRERGTTILlTSHDMD--DIeaLCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVL 254
|
250
....*....|....*.
gi 27368659 713 YIDRYCATESLSSLVR 728
Cdd:COG4586 255 ELAEPVPPLELPRGGE 270
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1319-1523 |
2.12e-25 |
|
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: 106.65 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsNEDDEST-----KCMGYCPQTNPLWPDITLQE 1393
Cdd:cd03299 18 VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILL-------NGKDITNlppekRDISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEiYG--AVKGMSSGDMKEVIsRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:cd03299 91 NIA-YGlkKRKVDKKEIERKVL-EIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1472 WRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1288-1519 |
2.38e-25 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 106.71 E-value: 2.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1288 PAIMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgshsn 1367
Cdd:COG1121 5 PAIELENLTVSYGGR-----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGK----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKCMGYCPQT---NPLWPdITLQE--------HFeiyGAVKGMSSGDmKEVISRITKALDLKEHLQKTVKKLPAG 1436
Cdd:COG1121 69 PPRRARRRIGYVPQRaevDWDFP-ITVRDvvlmgrygRR---GLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1437 IKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVaIMVSGQLRCIGT 1516
Cdd:COG1121 144 QQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGP 221
|
...
gi 27368659 1517 VQH 1519
Cdd:COG1121 222 PEE 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
484-691 |
2.80e-25 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 105.57 E-value: 2.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 484 QKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGIC 561
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 562 PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 642 TAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
494-647 |
3.67e-25 |
|
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: 106.28 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKmiGIC-----PQ 563
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGrilFDgrDITGLPPHRI-----ARL--GIArtfqnPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 564 SdmnFDVLTVEENL----------SILASVKGIPAN-----NIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG0411 90 L---FPELTVLENVlvaaharlgrGLLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170
....*....|....*....
gi 27368659 629 VLGNPKILLLDEPTAGMDP 647
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNP 185
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1290-1521 |
3.95e-25 |
|
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: 105.66 E-value: 3.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSN 1367
Cdd:cd03261 1 IELRGLTKSFGGRT-VLKG----------VDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 -EDDESTKCMGYCPQTNPLWPDIT--------LQEHFEiygavkgMSSGDMKEVISRITKALDLKEhlqkTVKKLPA--- 1435
Cdd:cd03261 70 aELYRLRRRMGMLFQSGALFDSLTvfenvafpLREHTR-------LSEEEIREIVLEKLEAVGLRG----AEDLYPAels 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1436 -GIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:cd03261 139 gGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
....*..
gi 27368659 1515 GTVQHLK 1521
Cdd:cd03261 219 GTPEELR 225
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1319-1522 |
4.66e-25 |
|
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: 105.21 E-value: 4.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsnEDDESTKC-------MGYCPQTNPLWPDITL 1391
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG------RDITGLPPheraragIGYVPEGRRIFPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIYGAVKGMSSG--DMKEVISRITKaldLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQ 1469
Cdd:cd03224 93 EENLLLGAYARRRAKRkaRLERVYELFPR---LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1470 HMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:cd03224 170 EIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
494-676 |
5.23e-25 |
|
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: 104.04 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEID----EMFEARKMIGICPQS-DMNF 568
Cdd:TIGR01166 5 PEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG---EPLDysrkGLLERRQRVGLVFQDpDDQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:TIGR01166 82 FAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....*....
gi 27368659 649 SRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:TIGR01166 162 GREQMLAILrRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1319-1506 |
5.53e-25 |
|
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: 104.54 E-value: 5.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSNEDDEStkcMGYCPQT---NPLWPdITLqEHF 1395
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV--FGKPLEKERKR---IGYVPQRrsiDRDFP-ISV-RDV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1396 EIYGAV--KGMSSGDMKEVISRITKALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQH 1470
Cdd:cd03235 91 VLMGLYghKGLFRRLSKADKAKVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQED 170
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 1471 MWRAIRTAfKNKKRAALLTTHYMEEAEAVCDRVAIM 1506
Cdd:cd03235 171 IYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
497-703 |
6.20e-25 |
|
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: 105.11 E-value: 6.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQSDMNFDVLTVEEN 576
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNLPPEKRDISYVPQNYALFPHMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL 656
Cdd:cd03299 92 IAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 657 LK-YRKANRVTVFS-THFMDEADILADRKAVISQGMLKCVGS--SIFLKSK 703
Cdd:cd03299 172 LKkIRKEFGVTVLHvTHDFEEAWALADKVAIMLNGKLIQVGKpeEVFKKPK 222
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
487-689 |
8.40e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.21 E-value: 8.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDM 566
Cdd:cd03245 10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQDVT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NFDVlTVEENLS----------ILASVKGIPANNIiqeVQKVLLDLDMQaIKDnQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03245 89 LFYG-TLRDNITlgapladderILRAAELAGVTDF---VNKHPNGLDLQ-IGE-RGRGLSGGQRQAVALARALLNDPPIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 637 LLDEPTAGMDPCS-RHIVWNLLKYRkANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03245 163 LLDEPTSAMDMNSeERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSG 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
496-689 |
9.12e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 105.60 E-value: 9.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQSDMN-------- 567
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHIGIVFQNPDNqfvgsivk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 FDVLTVEENLSIlasvkgiPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMD 646
Cdd:PRK13648 103 YDVAFGLENHAV-------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIaGVLAL-NPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27368659 647 PCSRHIVWNLLKYRKANR-VTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHnITIISiTHDLSEA-MEADHVIVMNKG 218
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1290-1516 |
1.61e-24 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 103.86 E-value: 1.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHS--- 1366
Cdd:cd03300 1 IELENVSKFYGGF-----------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpp 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 NEddestKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALS 1446
Cdd:cd03300 70 HK-----RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1447 MLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03300 145 LVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1290-1515 |
2.18e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 103.38 E-value: 2.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFLHSRKTTKVATKY-----------VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI- 1357
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSLKKLGILGRKgevgefwalkdVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1358 ---------FLGdYGSHsneddestkcmgycpqtnplwPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQK 1428
Cdd:cd03220 81 vrgrvssllGLG-GGFN---------------------PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1429 TVKKLPAGIKRKLCFALSMLGNPQVTLLDEP-STGmDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMV 1507
Cdd:cd03220 139 PVKTYSSGMKARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLE 216
|
....*...
gi 27368659 1508 SGQLRCIG 1515
Cdd:cd03220 217 KGKIRFDG 224
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
477-696 |
2.89e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 2.89e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEAR- 555
Cdd:PRK10851 2 SIEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL----HARd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMNFDVLTVEEN----LSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 632 NPKILLLDEPTAGMDPCSRHIV--W-----NLLKYrkanrVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELrrWlrqlhEELKF-----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1292-1511 |
3.53e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 102.58 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKDFLHsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDD 1370
Cdd:cd03257 4 VKNLSVSFPTGGGSVK-------ALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1371 EST--KCMGYCPQtNP---LWPDITLQEHFE--IYGAVKGMSSGDMKEVISRITKALDLKEHLqktVKKLPA----GIKR 1439
Cdd:cd03257 77 RKIrrKEIQMVFQ-DPmssLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEV---LNRYPHelsgGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1440 KLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03257 153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1325-1515 |
3.56e-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: 102.37 E-value: 3.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1325 KGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD---YGSHSNEDDESTK-CMGYCPQTNPLWPDITLQEHFEiYGA 1400
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENLA-FGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 vKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFK 1480
Cdd:cd03297 101 -KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|....*
gi 27368659 1481 NKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03297 180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
478-689 |
4.56e-24 |
|
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: 100.75 E-value: 4.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIqkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-ELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDvltveenlsilasvkGIPANNIiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03246 78 VGYLPQDDELFS---------------GSIAENI-----------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMdEADILADRKAVISQG 689
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRP-ETLASADRILVLEDG 171
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1319-1511 |
4.61e-24 |
|
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: 101.56 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNeddESTKCMGYCPQtnplwpDITLQEHFE-- 1396
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK---ERRKSIGYVMQ------DVDYQLFTDsv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 ----IYGAvkgMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMW 1472
Cdd:cd03226 90 reelLLGL---KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVG 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1473 RAIRTAfKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03226 167 ELIREL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
460-689 |
5.69e-24 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 109.57 E-value: 5.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 460 SLNEIVE-----PVSSEFIGKE----AIRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL 530
Cdd:TIGR03375 437 SLDELMQlpverPEGTRFLHRPrlqgEIEFRNVSFAY--PGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGL 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 531 CPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDVlTVEENL----------SILASVKGIPANNIIQEVQKvll 600
Cdd:TIGR03375 515 YQPTEGSVLLDGVDIRQID-PADLRRNIGYVPQDPRLFYG-TLRDNIalgapyaddeEILRAAELAGVTEFVRRHPD--- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 601 DLDMQAIKDNQAkkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLA 680
Cdd:TIGR03375 590 GLDMQIGERGRS--LSGGQRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLD-LV 666
|
....*....
gi 27368659 681 DRKAVISQG 689
Cdd:TIGR03375 667 DRIIVMDNG 675
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1314-1516 |
7.44e-24 |
|
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: 99.81 E-value: 7.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsneddestkcmgycpqtnplwpditlqE 1393
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-------------------------------K 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEIYGAVKGMSSGdmkevISritkaldlkehlqkTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWR 1473
Cdd:cd03216 63 EVSFASPRDARRAG-----IA--------------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 1474 AIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGqlRCIGT 1516
Cdd:cd03216 124 VIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1294-1506 |
7.51e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 101.39 E-value: 7.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKdflhsrkTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDest 1373
Cdd:cd03293 5 NVSKTYGGGG-------GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 kcMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQV 1453
Cdd:cd03293 75 --RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1454 TLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIM 1506
Cdd:cd03293 153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
497-675 |
9.45e-24 |
|
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: 102.08 E-value: 9.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF-ASIYGHRVSEIDeMFEARKMIGIC-PQSDMNFDV-LTV 573
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED-VWELRKRIGLVsPALQLRFPRdETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EEnlSIL----ASVkGIPAN---NIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1119 98 LD--VVLsgffDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190
....*....|....*....|....*....|.
gi 27368659 647 PCSRHIVWNLLKY--RKANRVTVFSTHFMDE 675
Cdd:COG1119 175 LGARELLLALLDKlaAEGAPTLVLVTHHVEE 205
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
478-689 |
1.11e-23 |
|
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: 101.61 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMNFDVLTVEENLSI--LASVKGIPAnnII-----QEVQKVLLDLDMQAIKD---NQAKKLSGGQKRKLSL 625
Cdd:TIGR02315 79 RRIGMIFQHYNLIERLTVLENVLHgrLGYKPTWRS--LLgrfseEDKERALSALERVGLADkayQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1312-1515 |
1.14e-23 |
|
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: 100.79 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1312 TKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYcpQTNPLWPDITL 1391
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF--QNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 1472 WRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03301 170 RAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
459-682 |
1.47e-23 |
|
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: 106.99 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 459 ISLNEIVEPVSSEFIGKEA--IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG 536
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPAssLEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEG 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 537 FASIYGHRVSEIDEMFeARKMIGICPQSDMNFDVlTVEENlsILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKK-- 614
Cdd:TIGR02857 378 SIAVNGVPLADADADS-WRDQIAWVPQHPFLFAG-TIAEN--IRLARPDASDAEIREALERAGLDEFVAALPQGLDTPig 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 615 -----LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR-HIVWNLLKYRKaNRVTVFSTHfmDEADI-LADR 682
Cdd:TIGR02857 454 eggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEaEVLEALRALAQ-GRTVLLVTH--RLALAaLADR 525
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
489-689 |
4.73e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.94 E-value: 4.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQS-DMN 567
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13642 94 FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 648 CSRHIVWNLL-KYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13642 174 TGRQEIMRVIhEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
495-689 |
5.05e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 100.92 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-EIDEMFEARKMIGICPQ-SDMNFDVLT 572
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQnPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIaGILAM-KPEIIVLDEPTSGLDPMGAS 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 652 IVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13639 175 QIMKLLYDLNKEGITiIISTHDVDLVPVYADKVYVMSDG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1290-1520 |
6.17e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 99.33 E-value: 6.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYddkkdflhsRKTTKVatKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsneD 1369
Cdd:COG1137 4 LEAENLVKSY---------GKRTVV--KDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL---------D 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DE----------STKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSsgdmKEVISRITKALdLKE-HLQKtVKKLPA--- 1435
Cdd:COG1137 64 GEdithlpmhkrARLGIGYLPQEASIFRKLTVEDNILAVLELRKLS----KKEREERLEEL-LEEfGITH-LRKSKAysl 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1436 --GIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK---QHMwraIRTAfKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:COG1137 138 sgGERRRVEIARALATNPKFILLDEPFAGVDPIAVadiQKI---IRHL-KERGIGVLITDHNVRETLGICDRAYIISEGK 213
|
250
....*....|
gi 27368659 1511 LRCIGTVQHL 1520
Cdd:COG1137 214 VLAEGTPEEI 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1286-1516 |
7.37e-23 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 102.10 E-value: 7.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1286 EKPAIMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygsh 1365
Cdd:COG3842 2 AMPALELENVSKRYGDV-----------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1366 snED---------DestkcMGYCPQTNPLWPDITLQEHfeI-YG-AVKGMSSGDMKEvisRITKALD---LKEHLQKTVK 1431
Cdd:COG3842 67 --RDvtglppekrN-----VGMVFQDYALFPHLTVAEN--VaFGlRMRGVPKAEIRA---RVAELLElvgLEGLADRYPH 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1432 KLPAG------IKRklcfALSMlgNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAI 1505
Cdd:COG3842 135 QLSGGqqqrvaLAR----ALAP--EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAV 208
|
250
....*....|.
gi 27368659 1506 MVSGQLRCIGT 1516
Cdd:COG3842 209 MNDGRIEQVGT 219
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
497-704 |
7.45e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.67 E-value: 7.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGICPQsdmnFDVLTV 573
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENlSILASVKGIPAN----------NIIQEVQKVLLDLDMQaikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNfgfsedeakeKALKWLKKVGLSEDLI---SKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 644 GMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLKSKW 704
Cdd:PRK13641 175 GLDPEGRKEMMQLFKdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASpkEIFSDKEW 238
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-689 |
9.57e-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: 98.84 E-value: 9.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03254 3 IEFENVNFSYDEKKPV---LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVlTVEENLS----------ILASVKGIPANNIIQEVQKvllDLDMQAikDNQAKKLSGGQKRKLSLGI 627
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRlgrpnatdeeVIEAAKEAGAHDFIMKLPN---GYDTVL--GENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMD---EAD--ILADRKAVISQG 689
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNADkiLVLDDGKIIEEG 219
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
487-689 |
1.05e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.81 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmFEARKMIGICPQ--S 564
Cdd:PRK13647 12 FRYKDGT-KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRSKVGLVFQdpD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNFDVlTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PRK13647 90 DQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 645 MDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13647 169 LDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
496-696 |
1.08e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 102.22 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfeaRKMIGICPQSDMNFDVLTVEE 575
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINMMFQSYALFPHMTVEQ 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR----H 651
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRdrmqL 190
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27368659 652 IVWNLLKYRKANRVTVfsTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11607 191 EVVDILERVGVTCVMV--THDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1294-1511 |
1.26e-22 |
|
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: 97.95 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYddkkdflHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD----YGSHSNED 1369
Cdd:cd03255 5 NLSKTY-------GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisKLSEKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03255 78 AFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAvCDRVAIMVSGQL 1511
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1319-1522 |
1.48e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 98.13 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsnED------DESTKC-MGYCPQTNPLWPDITL 1391
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG------EDitglppHRIARLgIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIyGAVKGMSSGDMKEVISRItkaLD----LKEHLqktvkKLPAGikrklcfALS-----ML-------GNPQVTL 1455
Cdd:COG0410 96 EENLLL-GAYARRDRAEVRADLERV---YElfprLKERR-----RQRAG-------TLSggeqqMLaigralmSRPKLLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1456 LDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:COG0410 160 LDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-695 |
1.55e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 103.71 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSI----LASVKGIPA---NNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 631 GNPKILLLDEPTAGM-DPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
497-658 |
1.58e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 104.36 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVsEIDEMfeaRKMIGICPQSDMNFDVLTV 573
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEM---RAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSILASVK---GIPANNIIQEVQKVLLDLDMQAIKD------NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:TIGR00955 117 REHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170
....*....|....
gi 27368659 645 MDPCSRHIVWNLLK 658
Cdd:TIGR00955 197 LDSFMAYSVVQVLK 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1319-1515 |
2.05e-22 |
|
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: 95.97 E-value: 2.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQtnplwpditlqehfeiy 1398
Cdd:cd03214 18 LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ----------------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 gavkgmssgdmkevISRITKALDLKEhlqKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTA 1478
Cdd:cd03214 81 --------------ALELLGLAHLAD---RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELLELLRRL 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 27368659 1479 FKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03214 144 ARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
478-689 |
2.72e-22 |
|
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: 96.83 E-value: 2.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:cd03262 1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 554 aRKMIGICPQSDMNFDVLTVEENLSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03262 75 -RQKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREVADRVIFMDDG 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
476-689 |
5.82e-22 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 97.24 E-value: 5.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 476 EAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfeAR 555
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KmiGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 636 LLLDEPTAGMDPCSR-HIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:COG4525 156 LLMDEPFGALDALTReQMQELLLDVWQRTGKGVFlITHSVEEALFLATRLVVMSPG 211
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
512-697 |
6.76e-22 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 98.72 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 512 LLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNI 591
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP---HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 592 IQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFS 669
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 27368659 670 THFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1288-1521 |
9.00e-22 |
|
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: 96.20 E-value: 9.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1288 PAIMVYNLHKEYDDK---KDflhsrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYG 1363
Cdd:COG1127 4 PMIEVRNLTKSFGDRvvlDG--------------VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEIlVDGQDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1364 SHSNEDDEST--KCMGYCPQTNPLWPDIT--------LQEHFeiygavkGMSSGDMKEVISRITKALDLKEHLqktvKKL 1433
Cdd:COG1127 70 TGLSEKELYElrRRIGMLFQGGALFDSLTvfenvafpLREHT-------DLSEAEIRELVLEKLELVGLPGAA----DKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1434 PA----GIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQ---HMWRAIRTAFKNkkrAALLTTHYMEEAEAVCDRVAIM 1506
Cdd:COG1127 139 PSelsgGMRKRVALARALALDPEILLYDEPTAGLDPITSAvidELIRELRDELGL---TSVVVTHDLDSAFAIADRVAVL 215
|
250
....*....|....*
gi 27368659 1507 VSGQLRCIGTVQHLK 1521
Cdd:COG1127 216 ADGKIIAEGTPEELL 230
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
478-647 |
1.04e-21 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 95.83 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:COG1126 2 IEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 554 aRKMIGICPQSdMN-FDVLTVEENLsILA--SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQK------RKLS 624
Cdd:COG1126 76 -RRKVGMVFQQ-FNlFPHLTVLENV-TLApiKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqrvaiaRALA 152
|
170 180
....*....|....*....|...
gi 27368659 625 LgiavlgNPKILLLDEPTAGMDP 647
Cdd:COG1126 153 M------EPKVMLFDEPTSALDP 169
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-696 |
1.07e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 96.34 E-value: 1.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEE 575
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQKPTVFEELTVFE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NL--------SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4674 105 NLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27368659 648 CSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4674 185 AETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1319-1510 |
1.11e-21 |
|
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: 93.60 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWpditlqehfeiy 1398
Cdd:cd03228 21 VSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAYVPQDPFLF------------ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 gavkgmsSGDMKEVIsritkaldlkehlqktvkkLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTA 1478
Cdd:cd03228 89 -------SGTIRENI-------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEALILEALRAL 142
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 1479 FKNkkRAALLTTHYMEEAEAvCDRVAIMVSGQ 1510
Cdd:cd03228 143 AKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
499-689 |
1.33e-21 |
|
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: 94.87 E-value: 1.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEEN 576
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LSiLASVKGIPANNIIQE-VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:cd03298 91 VG-LGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 656 L-LKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03298 170 LvLDLHAETKMTVlMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-696 |
1.77e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.35 E-value: 1.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 483 IQKAYrKKNETVEalrNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICP 562
Cdd:PRK10895 9 LAKAY-KGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 563 QSDMNFDVLTVEENL-SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK10895 85 QEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 642 TAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
487-710 |
2.16e-21 |
|
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: 94.86 E-value: 2.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDM 566
Cdd:cd03252 8 FRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW-LRRQVGVVLQENV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NFDvLTVEENLS----------ILASVKGIPANNIIQEvqkvlLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03252 87 LFN-RSIRDNIAladpgmsmerVIEAAKLAGAHDFISE-----LPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-689 |
3.01e-21 |
|
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: 94.45 E-value: 3.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEMfearkmigICPQSDMNFDVLTVE 574
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSIlaSVKGIPANNIIQEVQKVLLD-LDMQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:TIGR01184 73 ENIAL--AVDRVLPDLSKSERRAIVEEhIALVGLTEAADKRpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27368659 651 -HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR01184 151 gNLQEELMQIWEEHRVTvLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
477-696 |
3.23e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 99.33 E-value: 3.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVsEIDEMFEA 554
Cdd:COG3845 5 ALELRGITKRF----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--EILidGKPV-RIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKM-IGICPQSDMNFDVLTVEENLsILASVKG----IPANNIIQEVQKVL----LDLDMQA-IKDnqakkLSGGQKRKLS 624
Cdd:COG3845 78 IALgIGMVHQHFMLVPNLTVAENI-VLGLEPTkggrLDRKAARARIRELSerygLDVDPDAkVED-----LSVGEQQRVE 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 625 lgI--AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:COG3845 152 --IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIiFITHKLREVMAIADRVTVLRRG--KVVGT 222
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
479-671 |
3.84e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRvSEIDEMFEARKMI 558
Cdd:PRK13539 2 MLEGEDLACVRGGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GicPQSDMNfDVLTVEENLSILASVKGIPANNIIQevqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK13539 79 G--HRNAMK-PALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 27368659 639 DEPTAGMDPCSRHIVWNLLKYR-KANRVTVFSTH 671
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHlAQGGIVIAATH 185
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1287-1520 |
3.95e-21 |
|
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: 99.21 E-value: 3.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1287 KPAIMVYNLHKEYddkkdflhsRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPT---SGKIFLGDYG 1363
Cdd:COG1123 2 TPLLEVRDLSVRY---------PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1364 SHSNEDDESTKCMGYCPQT-----NPLwpdiTLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIK 1438
Cdd:COG1123 73 LLELSEALRGRRIGMVFQDpmtqlNPV----TVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1439 RKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
..
gi 27368659 1519 HL 1520
Cdd:COG1123 229 EI 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
497-680 |
4.32e-21 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 93.32 E-value: 4.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEIDEmfEARKmIGICPQSDMNFDVLTV 573
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRR-IGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSiLASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC----S 649
Cdd:COG4136 94 GENLA-FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAlraqF 172
|
170 180 190
....*....|....*....|....*....|.
gi 27368659 650 RHIVWNLLkyRKANRVTVFSTHfmDEADILA 680
Cdd:COG4136 173 REFVFEQI--RQRGIPALLVTH--DEEDAPA 199
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
480-658 |
4.92e-21 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 99.80 E-value: 4.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 480 ISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA---RK 556
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVI 166
|
170 180
....*....|....*....|..
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK10535 167 LADEPTGALDSHSGEEVMAILH 188
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1243-1525 |
5.97e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.20 E-value: 5.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1243 FRAL---SQKAKHKKFPEPPINEDEDEDvkaerlkvkelmgcqcceekPAIMVYNLHKEYDDkkdFlhsrkttkVATKYV 1319
Cdd:NF033858 237 FIALlpeEKRRGHQPVVIPPRPADDDDE--------------------PAIEARGLTMRFGD---F--------TAVDHV 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSNEDDEST-KCMGYCPQTNPLWPDITLQEHFEIY 1398
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWL--FGQPVDAGDIATrRRVGYMSQAFSLYGELTVRQNLELH 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAI--- 1475
Cdd:NF033858 364 ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLiel 443
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1476 -R----TAFknkkraalLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:NF033858 444 sRedgvTIF--------ISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
477-682 |
8.83e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 97.78 E-value: 8.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRkkneTVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVsEIDEMFEARK 556
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 M-IGICPQsDMN-FDVLTVEENLSI--LASVKG-IPANNIIQEVQKVL----LDLDMQAIkdnqAKKLSGGQKRKLSLGI 627
Cdd:COG1129 79 AgIAIIHQ-ELNlVPNLSVAENIFLgrEPRRGGlIDWRAMRRRARELLarlgLDIDPDTP----VGDLSVAQQQLVEIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADR 682
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAiIYISHRLDEVFEIADR 209
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
474-696 |
9.10e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 95.30 E-value: 9.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAY-RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASI------------ 540
Cdd:PRK13631 18 DDIILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnh 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 541 ---YGHRVSEIDEMFEARKMIGIC---PQSDMNFDvlTVEENLSILASVKGIPANNIIQEVQKVL--LDLDMQAIkDNQA 612
Cdd:PRK13631 98 eliTNPYSKKIKNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLnkMGLDDSYL-ERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 613 KKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFS-THFMDEADILADRKAVISQGM 690
Cdd:PRK13631 175 FGLSGGQKRRVAIaGILAI-QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMEHVLEVADEVIVMDKGK 253
|
....*.
gi 27368659 691 LKCVGS 696
Cdd:PRK13631 254 ILKTGT 259
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
477-647 |
9.18e-21 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 93.15 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS---EIDE--M 551
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 FEARKMIGICPQSDMNFDVLTVEENLsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:COG4161 78 RLLRQKVGMVFQQYNLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARAL 156
|
170
....*....|....*...
gi 27368659 630 LGNPKILLLDEPTAGMDP 647
Cdd:COG4161 157 MMEPQVLLFDEPTAALDP 174
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
475-703 |
1.62e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 475 KEAIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCP--PSDGFASIYGHRV-SEI 548
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 549 DEMFEARKMIGICPQSDMNFDvLTVEENLSILASVKGIPANNIIQE-VQKVLLDLDM-QAIKD---NQAKKLSGGQKRKL 623
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIwDEVKDrlhDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFMN 237
|
..
gi 27368659 702 SK 703
Cdd:PRK14239 238 PK 239
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1313-1523 |
1.73e-20 |
|
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: 97.52 E-value: 1.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSNEDDES-TKCMGYCPQtNPLWPDITL 1391
Cdd:COG4988 350 RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGV-DLSDLDPASwRRQIAWVPQ-NPYLFAGTI 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIYGAvkGMSSGDMKEVIsRITKALDLkehlqktVKKLPAGI---------------KRKLCFALSMLGNPQVTLL 1456
Cdd:COG4988 428 RENLRLGRP--DASDEELEAAL-EAAGLDEF-------VAALPDGLdtplgeggrglsggqAQRLALARALLRDAPLLLL 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1457 DEPSTGMDPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:COG4988 498 DEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
478-696 |
1.88e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 1.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKm 557
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA--ENRH- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK09452 88 VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK09452 168 LDESLSALDYKLRKQMQNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
487-710 |
2.14e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 91.91 E-value: 2.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNEtvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDM 566
Cdd:cd03251 10 YPGDGP--PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NFDVlTVEENLS----------ILASVKGIPANNIIQEvqkvlLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03251 87 LFND-TVAENIAygrpgatreeVEEAARAANAHEFIME-----LPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHrlstIEN-----ADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
478-689 |
2.67e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.66 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:PRK15439 12 LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 -IGICPQSDMNFDVLTVEENlsILAsvkGIPAN--------NIIQEVQkVLLDLDMQA----IKDNQAKKLSGGQKRkls 624
Cdd:PRK15439 87 gIYLVPQEPLLFPNLSVKEN--ILF---GLPKRqasmqkmkQLLAALG-CQLDLDSSAgsleVADRQIVEILRGLMR--- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 625 lgiavlgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRV-TVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK15439 158 -------DSRILILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-689 |
3.38e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 91.02 E-value: 3.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03244 3 IEFKNVSLRYR--PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG-LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVlTVEENL------------SILASVKgipannIIQEVQKVLLDLDMQaIKDNQaKKLSGGQKRKLSL 625
Cdd:cd03244 80 ISIIPQDPVLFSG-TIRSNLdpfgeysdeelwQALERVG------LKEFVESLPGGLDTV-VEEGG-ENLSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQG 689
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKG 213
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
487-689 |
6.46e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.83 E-value: 6.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE-MFEARKMIGICPQS- 564
Cdd:PRK13636 13 YNYSDGT-HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRESVGMVFQDp 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PRK13636 92 DNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 645 MDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13636 172 LDPMGVSEIMKLLVemQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
495-696 |
6.77e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.00 E-value: 6.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDvLTVE 574
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIGVVPQDTFLFS-GTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSIlasvkGIP-ANNiiQEVqkvlldldMQAIKDNQAK-------------------KLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG1132 432 ENIRY-----GRPdATD--EEV--------EEAAKAAQAHefiealpdgydtvvgergvNLSGGQRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 635 ILLLDEPTAGMDPCS-RHIVWNLLKYRKaNRVTVFSTH----FMDeadilADRKAVISQGMLKCVGS 696
Cdd:COG1132 497 ILILDEATSALDTETeALIQEALERLMK-GRTTIVIAHrlstIRN-----ADRILVLDDGRIVEQGT 557
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1319-1511 |
7.00e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 89.15 E-value: 7.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVG--DVEPTSGKIFLGDYGSHsneDDESTKCMGYCPQTNPLWPDITLQEHFE 1396
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDILHPTLTVRETLM 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVKGMSSGDMKevisritkaldlkehlqktvkklpagikrKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIR 1476
Cdd:cd03213 105 FAAKLRGLSGGERK-----------------------------RVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR 155
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 1477 tAFKNKKRAALLTTHY-MEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03213 156 -RLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
496-712 |
8.53e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 8.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRV--SEIDE--MFEARKMIGIC---PQSDMnF 568
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNkkLKPLRKKVGIVfqfPEHQL-F 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVlTVEENLSILASVKGIPANNIIQEVQKV--LLDLDmQAIKDNQAKKLSGGQKRKLSlgIA-VLG-NPKILLLDEPTAG 644
Cdd:PRK13634 100 EE-TVEKDICFGPMNFGVSEEDAKQKAREMieLVGLP-EELLARSPFELSGGQMRRVA--IAgVLAmEPEVLVLDEPTAG 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 645 MDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLKSKWGIGYRLSM 712
Cdd:PRK13634 176 LDPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEAIGLDL 247
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
478-710 |
8.83e-20 |
|
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: 90.29 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNEtVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03249 1 IEFKNVSFRYPSRPD-VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVlTVEENLSIlasvkGipANNIIQEvqkvlldLDMQAIKD-------------------NQAKKLSGG 618
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRY-----G--KPDATDE-------EVEEAAKKanihdfimslpdgydtlvgERGSQLSGG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 619 QKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdeADIL-ADRKAVISQGMLKCVGSS 697
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRnADLIAVLQNGQVVEQGTH 221
|
250
....*....|...
gi 27368659 698 IFLKSKWGIGYRL 710
Cdd:cd03249 222 DELMAQKGVYAKL 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
478-689 |
8.84e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.52 E-value: 8.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:cd03247 1 LSINNVSFSYPEQEQQV--LKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVltveenlsilasvkgipanniiqevqkvlldldmqAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03247 77 ISVLNQRPYLFDT-----------------------------------TLRNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH------FMDEAdILADRKAVISQG 689
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHhltgieHMDKI-LFLENGKIIMQG 178
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1308-1520 |
9.30e-20 |
|
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: 90.44 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1308 SRKTTKVATKYVSFCVKKGEILGLLGPNGAGKST---IINILvgdVEPTSGKIFLGdyGSHSNEDDEST--KCMGYCPQT 1382
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTtmkMINRL---IEPTSGEIFID--GEDIREQDPVElrRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1383 NPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDL--KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPS 1460
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1461 TGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
494-689 |
9.83e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.32 E-value: 9.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTV 573
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSIlasvKGIPAN--NIIQEVQKVL-LDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:PRK11614 98 EENLAM----GGFFAErdQFQERIKWVYeLFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27368659 651 HIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENG 213
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
478-696 |
9.94e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 91.20 E-value: 9.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkkNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK13644 2 IRLENVSYSY---PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQS-DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK13644 79 VGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 637 LLDEPTAGMDPCS-RHIVWNLLKYRKANRVTVFSTHFMDEADIlADRKAVISQGMLKCVGS 696
Cdd:PRK13644 159 IFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1290-1517 |
1.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 91.26 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFlhsrktTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSN 1367
Cdd:PRK13637 3 IKIENLTHIYMEGTPF------EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvDITDKKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKCMGYCPQtnplWPDITLqehFE-------IYGAVK-GMSSGDMKEVISRITKA--LDLKEHLQKTVKKLPAGI 1437
Cdd:PRK13637 77 KLSDIRKKVGLVFQ----YPEYQL---FEetiekdiAFGPINlGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1438 KRKLCFA--LSMlgNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK13637 150 KRRVAIAgvVAM--EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
..
gi 27368659 1516 TV 1517
Cdd:PRK13637 228 TP 229
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
495-691 |
1.05e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 91.38 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---HRVSEIDEMFEARKMIGIC---PQSDMNF 568
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DvlTVEENLSILASVKGIPANNIIQEVQKVLLDLDM-QAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13646 101 D--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 648 CSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13646 179 QSKRQVMRLLKslQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
495-710 |
1.10e-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: 89.98 E-value: 1.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSdmnfdvlTVE 574
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVVPQD-------TVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSILASVK-GIP-ANN--IIQEVQKVLLDLDMQAIKDNQAK-------KLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:cd03253 87 FNDTIGYNIRyGRPdATDeeVIEAAKAAQIHDKIMRFPDGYDTivgerglKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 644 GMD-PCSRHIVWNLLKYRKaNRVTVFSTHFMDEAdILADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:cd03253 167 ALDtHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
484-689 |
1.15e-19 |
|
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: 89.51 E-value: 1.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 484 QKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhRVSEIDEMfearkMIGICPQ 563
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL-----GGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 564 sdmnfdvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:cd03220 99 -------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 644 GMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03220 172 VGDAAFQEKCQRRLRELLKQGKTViLVSHDPSSIKRLCDRALVLEKG 218
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1319-1516 |
1.22e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 94.31 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsneDDEStkcmgyCPQTNP-------------- 1384
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILL---------DGEP------VRFRSPrdaqaagiaiihqe 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1385 --LWPDITLQE----HFEI--YGAVkgmssgDMKEVISRITKALD---LKEHLQKTVKKLPAGiKRKL---CFALSMlgN 1450
Cdd:COG1129 88 lnLVPNLSVAEniflGREPrrGGLI------DWRAMRRRARELLArlgLDIDPDTPVGDLSVA-QQQLveiARALSR--D 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1451 PQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLrcIGT 1516
Cdd:COG1129 159 ARVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1290-1518 |
1.22e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 92.52 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsneD 1369
Cdd:COG1118 3 IEVRNISKRFGSFT-----------LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG-------R 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKC------MGYCPQTNPLWPDITLQEHfeI-YGA-VKGMSSGDMKEVISRITKALDLkEHLQktvKKLPAgikrkl 1441
Cdd:COG1118 65 DLFTNLpprerrVGFVFQHYALFPHMTVAEN--IaFGLrVRPPSKAEIRARVEELLELVQL-EGLA---DRYPS------ 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1442 cfALS-----------ML-GNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:COG1118 133 --QLSggqrqrvalarALaVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
....*....
gi 27368659 1510 QLRCIGTVQ 1518
Cdd:COG1118 211 RIEQVGTPD 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1315-1619 |
1.34e-19 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 92.49 E-value: 1.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1315 ATKYVSFCVKKGEILGLLGPNGAG--KSTIINILVGdvePTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQ 1392
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMW 1472
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1473 RAIRTAFKNKKrAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGkGYFLEIKLKdwiENLEIDRLQREI-Q 1551
Cdd:NF000106 185 DEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPA---HAAELDRMVGAIaQ 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1552 YIFPNASRQESFSSILAYKIPKEDVQSLSQSFAKLEEakHTFAIEEYSFSQATLEQVFVELTKEQEEE 1619
Cdd:NF000106 260 AGLDGIAGATADHEDGVVNVPIVSDEQLSAVVGMLGE--RGFTISGHQHPSAQL*EVFLAITGQKTSE 325
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1287-1459 |
1.55e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.36 E-value: 1.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1287 KPAIMVYNLHKEYDDKKDFLHsrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdygshs 1366
Cdd:COG0488 313 KKVLELEGLSKSYGDKTLLDD-----------LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 neddESTKcMGYCPQTN-PLWPDITLQEHfeiygaVKGMSSGDMKEVISRITKALDLK-EHLQKTVKKLPAGIKRKLCFA 1444
Cdd:COG0488 376 ----ETVK-IGYFDQHQeELDPDKTVLDE------LRDGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALA 444
|
170
....*....|....*
gi 27368659 1445 LSMLGNPQVTLLDEP 1459
Cdd:COG0488 445 KLLLSPPNVLLLDEP 459
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
478-691 |
1.68e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.16 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK10908 2 IRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNLlkYRKANRVTV---FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRL--FEEFNRVGVtvlMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1319-1530 |
1.71e-19 |
|
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: 94.90 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPD-----ITLqe 1393
Cdd:COG2274 494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGtirenITL-- 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 hfeiygavkGMSSGDMKEVI--SRITKALDLKEHLQK---TV-----KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGM 1463
Cdd:COG2274 572 ---------GDPDATDEEIIeaARLAGLHDFIEALPMgydTVvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1464 DPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFL 1530
Cdd:COG2274 643 DAETEAIILENLRRLLKG--RTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
496-691 |
1.87e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 90.57 E-value: 1.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGIC---PQSDMnfd 569
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVfqfPESQL--- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 570 vltVEEnlSILASVKGIPANNIIQEVQKVLL---DLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK13649 99 ---FEE--TVLKDVAFGPQNFGVSQEEAEALareKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 643 AGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTiVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1292-1516 |
2.85e-19 |
|
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: 89.63 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKDFLHSRKTTkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDE 1371
Cdd:cd03294 17 AFKLLAKGKSKEEILKKTGQT-VGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1372 ST----KCMGYCPQTNPLWPDITLQEHFEiYG-AVKGMSSgdmKEVISRITKALD---LKEHLQKTVKKLPAGIKRKLCF 1443
Cdd:cd03294 96 LRelrrKKISMVFQSFALLPHRTVLENVA-FGlEVQGVPR---AEREERAAEALElvgLEGWEHKYPDELSGGMQQRVGL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1444 ALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03294 172 ARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
478-685 |
3.12e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.50 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEID--EMF 552
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 EAR-KMIGICPQSDMN-FD-VLTVEENLS-ILASVKGIPANNIIQEVQKVL----LDLDMQAIKD--NQakkLSGGQKRK 622
Cdd:COG0444 82 KIRgREIQMIFQDPMTsLNpVMTVGDQIAePLRIHGGLSKAEARERAIELLervgLPDPERRLDRypHE---LSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHfmdeaDI-----LADRKAV 685
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaiLFITH-----DLgvvaeIADRVAV 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
495-671 |
3.31e-19 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 93.19 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVE 574
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQD-EVRRRVSVCAQDAHLFDT-TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSILAsvKGIPANNIIQEVQKVLLDLDMQAIKDN-------QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:TIGR02868 427 ENLRLAR--PDATDEELWAALERVGLADWLRALPDGldtvlgeGGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 27368659 648 CSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITH 528
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1289-1516 |
3.40e-19 |
|
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: 88.55 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDkkdFlhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHS 1366
Cdd:cd03296 2 SIEVRNVSKRFGD---F--------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgeDATDVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 NEDDEstkcMGYCPQTNPLWPDITLQEH----FEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLC 1442
Cdd:cd03296 71 VQERN----VGFVFQHYALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1443 FALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1285-1520 |
3.94e-19 |
|
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: 93.04 E-value: 3.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1285 EEKPAIMVYNLHKEYDDKkdflhsRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DY 1362
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVR------GKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1363 GSHSNEDD-ESTKCMGYCPQ-----TNPLWP--DItLQEHFEIYGAVKGmssgdmKEVISRITKALDL----KEHLQKTV 1430
Cdd:COG1123 330 TKLSRRSLrELRRRVQMVFQdpyssLNPRMTvgDI-IAEPLRLHGLLSR------AERRERVAELLERvglpPDLADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1431 KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250
....*....|
gi 27368659 1511 LRCIGTVQHL 1520
Cdd:COG1123 483 IVEDGPTEEV 492
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
496-696 |
4.68e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.41 E-value: 4.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FASIYGHRVSEIDEMFEARKMIGIC---PQSDMnfd 569
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtVGDIVVSSTSKQKEIKPVRKKVGVVfqfPESQL--- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 570 vltVEEnlSILASVKGIPANNII--QEVQKVLLD-LDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK13643 98 ---FEE--TVLKDVAFGPQNFGIpkEKAEKIAAEkLEMVGLADEFWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 643 AGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13643 173 AGLDPKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
477-647 |
4.74e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 88.15 E-value: 4.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDE--M 551
Cdd:PRK11124 2 SIQLNGINCFY----GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 FEARKMIGICPQSDMNFDVLTVEENLsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK11124 78 RELRRNVGMVFQQYNLWPHLTVQQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170
....*....|....*...
gi 27368659 630 LGNPKILLLDEPTAGMDP 647
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDP 174
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
473-695 |
4.80e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.94 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 473 IGKEAIRISGIQKAYRKKNE-TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyghRVSE---- 547
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewvd 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 548 -----IDEMFEARKMIGICPQSDMNFDVLTVEENLSILASVKgIPANniiQEVQKVLLDLDMQAIKDNQAK--------K 614
Cdd:TIGR03269 352 mtkpgPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGLE-LPDE---LARMKAVITLKMVGFDEEKAEeildkypdE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKA-NRVTVFSTHFMDEADILADRKAVISQGMLK 692
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIV 507
|
...
gi 27368659 693 CVG 695
Cdd:TIGR03269 508 KIG 510
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1319-1510 |
6.27e-19 |
|
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: 88.22 E-value: 6.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSG---KIFLGDYGSHSneddestkcmgycpqtnpLWpDI------ 1389
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRGGED------------------VW-ELrkrigl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1390 ---TLQEHFEIYGAVKGM-------SSG-------DMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQ 1452
Cdd:COG1119 83 vspALQLRFPRDETVLDVvlsgffdSIGlyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1287-1566 |
6.48e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 6.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1287 KPAIMVYNLHKEYDDKKdflhsrkttKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHS 1366
Cdd:PRK13632 5 SVMIKVENVSFSYPNSE---------NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 NEDDESTKCMGYCPQTnplwPD-----ITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKL 1441
Cdd:PRK13632 76 ENLKEIRKKIGIIFQN----PDnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1442 CFALSMLGNPQVTLLDEpSTGM-DPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK13632 152 AIASVLALNPEIIIFDE-STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEI 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1521 kskfgkgyfleIKLKDWIENLEID-----RLQREIQYIFPNASRQESFSSI 1566
Cdd:PRK13632 230 -----------LNNKEILEKAKIDspfiyKLSKKLKGIDPTYNEEELIEQI 269
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-696 |
1.23e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 89.40 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE----IDEMFEARKmIGICPQSDMNFDVLTVEE 575
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRR-IGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSILASVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD-PCSRHIVW 654
Cdd:TIGR02142 95 NLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdPRKYEILP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 655 NLLKYRKANRV-TVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:TIGR02142 173 YLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1319-1516 |
1.61e-18 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 86.87 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsnED-------DESTKCMGYCPQTNPLWPDITL 1391
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD------EDisllplhARARRGIGYLPQEASIFRRLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFeiygavkgMSSGDMKEVIS---RITKALDLKE-----HLQKTV-KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:PRK10895 96 YDNL--------MAVLQIRDDLSaeqREDRANELMEefhieHLRDSMgQSLSGGERRRVEIARALAANPKFILLDEPFAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1463 MDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK10895 168 VDPISVIDIKRIIE-HLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
496-696 |
1.74e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 89.71 E-value: 1.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQSDMNFDVLT 572
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 653 VWN-LLKYR-KANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10070 203 MQDeLVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
501-696 |
1.79e-18 |
|
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: 89.00 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMFEARKmIGICPQSDMNFDVLTVEEN 576
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRR-IGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LsiLASVKGIPANNiiqevQKVLLD-----LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:COG4148 98 L--LYGRKRAPRAE-----RRISFDevvelLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 652 ivwNLLKY-----RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4148 171 ---EILPYlerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1286-1515 |
1.85e-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: 91.02 E-value: 1.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1286 EKPAIMVYNLHKEYddkkdFLHSRKTTKvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIF--LGD-- 1361
Cdd:TIGR03269 276 GEPIIKVRNVSKRY-----ISVDRGVVK-AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDew 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1362 ---YGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHF-EIYGAVKGMSSGDMKEVISRITKALD---LKEHLQKTVKKLP 1434
Cdd:TIGR03269 350 vdmTKPGPDGRGRAKRYIGILHQEYDLYPHRTVLDNLtEAIGLELPDELARMKAVITLKMVGFDeekAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1435 AGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
.
gi 27368659 1515 G 1515
Cdd:TIGR03269 510 G 510
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
474-642 |
2.40e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 90.51 E-value: 2.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAYRKKneTVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSeidemf 552
Cdd:COG0488 312 GKKVLELEGLSKSYGDK--TL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSG--TVkLGETVK------ 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 earkmIGICPQSDMNFDvltveENLSILASVKGIPANNIIQEVQKVLLDL----DMQaikDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG0488 380 -----IGYFDQHQEELD-----PDKTVLDELRDGAPGGTEQEVRGYLGRFlfsgDDA---FKPVGVLSGGEKARLALAKL 446
|
170
....*....|....
gi 27368659 629 VLGNPKILLLDEPT 642
Cdd:COG0488 447 LLSPPNVLLLDEPT 460
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
2.92e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 86.24 E-value: 2.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:COG1117 11 KIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeilldgEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 547 EIdemfEARKMIGicpqsdMNFDV-----LTVEENLSILASVKGIPANNIIQE-VQKVLLdldmQA-----IKDN---QA 612
Cdd:COG1117 87 VV----ELRRRVG------MVFQKpnpfpKSIYDNVAYGLRLHGIKSKSELDEiVEESLR----KAalwdeVKDRlkkSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 613 KKLSGGQKRKLSL--GIAVlgNPKILLLDEPTAGMDPCSRHIVWNL---LKyrkaNRVT-VFSTHFMDEADILADRKAVI 686
Cdd:COG1117 153 LGLSGGQQQRLCIarALAV--EPEVLLMDEPTSALDPISTAKIEELileLK----KDYTiVIVTHNMQQAARVSDYTAFF 226
|
....*
gi 27368659 687 SQGML 691
Cdd:COG1117 227 YLGEL 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1290-1510 |
3.32e-18 |
|
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: 85.70 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:cd03256 1 IEVENLSKTYPNGKKALKD----------VSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKC---MGYCPQTNPLWPDIT---------LQEHfeiyGAVKGMSSGDMKEVISRITKALD---LKEHLQKTVKKLP 1434
Cdd:cd03256 71 KALRQLrrqIGMIFQQFNLIERLSvlenvlsgrLGRR----STWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1435 AGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03256 147 GGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1294-1520 |
3.38e-18 |
|
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: 85.31 E-value: 3.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINIL-----VGDVEPTSGKIFL-GDYGSHSN 1367
Cdd:cd03260 5 DLNVYYGDKH-----------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLdGKDIYDLD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKC-MGYCPQT-NPLwpDITLQEHFEiYGaVKGMSSGDMKEVISRITKALDlKEHLQKTVK------KLPAGIKR 1439
Cdd:cd03260 74 VDVLELRRrVGMVFQKpNPF--PGSIYDNVA-YG-LRLHGIKLKEELDERVEEALR-KAALWDEVKdrlhalGLSGGQQQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1440 KLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAfkNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 27368659 1520 L 1520
Cdd:cd03260 227 I 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1314-1517 |
3.74e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.70 E-value: 3.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsneDDESTKcmgycpQTNP--------- 1384
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILI---------DGKPVR------IRSPrdaialgig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1385 -------LWPDITLQEHFeIYGAVKGMS-SGDMKEVISRIT---KALDLKEHLQKTVKKLPAGIKRKL----CfalsMLG 1449
Cdd:COG3845 84 mvhqhfmLVPNLTVAENI-VLGLEPTKGgRLDRKAARARIRelsERYGLDVDPDAKVEDLSVGEQQRVeilkA----LYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLrcIGTV 1517
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGTV 223
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
478-695 |
3.90e-18 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 88.16 E-value: 3.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 638 LDEPTAGMDPCSR---HIVWNLLkYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK11000 157 LDEPLSNLDAALRvqmRIEISRL-HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1301-1520 |
4.16e-18 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 87.85 E-value: 4.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1301 DKKDFLHSRKTTKVATKYV-----SFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshSNED--DEST 1373
Cdd:PRK11432 2 TQKNFVVLKNITKRFGSNTvidnlNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFI------DGEDvtHRSI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 K----CMGYcpQTNPLWPDITLQEHFEiYG-AVKGMSSGDMKEvisRITKAL---DLKEHLQKTVKKLPAGIKRKLCFAL 1445
Cdd:PRK11432 76 QqrdiCMVF--QSYALFPHMSLGENVG-YGlKMLGVPKEERKQ---RVKEALelvDLAGFEDRYVDQISGGQQQRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1446 SMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK11432 150 ALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-696 |
6.18e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.13 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 476 EAIRISGIQKAYR------------------KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF 537
Cdd:COG1134 3 SMIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 538 ASIYGhRVSEIDEMfearkMIGICPQsdmnfdvLTVEENLSILASVKGIPAnniiQEVQKVlldldMQAIK--------- 608
Cdd:COG1134 83 VEVNG-RVSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSR----KEIDEK-----FDEIVefaelgdfi 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 609 DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-----CSRHIvwnlLKYRKANRVTVFSTHFMDEADILADRK 683
Cdd:COG1134 141 DQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkCLARI----RELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|...
gi 27368659 684 AVISQGMLKCVGS 696
Cdd:COG1134 217 IWLEKGRLVMDGD 229
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1288-1515 |
7.30e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.58 E-value: 7.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1288 PAIMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHS 1366
Cdd:PRK11607 18 PLLEIRNLTKSFDGQH-----------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 NEDDESTKCMGycpQTNPLWPDITLQEHFEIYGAVKGMSSGdmkEVISRITKALDLKeHLQKTVKKLP----AGIKRKLC 1442
Cdd:PRK11607 87 PPYQRPINMMF---QSYALFPHMTVEQNIAFGLKQDKLPKA---EIASRVNEMLGLV-HMQEFAKRKPhqlsGGQRQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1443 FALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
496-689 |
1.00e-17 |
|
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: 82.87 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEA--------RKMIGICPQsd 565
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAgiayvpedRKREGLVLD-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 mnfdvLTVEENLSILASvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03215 93 -----LSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 646 DPCSRHIVWNLL-KYRKANR-VTVFSTHfMDEADILADRKAVISQG 689
Cdd:cd03215 136 DVGAKAEIYRLIrELADAGKaVLLISSE-LDELLGLCDRILVMYEG 180
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
486-691 |
1.17e-17 |
|
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: 83.67 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 486 AYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQSD 565
Cdd:cd03248 20 AYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 MNFdVLTVEENLS----------ILASVKGIPANNIIQEVQKvlldlDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03248 98 VLF-ARSLQDNIAyglqscsfecVKEAAQKAHAHSFISELAS-----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
507-646 |
1.34e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 507 GQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR-----KMIGICPQSDMNFDVLTVEENLSILA 581
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE--EARaklraKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 582 SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1290-1524 |
1.94e-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: 87.55 E-value: 1.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVG--DVEPTSGKIFL-------- 1359
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-----------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYhvalcekc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1360 GDYGSHSNEDDESTKCMG-YCPQTNPLW-PD------------ITLQEHFEIYG-------AVKGMSSGDMKEVISrITK 1418
Cdd:TIGR03269 70 GYVERPSKVGEPCPVCGGtLEPEEVDFWnLSdklrrrirkriaIMLQRTFALYGddtvldnVLEALEEIGYEGKEA-VGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1419 ALDLKEHLQ------KTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHY 1492
Cdd:TIGR03269 149 AVDLIEMVQlshritHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHW 228
|
250 260 270
....*....|....*....|....*....|..
gi 27368659 1493 MEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:TIGR03269 229 PEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
477-682 |
2.00e-17 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 83.25 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR- 555
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE--DARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 ----KMIGICPQSDMNFDVLTVEENlsilasvkgipanniiqevqkVLLDLDMQAIKDNQA------------------- 612
Cdd:COG4181 86 rlraRHVGFVFQSFQLLPTLTALEN---------------------VMLPLELAGRRDARArarallervglghrldhyp 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVT-VFSTHfmDEAdiLADR 682
Cdd:COG4181 145 AQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTlVLVTH--DPA--LAAR 212
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1319-1506 |
3.06e-17 |
|
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: 86.96 E-value: 3.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYG-SHSNEDDESTKCmGYCPQTnPLWPDITLQEhfEI 1397
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPlADADADSWRDQI-AWVPQH-PFLFAGTIAE--NI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGAVKGMSSGDMKEVISRiTKALDLkehlqktVKKLPAGI---------------KRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:TIGR02857 417 RLARPDASDAEIREALER-AGLDEF-------VAALPQGLdtpigeggaglsggqAQRLALARAFLRDAPLLLLDEPTAH 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27368659 1463 MDPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAEAvCDRVAIM 1506
Cdd:TIGR02857 489 LDAETEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
493-701 |
3.49e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 83.70 E-value: 3.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-SDMNFDVL 571
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQnPDDQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 572 TVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK13652 95 TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVK 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 652 ivwNLLKYRKANRVT-----VFSTHFMDEADILADRKAVISQGMLKCVGS--SIFLK 701
Cdd:PRK13652 175 ---ELIDFLNDLPETygmtvIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQ 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1315-1566 |
3.92e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1315 ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYG-SHSNEDDESTKCMGYCPQTNPLWPDITLQE 1393
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINyNKLDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEI----YGAVKGMSSGD---MKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPR 1466
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1467 AKQHMWrAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHlkskfgkgyfleiklkdwIENLEIDRL 1546
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSD------------------VSNDDIVRL 240
|
250 260
....*....|....*....|..
gi 27368659 1547 Q--REIQYIFPnaSRQESFSSI 1566
Cdd:PRK09700 241 MvgRELQNRFN--AMKENVSNL 260
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
477-677 |
3.92e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.87 E-value: 3.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidEMFEARK 556
Cdd:NF033858 1 VARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG------DMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQ-SDM------N-FDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:NF033858 71 RRAVCPRiAYMpqglgkNlYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCA 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANR----VTVfSTHFMDEAD 677
Cdd:NF033858 151 LIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmsVLV-ATAYMEEAE 202
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
497-695 |
4.20e-17 |
|
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: 86.63 E-value: 4.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFEarKMIGICPQSDMNFDVlTVEE 575
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDrETFG--KHIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLS----ILASVKGIPANNIIQeVQKVLLDLDM---QAIKDNQAKkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:TIGR01842 411 NIArfgeNADPEKIIEAAKLAG-VHELILRLPDgydTVIGPGGAT-LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27368659 649 SRHIVWNLLKYRKANRVTV-FSTHfMDEADILADRKAVISQGMLKCVG 695
Cdd:TIGR01842 489 GEQALANAIKALKARGITVvVITH-RPSLLGCVDKILVLQDGRIARFG 535
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
476-696 |
4.52e-17 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 82.90 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 476 EAIRISGIqkAYRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMfe 553
Cdd:PRK13548 1 AMLEARNL--SVRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 554 ARkMIGICPQ-SDMNFDvLTVEE----NLSILASVKGiPANNIIQEvqkVLLDLDMQAIKDNQAKKLSGGQKRKLSLgiA 628
Cdd:PRK13548 75 AR-RRAVLPQhSSLSFP-FTVEEvvamGRAPHGLSRA-EDDALVAA---ALAQVDLAHLAGRDYPQLSGGEQQRVQL--A 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 629 -VL-------GNPKILLLDEPTAGMDPCSRHIVWNLLKYR-KANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13548 147 rVLaqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVlHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
85-416 |
6.04e-17 |
|
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: 84.36 E-value: 6.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 85 TNTTSSVMQRVSTDhlPDVLVTEEYASEKELLASSLSKPSNFVGVVFKDvmsYELRFFPDMVPVSSVYMDSrAGCSKSCD 164
Cdd:pfam12698 42 SSLSRQLVRALEAS--PTVNLVQYVDSEEEAKEALKNGKIDGLLVIPKG---FSKDLLKGESATVTVYINS-SNLLVSKL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 165 AAQYWSSgFTALQASIDAAIIQLKTNVSLWRELESTkavimgeAAVVEIDTFPRGVILIYLVIAFSPFGYFLAIHIVAEK 244
Cdd:pfam12698 116 ILNALQS-LLQQLNASALVLLLEALSTSAPIPVEST-------PLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVEEK 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 245 EKRLKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATASSlFPQSSSIVIFLLFFLYGLSSVFFALMLTPLFKKS 324
Cdd:pfam12698 188 ESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIG-IPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 325 KHVGVVEFFVTVVFGFVGLLIVLVESFPRSLVWLFSPLCQCAFLIGIAQVMhledfnegalfssLTEGPYPLIITLTMLA 404
Cdd:pfam12698 267 EDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLRLI-------------YGDSLWEIAPSLIILL 333
|
330
....*....|..
gi 27368659 405 LDSVFYALLAVY 416
Cdd:pfam12698 334 LFAVVLLLLALL 345
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
494-697 |
6.79e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.27 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC-----PPSDGFASIYGHRVSEIDeMFEARKMIgicpqsDMNF 568
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMD-VIELRRRV------QMVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQ------------AKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK14247 89 QIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQlwdevkdrldapAGKLSGGQQQRLCIARALAFQPEVL 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK14247 169 LADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1319-1511 |
7.96e-17 |
|
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: 79.95 E-value: 7.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQtnplwpDITLqehFeiy 1398
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ------DDEL---F--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 gavkgmsSGDMKEVIsritkaldlkehlqktvkkLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRtA 1478
Cdd:cd03246 89 -------SGSIAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA-A 141
|
170 180 190
....*....|....*....|....*....|...
gi 27368659 1479 FKNKKRAALLTTHYMEEAEAvCDRVAIMVSGQL 1511
Cdd:cd03246 142 LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
495-647 |
1.07e-16 |
|
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: 80.10 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVE 574
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLK-PELSAL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 575 ENLSILASVKGIPANNIIQEVQKVLLDldmqAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:TIGR01189 92 ENLHFWAAIHGGAQRTIEDALAAVGLT----GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
501-695 |
1.36e-16 |
|
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: 80.29 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQSDMNFDVLTVEENLSiL 580
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIG-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 581 ASVKGIPANNIIQE-VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY 659
Cdd:TIGR01277 94 GLHPGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 27368659 660 --RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:TIGR01277 174 lcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
496-684 |
1.60e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 1.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPP--SDGFASIYGHRV--SEIDEMfEARKMIGICPQSDMNF 568
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyaPDVDPV-EVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVlTVEENLSILASVKGIPANniIQEV------QKVLLDLDMQAIKDNqAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGD--MDELverslrQAALWDEVKDKLKQS-GLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-646 |
1.95e-16 |
|
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: 79.61 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 483 IQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGHrVS----EIDEMFE-ARKM 557
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGD-IHyngiPYKEFAEkYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQSDMNFDVLTVEENLSILASVKGipaNNIIqevqkvlldldmqaikdnqaKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG---NEFV--------------------RGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 27368659 638 LDEPTAGMD 646
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1290-1520 |
2.19e-16 |
|
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: 80.32 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFLHsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSN 1367
Cdd:cd03258 2 IELKNVSKVFGDTGGKVT-------ALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 -EDDESTKCMGYCPQTNPLWPDITLQEH----FEIYGAvkgmssgDMKEVISRITKAL---DLKEHLQKTVKKLPAGIKR 1439
Cdd:cd03258 75 kELRKARRRIGMIFQHFNLLSSRTVFENvalpLEIAGV-------PKAEIEERVLELLelvGLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1440 KLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAfkNKKR--AALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTV 1517
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDI--NRELglTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTV 225
|
...
gi 27368659 1518 QHL 1520
Cdd:cd03258 226 EEV 228
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-703 |
2.36e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 80.86 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAYRKKNETVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP------PSDGFASIYGHRVSE 547
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 548 IDEMfEARKMIGICPQSDMNFDVLTVEENLSILASVKGIPANNIIQEV-----QKVLLDLDMQAIKDNQAKKLSGGQKRK 622
Cdd:PRK14246 83 IDAI-KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIveeclRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS--IFL 700
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSneIFT 241
|
...
gi 27368659 701 KSK 703
Cdd:PRK14246 242 SPK 244
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
494-691 |
2.37e-16 |
|
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: 84.38 E-value: 2.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTV 573
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-TLASLRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSIlasvkGIPANNIIQEVQKVLLDLDMQAIKDN-----------QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:TIGR02203 423 ANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAIARALLKDAPILILDEAT 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27368659 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:TIGR02203 498 SALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-682 |
2.91e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.81 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-------SEIDEMFearkmigicPqsdmnf 568
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqrSEVPDSL---------P------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 dvLTVEENLSI----LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:NF040873 72 --LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 645 MDPCSRHIVWNLLKYRKANRVTVF-STHFMDEAdILADR 682
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVvVTHDLELV-RRADP 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
461-689 |
3.62e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 84.11 E-value: 3.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 461 LNEIVE-PVSSEFIGKE-------AIRISGIQKAYrkKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:PRK11160 314 INEITEqKPEVTFPTTStaaadqvSLTLNNVSFTY--PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 533 PSDGFASIYGHRVSEIDEMfEARKMIGICPQSdmnFDVL--TVEENLSILASvkgiPANN--IIQEVQKVLLDLDMQAIK 608
Cdd:PRK11160 392 PQQGEILLNGQPIADYSEA-ALRQAISVVSQR---VHLFsaTLRDNLLLAAP----NASDeaLIEVLQQVGLEKLLEDDK 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 609 DNQA------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSRHIVWNLLKYRKaNRVTVFSTH---FMDEAD- 677
Cdd:PRK11160 464 GLNAwlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeTERQILELLAEHAQ-NKTVLMITHrltGLEQFDr 542
|
250
....*....|...
gi 27368659 678 -ILADRKAVISQG 689
Cdd:PRK11160 543 iCVMDNGQIIEQG 555
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1319-1464 |
3.70e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.16 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygshsnEDDESTKcMGYCPQTnpLWPDITLQEHFEIY 1398
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLR-IGYVPQK--LYLDTTLPLTVNRF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1399 GAVK-GMSSGDMKEVISRITKAldlkeHL-QKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PRK09544 90 LRLRpGTKKEDILPALKRVQAG-----HLiDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1319-1491 |
4.67e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.76 E-value: 4.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEStkcMGYCPQTNPLWPDITLQEHFEIY 1398
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEA---CHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMSSGDMKEVISRItkALDLKEHLQktVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDpRAKQHMWRAIRTA 1478
Cdd:PRK13539 98 AAFLGGEELDIAAALEAV--GLAPLAHLP--FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD-AAAVALFAELIRA 172
|
170
....*....|...
gi 27368659 1479 FKNKKRAALLTTH 1491
Cdd:PRK13539 173 HLAQGGIVIAATH 185
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
490-658 |
5.00e-16 |
|
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: 78.05 E-value: 5.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcppsdgfASIYGHRVSEI-------DEMFeaRKMIGICP 562
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--------RKTAGVITGEIlingrplDKNF--QRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 563 QSDMNFDVLTVEENLSILASVKGipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:cd03232 86 QQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170
....*....|....*.
gi 27368659 643 AGMDPCSRHIVWNLLK 658
Cdd:cd03232 137 SGLDSQAAYNIVRFLK 152
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1319-1511 |
5.68e-16 |
|
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: 78.79 E-value: 5.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQtnplwpDITLqehfeIY 1398
Cdd:cd03245 23 VSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ------DVTL-----FY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVK-----GMSSGDMKEVI--SRITKALDLkehlqktVKKLPAGIKRKLC---FALS------------MLGNPQVTLL 1456
Cdd:cd03245 92 GTLRdnitlGAPLADDERILraAELAGVTDF-------VNKHPNGLDLQIGergRGLSggqrqavalaraLLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1457 DEPSTGMDPRAKQHMWRAIRTAFKNKkrAALLTTHYMeEAEAVCDRVAIMVSGQL 1511
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1319-1511 |
5.69e-16 |
|
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: 78.85 E-value: 5.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEptSGKIFLGD--YGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFe 1396
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQilFNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVKGMSSGDMKEVISRITKALDLKE-HLQ----KTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:cd03234 103 TYTAILRLPRKSSDAIRKKRVEDVLLRDlALTriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1472 WRAIR-TAFKNkkRAALLTTHY-MEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03234 183 VSTLSqLARRN--RIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1294-1482 |
5.78e-16 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 78.81 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKDFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEST 1373
Cdd:cd03254 7 NVNFSYDEKKPVLKD----------INFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQTNPLWPDiTLQEHFEIygavkGMSSGDMKEVI--SRITKALDLKEHLQK---TV-----KKLPAGIKRKLCF 1443
Cdd:cd03254 77 SMIGVVLQDTFLFSG-TIMENIRL-----GRPNATDEEVIeaAKEAGAHDFIMKLPNgydTVlgengGNLSQGERQLLAI 150
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1444 ALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNK 1482
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR 189
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
478-696 |
9.53e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 9.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNE-TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfASIYGH-----RVSEIDEM 551
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-QTIVGDyaipaNLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 FEARKMIGIC---PQSDMNFDvlTVEENLSILASVKGIPANNIIQEVQKVLldlDMQAIKDNQAKK----LSGGQKRKLS 624
Cdd:PRK13645 86 KRLRKEIGLVfqfPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELL---KLVQLPEDYVKRspfeLSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL---LKYRKANRVtVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRI-IMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-692 |
9.89e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.32 E-value: 9.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 485 KAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR---KMIGIC 561
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 562 PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 642 TAGMDPCSRHIVWNLLKYRKANRVTVF--STHFMDEADILaDRKAVISQGMLK 692
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
475-671 |
1.01e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 79.16 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 475 KEAIRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfea 554
Cdd:PRK15056 4 QAGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGICPQS---DMNFDVLtVEEnlSILASVKG------IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL 625
Cdd:PRK15056 77 KNLVAYVPQSeevDWSFPVL-VED--VVMMGRYGhmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTH 671
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLReLRDEGKTMLVSTH 200
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
487-689 |
1.18e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.90 E-value: 1.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE-MFEARKMIGICPQ-- 563
Cdd:PRK13638 9 FRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRgLLALRQQVATVFQdp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 564 ------SDMNFDVLTVEENLsilasvkGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK13638 87 eqqifyTDIDSDIAFSLRNL-------GVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVtVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRriVAQGNHV-IISSHDIDLIYEISDAVYVLRQG 212
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1303-1516 |
1.27e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 80.85 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDE----STKCMGY 1378
Cdd:PRK10070 31 KEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1379 CPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDE 1458
Cdd:PRK10070 111 VFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDE 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1459 PSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK10070 191 AFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
458-710 |
1.32e-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: 82.48 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 458 NISLNEiVEPVSSEFIGK----EAIRISG---IQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL 530
Cdd:TIGR01193 445 NNRLNE-VYLVDSEFINKkkrtELNNLNGdivINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGF 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 531 CPPSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVEENLsILASVKGIPANNIIQEVQKVLLDLDMQAIK-- 608
Cdd:TIGR01193 524 FQARSGEILLNGFSLKDIDRH-TLRQFINYLPQEPYIFSG-SILENL-LLGAKENVSQDEIWAACEIAEIKDDIENMPlg 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 609 -----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH-IVWNLLKYRkaNRVTVFSTHFMDEADiLADR 682
Cdd:TIGR01193 601 yqtelSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKkIVNNLLNLQ--DKTIIFVAHRLSVAK-QSDK 677
|
250 260
....*....|....*....|....*...
gi 27368659 683 KAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:TIGR01193 678 IIVLDHGKIIEQGSHDELLDRNGFYASL 705
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1301-1568 |
1.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.28 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1301 DKKDFLHSRKT--TKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSN-----EDDEST 1373
Cdd:PRK13645 10 DNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANlkkikEVKRLR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQtnplWPDITL-QEHFEIYGAVKGMSSG-DMKEVISRITKALDL----KEHLQKTVKKLPAGIKRKLCFA--L 1445
Cdd:PRK13645 90 KEIGLVFQ----FPEYQLfQETIEKDIAFGPVNLGeNKQEAYKKVPELLKLvqlpEDYVKRSPFELSGGQKRRVALAgiI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1446 SMLGNPQVtlLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTV------QH 1519
Cdd:PRK13645 166 AMDGNTLV--LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQE 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1520 LKSKFG----KGYFLEIKLKdwieNLEIDRLQREIQYIfpnasrqESFSSILA 1568
Cdd:PRK13645 244 LLTKIEidppKLYQLMYKLK----NKGIDLLNKNIRTI-------EEFAKELA 285
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1290-1511 |
1.44e-15 |
|
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: 77.18 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD--YGSHSN 1367
Cdd:cd03262 1 IEIKNLHKSFGDFH-----------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1368 EDDESTKCMGYCPQTNPLWPDITLQEHfeIYGA---VKGMSSgdmKEVISRITKALD---LKEHLQKTVKKLPAGIKRKL 1441
Cdd:cd03262 70 NINELRQKVGMVFQQFNLFPHLTVLEN--ITLApikVKGMSK---AEAEERALELLEkvgLADKADAYPAQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1442 CFALSMLGNPQVTLLDEPSTGMDPR------------AKQHMwrairtafknkkrAALLTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:cd03262 145 AIARALAMNPKVMLFDEPTSALDPElvgevldvmkdlAEEGM-------------TMVVVTHEMGFAREVADRVIFMDDG 211
|
..
gi 27368659 1510 QL 1511
Cdd:cd03262 212 RI 213
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1321-1491 |
2.07e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 76.81 E-value: 2.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1321 FCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEIYGA 1400
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---QIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHFLCG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 VKGMSSgdmKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIrTAFK 1480
Cdd:PRK13543 109 LHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI-SAHL 184
|
170
....*....|.
gi 27368659 1481 NKKRAALLTTH 1491
Cdd:PRK13543 185 RGGGAALVTTH 195
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1311-1516 |
2.12e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 78.59 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1311 TTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGShSNEDD--ESTKCMGYCPQTnplwPD 1388
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDT-SDEENlwDIRNKAGMVFQN----PD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1389 ----ITLQEHFEIYGAVK-GMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFA--LSMlgNPQVTLLDEPST 1461
Cdd:PRK13633 96 nqivATIVEEDVAFGPENlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAgiLAM--RPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1462 GMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1290-1511 |
2.12e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 75.81 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:cd03247 1 LSINNVSFSYPEQE---------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DEStKCMGYCPQTNPLWpDITLQEHFEiygavkgmssgdmkevisritkaldlkehlqktvKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03247 72 ALS-SLISVLNQRPYLF-DTTLRNNLG----------------------------------RRFSGGERQRLALARILLQ 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKkrAALLTTHYMEEAEAVcDRVAIMVSGQL 1511
Cdd:cd03247 116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1290-1527 |
2.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDflhsrkttKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNE 1368
Cdd:PRK13650 5 IEVKNLTFKYKEDQE--------KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1369 DDESTKcMGYCPQTnplwPD-----ITLQEHFEIYGAVKGMSSGDMKEvisRITKALDL---KEHLQKTVKKLPAGIKRK 1440
Cdd:PRK13650 77 WDIRHK-IGMVFQN----PDnqfvgATVEDDVAFGLENKGIPHEEMKE---RVNEALELvgmQDFKEREPARLSGGQKQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1441 LCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK13650 149 VAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL 227
|
....*..
gi 27368659 1521 kskFGKG 1527
Cdd:PRK13650 228 ---FSRG 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1311-1511 |
2.73e-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: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1311 TTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDESTKCMGYCPqtnplwpdi 1389
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdGKPVTRRSPRDAIRAGIAYVP--------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1390 tlQEHFEiYGAVKGMSsgdmkeVISRITkaldLKEHL-----QktvkklpagikrKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:cd03215 82 --EDRKR-EGLVLDLS------VAENIA----LSSLLsggnqQ------------KVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 1465 PRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03215 137 VGAKAEIYRLIR-ELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1292-1528 |
2.86e-15 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 76.03 E-value: 2.86e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKdFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVG--DVEPTSGKIFLGDYGSHSNED 1369
Cdd:cd03217 3 IKDLHVSVGGKE-ILKG----------VNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKC-MGYCPQTNPLWPDITLqEHFeIYGAVKGMSSGDMKEVisritkaldlkEHLQktvkklpagikrklcfalSML 1448
Cdd:cd03217 72 EERARLgIFLAFQYPPEIPGVKN-ADF-LRYVNEGFSGGEKKRN-----------EILQ------------------LLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1449 GNPQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAV-CDRVAIMVSGQLRCIGTVQHLKSKFGKG 1527
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINK-LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
.
gi 27368659 1528 Y 1528
Cdd:cd03217 200 Y 200
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
496-689 |
2.90e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.43 E-value: 2.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfeARKmiGICPQSDMNFDVLTVEE 575
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AER--GVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 656 LL--KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11248 170 LLlkLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
478-696 |
3.07e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 77.36 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeideMFEARKM 557
Cdd:PRK11231 3 LRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----MLSSRQL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 ---IGICPQsdmnfdVLTVEENLSI--LASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLS 624
Cdd:PRK11231 75 arrLALLPQ------HHLTPEGITVreLVAYGRSPWLSLWgrlsaednARVNQAMEQTRINHLADRRLTDLSGGQRQRAF 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11231 149 LAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
479-689 |
3.56e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIDEMFEARk 556
Cdd:PRK11288 6 SFDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 mIGICPQSDMNFDVLTVEENLSI--LASVKG-IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK11288 81 -VAIIYQELHLVPEMTVAENLYLgqLPHKGGiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 634 KILLLDEPTAGMDpcSRHIVwNLLK----YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11288 160 RVIAFDEPTSSLS--AREIE-QLFRvireLRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1315-1544 |
3.71e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 77.97 E-value: 3.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1315 ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG----DYGSHSNEDDESTKCMGYCPQTNPLWPDIT 1390
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKLRESVGMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1391 LQEhfEIYGAVK-GMSSGDMKEVISRITKALDLkEHLQ-KTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK 1468
Cdd:PRK13636 101 YQD--VSFGAVNlKLPEDEVRKRVDNALKRTGI-EHLKdKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1469 QHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLkskFGK--------------GYFLEI-K 1533
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---FAEkemlrkvnlrlpriGHLMEIlK 254
|
250
....*....|.
gi 27368659 1534 LKDWIENLEID 1544
Cdd:PRK13636 255 EKDGFVFDELD 265
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
495-695 |
4.17e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.19 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPPS--DGFASIYGHRVSEID-EMFEARKMIGICPQSDMNF 568
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIYSPDvDPIEVRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLSILASVKGI--PANNIIQEVQKVLLDLDM-QAIKD---NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDrlnDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1294-1520 |
4.19e-15 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 78.58 E-value: 4.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsnED--DE 1371
Cdd:COG3839 8 NVSKSYGGV-----------EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG------RDvtDL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1372 STKC--MGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAG----------IKR 1439
Cdd:COG3839 71 PPKDrnIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvalgraLVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1440 klcfalsmlgNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:COG3839 151 ----------EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEE 220
|
.
gi 27368659 1520 L 1520
Cdd:COG3839 221 L 221
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1319-1518 |
5.79e-15 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 76.73 E-value: 5.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEIY 1398
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVVAMG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFA--LSML----GNPQVTLLDEPSTGMDPRAKQHMW 1472
Cdd:PRK13548 101 RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvLAQLwepdGPPRWLLLDEPTSALDLAHQHHVL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1473 RAIRTAFKNKKRAAL-------LTTHYmeeaeavCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK13548 181 RLARQLAHERGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1323-1510 |
6.08e-15 |
|
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: 76.29 E-value: 6.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygshsnedDESTKCMGYCPQTnpLWPDITLQEHFEIYGAVK 1402
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI------------EIELDTVSYKPQY--IKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1403 GMssGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNK 1482
Cdd:cd03237 88 DF--YTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENN 165
|
170 180 190
....*....|....*....|....*....|
gi 27368659 1483 KRAALLTTH--YMeeAEAVCDRVaIMVSGQ 1510
Cdd:cd03237 166 EKTAFVVEHdiIM--IDYLADRL-IVFEGE 192
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1286-1520 |
6.40e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 76.98 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1286 EKPAIMVYNLHKEYDDkkdflhsrkTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGSH 1365
Cdd:PRK13635 2 KEEIIRVEHISFRYPD---------AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVG--GMV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1366 SNEDD--ESTKCMGYCPQTnplwPD-----ITLQEHFEIYGAVKGMSSGDMkevISRITKALDL---KEHLQKTVKKLPA 1435
Cdd:PRK13635 71 LSEETvwDVRRQVGMVFQN----PDnqfvgATVQDDVAFGLENIGVPREEM---VERVDQALRQvgmEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1436 GIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLT-THYMEEAeAVCDRVAIMVSGQLRCI 1514
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ-LKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEE 221
|
....*.
gi 27368659 1515 GTVQHL 1520
Cdd:PRK13635 222 GTPEEI 227
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1313-1551 |
8.34e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 76.98 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKcmgycpqtnPLWPD--IT 1390
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLK---------PLRKKvgIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1391 LQ--EH--FE-------IYGAVK-GMSSGDMKEVISRITKALDLKEH-LQKTVKKLPAGIKRKLCFA--LSMlgNPQVTL 1455
Cdd:PRK13634 91 FQfpEHqlFEetvekdiCFGPMNfGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAgvLAM--EPEVLV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1456 LDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKfgkgyfleiklK 1535
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD-----------P 237
|
250 260
....*....|....*....|.
gi 27368659 1536 DWIENLEID-----RLQREIQ 1551
Cdd:PRK13634 238 DELEAIGLDlpetvKFKRALE 258
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
476-682 |
8.60e-15 |
|
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: 75.55 E-value: 8.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 476 EAIRISGIQKAYRKKNE---TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSEID-- 549
Cdd:COG4778 3 TLLEVENLSKTFTLHLQggkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--SIlVRHDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 550 -----EMFEARK-MIGICPQsdmnFdvLTVeenlsilasVKGIPANNIiqeVQKVLLDLDM-QAIKDNQAKKL------- 615
Cdd:COG4778 81 qasprEILALRRrTIGYVSQ----F--LRV---------IPRVSALDV---VAEPLLERGVdREEARARARELlarlnlp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 616 -----------SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSThFMDEA--DILADR 682
Cdd:COG4778 143 erlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADR 221
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
500-689 |
9.03e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 75.56 E-value: 9.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 500 LSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQSDMNFDVLTVEENL 577
Cdd:COG3840 16 LRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTALPPAERPVSMLFQENNLFPHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 578 SIlasvkGIPAN---------NIIQEVQKVLLDlDMQAIKDNQakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:COG3840 93 GL-----GLRPGlkltaeqraQVEQALERVGLA-GLLDRLPGQ---LSGGQRQRVALARCLVRKRPILLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 649 SRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG3840 164 LRQEMLDLVDelCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
489-677 |
9.81e-15 |
|
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: 74.81 E-value: 9.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSD--M 566
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NfdvLTVEENlsILAsvkGIPANNiiQEVQKVL----LDLDMQAIKD-----------NqakkLSGGQKRKLSLGIAVLG 631
Cdd:cd03250 79 N---GTIREN--ILF---GKPFDE--ERYEKVIkacaLEPDLEILPDgdlteigekgiN----LSGGQKQRISLARAVYS 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 632 NPKILLLDEPTAGMDP-CSRHIVWN-LLKYRKANRVTVFSTH---FMDEAD 677
Cdd:cd03250 145 DADIYLLDDPLSAVDAhVGRHIFENcILGLLLNNKTRILVTHqlqLLPHAD 195
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1290-1503 |
1.04e-14 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 72.87 E-value: 1.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFlhsrkttkvatKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdygshsned 1369
Cdd:cd03221 1 IELENLSKTYGGKLLL-----------KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG--------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 deSTKCMGYCPQtnplwpditlqehfeiygavkgMSSGDmkevisritkaldlkehlqktvkklpagiKRKLCFALSMLG 1449
Cdd:cd03221 61 --STVKIGYFEQ----------------------LSGGE-----------------------------KMRLALAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQhmwrAIRTAFKNKKRAALLTTHYMEEAEAVCDRV 1503
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIE----ALEEALKEYPGTVILVSHDRYFLDQVATKI 137
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
500-646 |
1.17e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVEENLSI 579
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI-ARGLLYLGHAPGIK-TTLSVLENLRF 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 580 LAsvkgipANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03231 97 WH------ADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1323-1511 |
1.25e-14 |
|
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: 74.45 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHsnedDESTKCMGYCPQTNPLWPDITLQEHFEIyGA 1400
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvDVTAA----PPADRPVSMLFQENNLFAHLTVEQNVGL-GL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 VKGMS-SGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAF 1479
Cdd:cd03298 96 SPGLKlTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 1480 KNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03298 176 AETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1313-1570 |
1.28e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 76.36 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEST----KCMGYCPQtnplWPD 1388
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1389 ITLQE---HFEIYGAVK--GMssgDMKEVISRITKAL-DL---KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEP 1459
Cdd:PRK13646 96 SQLFEdtvEREIIFGPKnfKM---NLDEVKNYAHRLLmDLgfsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1460 STGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLkskFGKGYfleiKLKDW-I 1538
Cdd:PRK13646 173 TAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKK----KLADWhI 245
|
250 260 270
....*....|....*....|....*....|....*..
gi 27368659 1539 ENLEIDRLQREI----QYIFPN-ASRQESFSSIlaYK 1570
Cdd:PRK13646 246 GLPEIVQLQYDFeqkyQTKLKDiALTEEEFVSL--YK 280
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
477-689 |
1.42e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 75.56 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIyghRVSEID------- 549
Cdd:PRK11264 3 AIEVKNLVKKF--HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TI---RVGDITidtarsl 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 550 -----EMFEARKMIGICPQSDMNFDVLTVEENlsILAS---VKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKR 621
Cdd:PRK11264 74 sqqkgLIRQLRQHVGFVFQNFNLFPHRTVLEN--IIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPcsrHIVWNLLKYRKA----NRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
477-696 |
1.47e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.19 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARK 556
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQsdmNFDV---LTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK11650 77 DIAMVFQ---NYALyphMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 634 KILLLDEPTAGMDPcsrhivwnllKYRKANRV------------TVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11650 154 AVFLFDEPLSNLDA----------KLRVQMRLeiqrlhrrlkttSLYVTHDQVEAMTLADRVVVMNGGVAEQIGT 218
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1520 |
1.64e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 75.61 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDdESTKCMGYCPQ 1381
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIrGEPITKENIR-EVRKFVGLVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1382 TnplwPD-----ITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLL 1456
Cdd:PRK13652 86 N----PDdqifsPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1457 DEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1312-1518 |
2.19e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1312 TKVATKyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDDEStkcMGYCPQTNPLWPDIT 1390
Cdd:PRK10851 15 TQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTDVSRLHARDRK---VGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1391 LQEHFEIygavkGMS------SGDMKEVISRITKALDLK--EHL-QKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:PRK10851 91 VFDNIAF-----GLTvlprreRPNAAAIKAKVTQLLEMVqlAHLaDRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1462 GMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1309-1516 |
2.24e-14 |
|
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: 74.07 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1309 RKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgshsnedDEST-------KCMGYCPQ 1381
Cdd:cd03244 13 RPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV-------DISKiglhdlrSRISIIPQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1382 tNPLWPDITLQEH---------FEIYGAVKGMSsgdMKEVISRITKALDLKEHLQKtvKKLPAGIKRKLCFALSMLGNPQ 1452
Cdd:cd03244 86 -DPVLFSGTIRSNldpfgeysdEELWQALERVG---LKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTAFKNkkRAALLTTHYMeeaEAV--CDRVAIMVSGQLRCIGT 1516
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKD--CTVLTIAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1306-1514 |
2.44e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1306 LHSRKTTKVatKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDESTKCMGYCPQT-- 1382
Cdd:PRK09700 271 VTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISPRSPLDAVKKGMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1383 -NPLWPDITLQEHFEIY---------GAVKGMSSGDMKEVISRITKALDLKEH-LQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:PRK09700 349 dNGFFPNFSIAQNMAISrslkdggykGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1452 QVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
499-646 |
3.40e-14 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 75.91 E-value: 3.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARKmIGICPQSDMNFDVLTVEENLS 578
Cdd:PRK11432 24 NLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRD-ICMVFQSYALFPHMSLGENVG 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 579 ILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11432 101 YGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
478-691 |
4.04e-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: 4.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYR-----KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--E 550
Cdd:TIGR02769 3 LEVRDVTHTYRtgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 551 MFEARKMIGICPQSDMNfdvlTVEENLSILASVkGIPANNII-----QEVQKVLLDLDMQAIKDNQAKK----LSGGQKR 621
Cdd:TIGR02769 83 RRAFRRDVQLVFQDSPS----AVNPRMTVRQII-GEPLRHLTsldesEQKARIAELLDMVGLRSEDADKlprqLSGGQLQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQGML 691
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-643 |
5.35e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.53 E-value: 5.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 498 RNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQSDMNfDVLTVEENL 577
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLLYLGHQPGIK-TELTALENL 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 578 SILASVKGIPANNIIQEV-QKVLLdldmQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP-TA 643
Cdd:PRK13538 96 RFYQRLHGPGDDEALWEAlAQVGL----AGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPfTA 159
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1290-1511 |
5.94e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 72.78 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKDFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:COG2884 2 IRFENVSKRYPGGREALSD----------VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTK---CMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEvisRITKALD---LKEHLQKTVKKLPAGIKRKLCF 1443
Cdd:COG2884 72 REIPYlrrRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRR---RVREVLDlvgLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1444 ALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAfkNKKRAA-LLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEI--NRRGTTvLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1516 |
5.97e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 73.96 E-value: 5.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNED-DESTKCMGYCP 1380
Cdd:PRK13639 5 RDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIkGEPIKYDKKSlLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1381 QtNPlwPDITLQEHFEIYGAVKGMSSG-DMKEVISRITKAL---DLKEHLQKTVKKLPAGIKRKLCFA--LSMlgNPQVT 1454
Cdd:PRK13639 85 Q-NP--DDQLFAPTVEEDVAFGPLNLGlSKEEVEKRVKEALkavGMEGFENKPPHHLSGGQKKRVAIAgiLAM--KPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1455 LLDEPSTGMDPRAKQHMWRAIRTAfkNKKRAAL-LTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDL--NKEGITIiISTHDVDLVPVYADKVYVMSDGKIIKEGT 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1319-1511 |
6.42e-14 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.21 E-value: 6.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD--YGSHSNEDdeSTKC-MGYCP---QTNPLWPD---- 1388
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRD--AIRAgIAYVPedrKGEGLVLDlsir 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1389 --ITL--QEHFEIYGAVkgmSSGDMKEVISRITKALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGM 1463
Cdd:COG1129 349 enITLasLDRLSRGGLL---DRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGI 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27368659 1464 DPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG1129 426 DVGAKAEIYRLIR-ELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
480-642 |
6.56e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 480 ISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemFEARKMIG 559
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVS-----IPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 ICPQSDMNFDVLTVEENlsILASVKGIPAnnIIQEVQKVL-----LDLDMQAIKDNQAK--------------------- 613
Cdd:COG0488 65 YLPQEPPLDDDLTVLDT--VLDGDAELRA--LEAELEELEaklaePDEDLERLAELQEEfealggweaearaeeilsglg 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27368659 614 -----------KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG0488 141 fpeedldrpvsELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-705 |
6.97e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.16 E-value: 6.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 474 GKEAIRISGIQKAYRKknetVEALRNLSFDIYEGQITALLGHSGTG--KSTLMNILCGlcpPSDG-----FASIYGHRVS 546
Cdd:NF000106 10 ARNAVEVRGLVKHFGE----VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrpwrF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 547 eidemfeARKMIGIC-PQSDMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSL 625
Cdd:NF000106 83 -------LRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGMLKCVGSSIFLKSKW 704
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVlLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
.
gi 27368659 705 G 705
Cdd:NF000106 236 G 236
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
489-697 |
7.19e-14 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 76.38 E-value: 7.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL--CPPSDGfASIY------------------------G 542
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSG-RIIYhvalcekcgyverpskvgepcpvcG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 543 HRVSEIDEMF---------EARKMIGICPQSDMN-FDVLTVEENlsILASVK--GIPANNIIQEVQKVLLDLDMQAIKDN 610
Cdd:TIGR03269 87 GTLEPEEVDFwnlsdklrrRIRKRIAIMLQRTFAlYGDDTVLDN--VLEALEeiGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 611 QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVT-VFSTHFMDEADILADRKAVISQ 688
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISmVLTSHWPEVIEDLSDKAIWLEN 244
|
....*....
gi 27368659 689 GMLKCVGSS 697
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1323-1507 |
8.02e-14 |
|
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: 76.36 E-value: 8.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygshsnedDESTKcMGYCPQTnpLWPDI--TLQEHfeIYGA 1400
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------DEDLK-ISYKPQY--ISPDYdgTVEEF--LRSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 VKGMSSGDMKEviSRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFK 1480
Cdd:COG1245 426 NTDDFGSSYYK--TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAE 503
|
170 180
....*....|....*....|....*....
gi 27368659 1481 NKKRAALLTTH--YMeeAEAVCDRvaIMV 1507
Cdd:COG1245 504 NRGKTAMVVDHdiYL--IDYISDR--LMV 528
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1323-1516 |
8.14e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 8.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDY----GSHSNEDDESTKCMGYCPQ--TNPLWPDITLQEhfE 1396
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKPVRKKVGVVFQfpESQLFEETVLKD--V 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVK-GMSSGDMKEVISRITKALDL-KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRA 1474
Cdd:PRK13643 107 AFGPQNfGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1475 IRTAFKNKKrAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK13643 187 FESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1319-1511 |
8.17e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.10 E-value: 8.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHfeI 1397
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAEN--L 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 Y--------GAVKgmsSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQ 1469
Cdd:PRK11288 101 YlgqlphkgGIVN---RRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSAREIE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1470 HMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11288 178 QLFRVIR-ELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-697 |
8.41e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.51 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---PPSDGFASIYGHRVSE----IDE 550
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 551 MFEARKMIGICPQSDMNFDVLTVEENLsILASVKGIP---------ANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKR 621
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1319-1525 |
8.58e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 75.26 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEI- 1397
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSFEFDVRQVVEMg 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 ----YGAVKGMSSGDmKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDprakqhMWR 1473
Cdd:PRK09536 102 rtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD------INH 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1474 AIRT-----AFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIG------TVQHLKSKFG 1525
Cdd:PRK09536 175 QVRTlelvrRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFD 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1320-1520 |
8.88e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 72.48 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgSHSneddestkcmGYCP---------QTNPLWPDIT 1390
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ-DLT----------ALPPaerpvsmlfQENNLFPHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1391 LQEHFEIygavkGMSSG-----DMKEVISRITKALDLKEHLQktvkKLPA----GIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:COG3840 88 VAQNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLD----RLPGqlsgGQRQRVALARCLVRKRPILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1462 GMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:COG3840 159 ALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1286-1511 |
1.08e-13 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 72.54 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1286 EKPAIMVYNLHKEYDDKK---DFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGK-IFLG- 1360
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGSvqtDVLHN----------VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDvIFNGq 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1361 --DYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIK 1438
Cdd:PRK11629 72 pmSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGER 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1439 RKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVcDRVAIMVSGQL 1511
Cdd:PRK11629 152 QRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1289-1524 |
1.12e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.93 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEY-------DDKKDFLHSRKTTKV--ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIfl 1359
Cdd:PRK13546 4 SVNIKNVTKEYriyrtnkERMKDALIPKHKNKTffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1360 gdygshsnEDDESTKCMGYCPQTNplwPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKR 1439
Cdd:PRK13546 82 --------DRNGEVSVIAISAGLS---GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1440 KLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:PRK13546 151 KLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDD 229
|
....*
gi 27368659 1520 LKSKF 1524
Cdd:PRK13546 230 VLPKY 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
489-689 |
1.18e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.63 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMfeARKMIGICPQS 564
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSgsplKASNIRDT--ERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNFDVLTVEENLSI---LASVKGIPANN-IIQEVQKVLLDLDMQAIKDNQA-KKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:TIGR02633 87 LTLVPELSVAENIFLgneITLPGGRMAYNaMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 640 EPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDG 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1292-1528 |
1.18e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 75.70 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNlhKEYDDKKDFLHSRKTTKV--ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGSHSned 1369
Cdd:PRK13545 16 MYN--KPFDKLKDLFFRSKDGEYhyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK--GSAA--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 destkcmgYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:PRK13545 89 --------LIAISSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1450 NPQVTLLDEP-STGMDPRAKQHMWRAirTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFG--- 1525
Cdd:PRK13545 161 NPDILVIDEAlSVGDQTFTKKCLDKM--NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDefl 238
|
...
gi 27368659 1526 KGY 1528
Cdd:PRK13545 239 KKY 241
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
473-689 |
1.68e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 473 IGKEAIRISGIQKAyrkknetveALRN-LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEM 551
Cdd:PRK11288 253 LGEVRLRLDGLKGP---------GLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 FEA-RKMIGICPQsDMNFD----VLTVEENLSILASVKGIPANNII---QEVQKVLLDLDMQAIK----DNQAKKLSGG- 618
Cdd:PRK11288 323 RDAiRAGIMLCPE-DRKAEgiipVHSVADNINISARRHHLRAGCLInnrWEAENADRFIRSLNIKtpsrEQLIMNLSGGn 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 619 -QK----RKLSLGIavlgnpKILLLDEPTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK11288 402 qQKailgRWLSEDM------KVILLDEPTRGIDVGAKHEIYNVI-YELAAQgvaVLFVSSDLP-EVLGVADRIVVMREG 472
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-684 |
1.78e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.38 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrvegrveffnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 547 eIDEMFEARKMIGICPqsdmNFDVLTVEENLSILASVKGI-PANNIIQEVQKVLLDLDM-QAIKDN---QAKKLSGGQKR 621
Cdd:PRK14258 83 -LNRLRRQVSMVHPKP----NLFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwDEIKHKihkSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR--KANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1276-1516 |
1.90e-13 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.83 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1276 KELMGCQCCEEKPAIMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSG 1355
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1356 KIFLGDygshsneddestKCMGYCP----------QTNPLWPDITLqehFEIYGAVKGMSSGDMKEVISRITKAL---DL 1422
Cdd:PRK09452 70 RIMLDG------------QDITHVPaenrhvntvfQSYALFPHMTV---FENVAFGLRMQKTPAAEITPRVMEALrmvQL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1423 KEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMwraiRTAFKNKKRAALLT----THYMEEAEA 1498
Cdd:PRK09452 135 EEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM----QNELKALQRKLGITfvfvTHDQEEALT 210
|
250
....*....|....*...
gi 27368659 1499 VCDRVAIMVSGQLRCIGT 1516
Cdd:PRK09452 211 MSDRIVVMRDGRIEQDGT 228
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
490-658 |
2.00e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.92 E-value: 2.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHrvsEIDEMFEARkmIGICPQSDM 566
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR---PLDSSFQRS--IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NFDVLTVEENLSILASVKgIPANNIIQE----VQKVLLDLDMQAIKDN----QAKKLSGGQKRKLSLGIAVLGNPKILL- 637
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLR-QPKSVSKSEkmeyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180
....*....|....*....|.
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLK 658
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMR 946
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
497-695 |
2.19e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 74.78 E-value: 2.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQsdmnfDV-L---T 572
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE-ELGRHIGYLPQ-----DVeLfdgT 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSILASVkgiPANNIIQEVQKV-----LLDL----DMQaIKDNQAKkLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:COG4618 422 IAENIARFGDA---DPEKVVAAAKLAgvhemILRLpdgyDTR-IGEGGAR-LSGGQRQRIGLARALYGDPRLVVLDEPNS 496
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 644 GMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADIL--ADRKAVISQGMLKCVG 695
Cdd:COG4618 497 NLDDEGEAALAAAIRALKARGATVVvITH---RPSLLaaVDKLLVLRDGRVQAFG 548
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1319-1491 |
2.40e-13 |
|
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: 74.70 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWpDITLQEHFEIy 1398
Cdd:TIGR02868 354 VSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLF-DTTVRENLRL- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 gAVKGMSSGDMKEVISRITKALDLKEH-------LQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:TIGR02868 432 -ARPDATDEELWAALERVGLADWLRALpdgldtvLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADEL 510
|
170 180
....*....|....*....|
gi 27368659 1472 WRAIRTAfkNKKRAALLTTH 1491
Cdd:TIGR02868 511 LEDLLAA--LSGRTVVLITH 528
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
478-676 |
3.57e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 72.43 E-value: 3.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETV-EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIYGHRVSEIDEM 551
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 552 F------------------EARKMIGICPQ-SDMNFDVLTVEENLSILASVKGIPANNIIQEVQKV--LLDLDMQAIKDN 610
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLDESYLQRS 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 611 QAKkLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:PRK13651 163 PFE-LSGGQKRRVALaGILAM-EPDFLVFDEPTAGLDPQGVKEILEIFdNLNKQGKTIILVTHDLDNV 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1294-1525 |
3.70e-13 |
|
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: 70.72 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKDFLhsrkttkvatKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEST 1373
Cdd:cd03253 5 NVTFAYDPGRPVL----------KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQTNPLW------------PDITLQehfEIYGAVKgmsSGDMKEVISRITKALDlkehlqkTV-----KKLPAG 1436
Cdd:cd03253 75 RAIGVVPQDTVLFndtigynirygrPDATDE---EVIEAAK---AAQIHDKIMRFPDGYD-------TIvgergLKLSGG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1437 IKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03253 142 EKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGT 218
|
....*....
gi 27368659 1517 VQHLKSKFG 1525
Cdd:cd03253 219 HEELLAKGG 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
489-689 |
4.43e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.81 E-value: 4.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY---------GHRVSEidemfeaRKMIG 559
Cdd:PRK13549 13 KTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqasNIRDTE-------RAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 ICPQSDMNFDVLTVEENLsILAS--VKG--IPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13549 86 IIHQELALVKELSVLENI-FLGNeiTPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIAcIYISHKLNEVKAISDTICVIRDG 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-691 |
5.08e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.28 E-value: 5.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 509 ITALLGHSGTGKSTLMNILCGLCPPSDGF-----ASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEENLSILASV 583
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 584 KGIPANNIIQEVQKVLLDLDM-QAIKDNQAK---KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKy 659
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR- 207
|
170 180 190
....*....|....*....|....*....|...
gi 27368659 660 RKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK14271 208 SLADRLTViIVTHNLAQAARISDRAALFFDGRL 240
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1301-1511 |
5.19e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 71.40 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1301 DKKDFLHSRKTT--KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCM-- 1376
Cdd:PRK13641 6 ENVDYIYSPGTPmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrk 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1377 --GYCPQtnplWPDITLQEHFEI----YGAVK-GMSSGDMKEVISRITKALDLKEHL-QKTVKKLPAGIKRKLCFALSML 1448
Cdd:PRK13641 86 kvSLVFQ----FPEAQLFENTVLkdveFGPKNfGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1449 GNPQVTLLDEPSTGMDPRAKQHMWRairtAFKNKKRAA---LLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1294-1459 |
5.22e-13 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 73.56 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKDFLHsrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsnedDEST 1373
Cdd:COG0488 3 NLSKSFGGRPLLDD-----------VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI----------PKGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KcMGYCPQTNPLWPDITLQE-----HFEIYGAVK---------GMSSGDMKEV------------------ISRITKALD 1421
Cdd:COG0488 62 R-IGYLPQEPPLDDDLTVLDtvldgDAELRALEAeleeleaklAEPDEDLERLaelqeefealggweaearAEEILSGLG 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1422 LKEH-LQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEP 1459
Cdd:COG0488 141 FPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
497-646 |
5.27e-13 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.91 E-value: 5.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARKMIGICPQSdMNFDV---LTV 573
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKR--NGKLRIGYVPQK-LYLDTtlpLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 574 EENLSILASVKG---IPANNIIQEVQkvLLDLDMQaikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK09544 87 NRFLRLRPGTKKediLPALKRVQAGH--LIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1287-1511 |
5.33e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 70.57 E-value: 5.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1287 KPAIMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINIL--VGDVEP---TSGKIFLGD 1361
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1362 YGSHSNEDD--ESTKCMGYC-PQTNPlWPdITLQEHFeIYG-AVKGMSSgdmKEVISR-ITKAL-------DLKEHLQKT 1429
Cdd:PRK14239 72 HNIYSPRTDtvDLRKEIGMVfQQPNP-FP-MSIYENV-VYGlRLKGIKD---KQVLDEaVEKSLkgasiwdEVKDRLHDS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1430 VKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQhmwRAIRTAFKNKKRAALLT-THYMEEAEAVCDRVAIMVS 1508
Cdd:PRK14239 146 ALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG---KIEETLLGLKDDYTMLLvTRSMQQASRISDRTGFFLD 222
|
...
gi 27368659 1509 GQL 1511
Cdd:PRK14239 223 GDL 225
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
480-689 |
5.95e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 70.86 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 480 ISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE----MF-EA 554
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrlMFqDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RkmigICPQSdmnfdvlTVEENLSIlaSVKGIPANNIIQEVQKVLLDldmqaikdNQAKK----LSGGQKRKLSLGIAVL 630
Cdd:PRK11247 91 R----LLPWK-------KVIDNVGL--GLKGQWRDAALQALAAVGLA--------DRANEwpaaLSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1509 |
6.52e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.92 E-value: 6.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDKkdflhsrktTKvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNE 1368
Cdd:PRK13647 4 IIEVEDLHFRYKDG---------TK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1369 DDESTKCMGYCPQ-------TNPLWPDITlqehfeiYGAVK-GMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRK 1440
Cdd:PRK13647 74 EKWVRSKVGLVFQdpddqvfSSTVWDDVA-------FGPVNmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1441 LCFA--LSMlgNPQVTLLDEPSTGMDPRAKQHMwRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK13647 147 VAIAgvLAM--DPDVIVLDEPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-705 |
6.90e-13 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 71.83 E-value: 6.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 509 ITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMF----EARKmIGICPQSDMNFDVLTVEENLSIlasvk 584
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppEKRR-IGYVFQDARLFPHYKVRGNLRY----- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 585 GIPANNIIQEVQKVLLdLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD-PCSRHivwnLLKY--RK 661
Cdd:PRK11144 100 GMAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE----LLPYleRL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 662 ANRVT---VFSTHFMDEADILADRKAVISQGMLKCVGSsifLKSKWG 705
Cdd:PRK11144 175 AREINipiLYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1319-1516 |
7.05e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 70.43 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEiY 1398
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELVA-Y 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 G-----AVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWR 1473
Cdd:PRK11231 100 GrspwlSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 1474 AIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK11231 180 LMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
499-689 |
7.78e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.56 E-value: 7.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEARKMIGICPQSDMNFDVLTVEEN 576
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:PRK11831 105 VAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 656 LL-KYRKANRVT-VFSTH-------FMDEADILADRKaVISQG 689
Cdd:PRK11831 185 LIsELNSALGVTcVVVSHdvpevlsIADHAYIVADKK-IVAHG 226
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1319-1511 |
7.96e-13 |
|
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: 69.36 E-value: 7.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDY---GSHSNEDDESTKCMGYCPQTNPLWPDITLQEHF 1395
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRRKIGVVFQDFRLLPDRNVYENV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1396 EIYGAVKGMSSgdmKEVISRITKALDLKEhLQKTVKKLPAGIKR----KLCFALSMLGNPQVTLLDEPSTGMDPrakQHM 1471
Cdd:cd03292 100 AFALEVTGVPP---REIRKRVPAALELVG-LSHKHRALPAELSGgeqqRVAIARAIVNSPTILIADEPTGNLDP---DTT 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1472 WRAIRTAFKNKKRAA--LLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03292 173 WEIMNLLKKINKAGTtvVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1289-1511 |
8.39e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.16 E-value: 8.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDKKdFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTI---INILVgdvEPTSGKIFLGDY--- 1362
Cdd:PRK11264 3 AIEVKNLVKKFHGQT-VLHG----------IDLEVKPGEVVAIIGPSGSGKTTLlrcINLLE---QPEAGTIRVGDItid 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1363 -----GSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFeIYGA--VKGMSSGDM----KEVISRItkALDLKEhlQKTVK 1431
Cdd:PRK11264 69 tarslSQQKGLIRQLRQHVGFVFQNFNLFPHRTVLENI-IEGPviVKGEPKEEAtaraRELLAKV--GLAGKE--TSYPR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1432 KLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11264 144 RLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIR-QLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
490-657 |
8.63e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 8.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK--MIGICPQSDMN 567
Cdd:PRK15112 22 RRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRirMIFQDPSTSLN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 --------FDV-LTVEENLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQakkLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK15112 102 prqrisqiLDFpLRLNTDLEPEQREK-----QIIETLRQVGLLPDHASYYPHM---LAPGQKQRLGLARALILRPKVIIA 173
|
170
....*....|....*....
gi 27368659 639 DEPTAGMDPCSRHIVWNLL 657
Cdd:PRK15112 174 DEALASLDMSMRSQLINLM 192
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1294-1509 |
8.89e-13 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 69.98 E-value: 8.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGD--VEPTSGKIFLGdyGSHSNE--- 1368
Cdd:TIGR01978 5 DLHVSVEDKE-----------ILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTILFK--GQDLLElep 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1369 DDESTKCMGYCPQTNPLWPDITLQEhFeIYGAVKGMSSGDMKEVIsritKALDLKEHLQKTVKKL---PAGIKRKL---- 1441
Cdd:TIGR01978 72 DERARAGLFLAFQYPEEIPGVSNLE-F-LRSALNARRSARGEEPL----DLLDFEKLLKEKLALLdmdEEFLNRSVnegf 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1442 ---------CFALSMLgNPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVC-DRVAIMVSG 1509
Cdd:TIGR01978 146 sggekkrneILQMALL-EPKLAILDEIDSGLDIDALKIVAEGIN-RLREPDRSFLIITHYQRLLNYIKpDYVHVLLDG 221
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1306-1528 |
9.58e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 70.11 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1306 LHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdygshSNEDDESTKCMGYCPQTNPL 1385
Cdd:PRK11248 7 LYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLD-----GKPVEGPGAERGVVFQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 WPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:PRK11248 82 LPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1466 RAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRcigTVQHLKSKFGKGY 1528
Cdd:PRK11248 162 FTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGR---VVERLPLNFARRF 221
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
460-671 |
9.73e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 73.52 E-value: 9.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 460 SLNEIV--EP-VSSEFIGKEAIRISGIQ-KAYRKKNET---VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:PTZ00265 357 SLYEIInrKPlVENNDDGKKLKDIKKIQfKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYD 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 533 PSDGFASIY-GHRVSEIDEMFeARKMIGICPQSDMNF---------------------------DVLTVEENLSILASVK 584
Cdd:PTZ00265 437 PTEGDIIINdSHNLKDINLKW-WRSKIGVVSQDPLLFsnsiknnikyslyslkdlealsnyyneDGNDSQENKNKRNSCR 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 585 GIPA---NNIIQEV------------------------QKVLLDLDMQAIKD-------NQAKKLSGGQKRKLSLGIAVL 630
Cdd:PTZ00265 516 AKCAgdlNDMSNTTdsneliemrknyqtikdsevvdvsKKVLIHDFVSALPDkyetlvgSNASKLSGGQKQRISIARAII 595
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 27368659 631 GNPKILLLDEPTAGMDPCSRHIVWNLLKYRKA--NRVTVFSTH 671
Cdd:PTZ00265 596 RNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITIIIAH 638
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1319-1516 |
1.19e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.63 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygsHSNEDDESTKC--MGYCP--QTNPLWPDITLQEH 1394
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRG---QHIEGLPGHQIarMGVVRtfQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEI--YGAVK-GMSSGDMK---------EVISRITKALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEP 1459
Cdd:PRK11300 101 LLVaqHQQLKtGLFSGLLKtpafrraesEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1460 STGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1319-1511 |
1.23e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 72.39 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygsHSNEDDESTKCMG----YCP---QTNPLWPDITL 1391
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLArglvYLPedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 qehfeiYGAVKGMSSGDM---------KEVISRITKALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:PRK15439 359 ------AWNVCALTHNRRgfwikpareNAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 1462 GMDPRAKQHMWRAIRTAFKnKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
497-675 |
1.41e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.97 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFeaRKMIGICPQSDMNFDVlTVEE 575
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIY--RQQVSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK10247 100 NLIFPWQIR-----NQQPDPAIFLDDLERFALPDTILTKniaeLSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 27368659 652 IVWNLL-KYRKANRVTV-FSTHFMDE 675
Cdd:PRK10247 175 NVNEIIhRYVREQNIAVlWVTHDKDE 200
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1306-1525 |
1.67e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 1.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1306 LHSRKTtkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI--FLGDYGSHSNEDDESTKcMGYCPQ-- 1381
Cdd:NF033858 9 HRYGKT--VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVevLGGDMADARHRRAVCPR-IAYMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1382 -TNpLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRK--LCFALsmLGNPQVTLLDE 1458
Cdd:NF033858 86 gKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1459 PSTGMDPRAKQHMWR---AIRTAfknkkRAA---LLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:NF033858 163 PTTGVDPLSRRQFWElidRIRAE-----RPGmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1320-1511 |
2.24e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 68.46 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshSNEDDESTK------CMGYcpQTNPLWPDITLQE 1393
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTL------NGQDHTTTPpsrrpvSMLF--QENNLFSHLTVAQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEIygavkGMSSG-----DMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK 1468
Cdd:PRK10771 91 NIGL-----GLNPGlklnaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 1469 QHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1315-1509 |
2.50e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1315 ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSNEDDESTkCMGYCPQTNPL-WP------ 1387
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI--LGQPTRQALQKN-LVAYVPQSEEVdWSfpvlve 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1388 DITLQEHFEIYGAVKGMSSGDmKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRA 1467
Cdd:PRK15056 99 DVVMMGRYGHMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1468 KQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDrVAIMVSG 1509
Cdd:PRK15056 178 EARIISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
496-690 |
2.72e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.86 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMNFDVLTVEE 575
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NL----------SILASVKGIPA-----NNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK11300 100 NLlvaqhqqlktGLFSGLLKTPAfrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 641 PTAGMDPCSRHIVWNLL-KYRKANRVTVFST-HFMDEADILADRKAVISQGM 690
Cdd:PRK11300 180 PAAGLNPKETKELDELIaELRNEHNVTVLLIeHDMKLVMGISDRIYVVNQGT 231
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1319-1512 |
2.94e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.88 E-value: 2.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDES---TKCMGYCPQTNPLWPDITLQEH 1394
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQMDEEARAklrAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDpraKQHMWRA 1474
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD---RQTGDKI 185
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27368659 1475 IRTAFKNKKRAA---LLTTHYMEEAeAVCDRVAIMVSGQLR 1512
Cdd:PRK10584 186 ADLLFSLNREHGttlILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-689 |
3.07e-12 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 3.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 467 PVSSEFIGKEAIRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---- 542
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 543 ---HRVSEIDEMFEAR---------KMIGICPQSDMNfDVLTVEENlsILASVK---GIPANNIIQEVQKvLLDL----D 603
Cdd:PRK10261 82 rrsRQVIELSEQSAAQmrhvrgadmAMIFQEPMTSLN-PVFTVGEQ--IAESIRlhqGASREEAMVEAKR-MLDQvripE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 604 MQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILAD 681
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlqKEMSMGVIFITHDMGVVAEIAD 237
|
....*...
gi 27368659 682 RKAVISQG 689
Cdd:PRK10261 238 RVLVMYQG 245
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
478-689 |
3.15e-12 |
|
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: 65.55 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNetveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFaSIYGHRVSeidemfearkm 557
Cdd:cd03221 1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 IGICPQsdmnfdvltveenlsilasvkgipanniiqevqkvlldldmqaikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03221 65 IGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVfsTH---FMDEadiLADRKAVISQG 689
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGTVILV--SHdryFLDQ---VATKIIELEDG 143
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1317-1516 |
3.19e-12 |
|
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: 67.44 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSNEDDESTkcMGYCPQtNPLWPDITLQEH 1394
Cdd:cd03369 25 KNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgiDISTIPLEDLRSS--LTIIPQ-DPTLFSGTIRSN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEIYgavkGMSSGDmkevisRITKALDLKEhlqkTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRA 1474
Cdd:cd03369 102 LDPF----DEYSDE------EIYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKT 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 1475 IRTAFKNkkrAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03369 168 IREEFTN---STILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1319-1518 |
3.28e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 68.62 E-value: 3.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTnplwPDITLQEHFEIY 1398
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQN----PDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGM-----SSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWR 1473
Cdd:PRK13648 104 DVAFGLenhavPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27368659 1474 AIRTAFKNKKRAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK13648 184 LVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPT 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
494-691 |
3.82e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 70.83 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEMFEA--------RKMIGICPq 563
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRERRRLgvayipedRLGRGLVP- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 564 sDMnfdvlTVEENLsILASVKGIP-ANNIIqevqkvlldLDMQAIKDN-----------------QAKKLSGGQKRKLSL 625
Cdd:COG3845 350 -DM-----SVAENL-ILGRYRRPPfSRGGF---------LDRKAIRAFaeelieefdvrtpgpdtPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANR-VTVFSTHfMDEADILADRKAVISQGML 691
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAaVLLISED-LDEILALSDRIAVMYEGRI 480
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-671 |
4.06e-12 |
|
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: 71.48 E-value: 4.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTVEEN 576
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSV-TLQTWRKAFGVIPQKVFIFSG-TFRKN 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LSILASVKGipanniiQEVQKVLLDLDMQAIKDNQAKKL-----------SGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:TIGR01271 1312 LDPYEQWSD-------EEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHL 1384
|
170 180
....*....|....*....|....*.
gi 27368659 646 DPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR01271 1385 DPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1323-1491 |
4.76e-12 |
|
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: 68.16 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTsgkifLGDYGShsneddestkcmgycpqtNPLWPDI-------TLQEHF 1395
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDD------------------PPDWDEIldefrgsELQNYF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1396 E------------------IYGAVKG-----MSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQ 1452
Cdd:cd03236 80 TkllegdvkvivkpqyvdlIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTAFKNkKRAALLTTH 1491
Cdd:cd03236 160 FYFFDEPSSYLDIKQRLNAARLIRELAED-DNYVLVVEH 197
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
458-695 |
5.82e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.92 E-value: 5.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 458 NISLNeiVEPVSSEF----IGKEAIRISGIQKayrKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP 533
Cdd:PRK13546 2 NVSVN--IKNVTKEYriyrTNKERMKDALIPK---HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 534 SDGFASIYGH-RVSEIDEMFEARkmigicpqsdmnfdvLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQA 612
Cdd:PRK13546 77 TVGKVDRNGEvSVIAISAGLSGQ---------------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEP-TAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13546 142 KKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
....
gi 27368659 692 KCVG 695
Cdd:PRK13546 222 KDYG 225
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1260-1482 |
6.04e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 6.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1260 INEDEDEDVKAERLKVkelmGCQCCEEK-P--AIMVYNLHKEYDDkkDFLHSRKTTkvatkyvSF------CVKKGEILG 1330
Cdd:PRK13409 37 IDEDDGKPVISEELCI----GCGICVKKcPfdAISIVNLPEELEE--EPVHRYGVN-------GFklyglpIPKEGKVTG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1331 LLGPNGAGKSTIINILVGDVEPTsgkifLGDYGShsneddestkcmgycpqtNPLWPDI-------TLQEHFE------- 1396
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPN-----LGDYEE------------------EPSWDEVlkrfrgtELQNYFKklyngei 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 -----------IYGAVKGMSS---------GDMKEVISRitkaLDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLL 1456
Cdd:PRK13409 161 kvvhkpqyvdlIPKVFKGKVRellkkvderGKLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
250 260
....*....|....*....|....*.
gi 27368659 1457 DEPSTGMDPRAKQHMWRAIRTAFKNK 1482
Cdd:PRK13409 237 DEPTSYLDIRQRLNVARLIRELAEGK 262
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
497-692 |
6.46e-12 |
|
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: 67.96 E-value: 6.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNFDVlTVEEN 576
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDGVSWNSV-PLQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LSILASVKGipanniiQEVQKVLLDLDMQAIKDNQAKK-----------LSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03289 97 LDPYGKWSD-------EEIWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 646 DPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLK 692
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
501-689 |
6.84e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 66.91 E-value: 6.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIdemfeARKMIGICPQSDMNFDVLTVEENLS 578
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPP-----SRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 579 IlasvkGIPANNIIQEVQKVLLdldmQAIKDNQA---------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK10771 94 L-----GLNPGLKLNAAQREKL----HAIARQMGiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 650 RHIVWNLLKYRKANR-VTVFS-THFMDEADILADRKAVISQG 689
Cdd:PRK10771 165 RQEMLTLVSQVCQERqLTLLMvSHSLEDAARIAPRSLVVADG 206
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
499-675 |
7.09e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.26 E-value: 7.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIDEMfEARKMIGICPQSDMNFDVlTVEENLS 578
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPE-SWRKHLSWVGQNPQLPHG-TLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 579 iLASVKgipANNiiQEVQKVLLD------LDMQA------IKDnQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11174 445 -LGNPD---ASD--EQLQQALENawvsefLPLLPqgldtpIGD-QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180
....*....|....*....|....*....
gi 27368659 647 PCSRHIVWNLLKYRKANRVTVFSTHFMDE 675
Cdd:PRK11174 518 AHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1319-1518 |
7.39e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.45 E-value: 7.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSNEddESTKCMGYCPQTNPLWPDITLQEHFE 1396
Cdd:COG4559 20 VSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgrPLAAWSPW--ELARRRAVLPQHSSLAFPFTVEEVVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFA--LSML-----GNPQVTLLDEPSTGMDPRAKQ 1469
Cdd:COG4559 98 LGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLwepvdGGPRWLFLDEPTSALDLAHQH 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1470 HMWRAIRTaFKNKKRAAL-------LTTHYmeeaeavCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG4559 178 AVLRLARQ-LARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
473-692 |
7.47e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 7.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 473 IGKEAIRISGIQkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-DGFASIYGHRV------ 545
Cdd:TIGR02633 253 IGDVILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 546 ----SEIDEMFEARKMIGICPQsdmnfdvLTVEEN--LSILASVKGIPANNIIQEVQKVLLDLDMQAIK----DNQAKKL 615
Cdd:TIGR02633 332 qairAGIAMVPEDRKRHGIVPI-------LGVGKNitLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRL 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHfMDEADILADRKAVISQGMLK 692
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGKLK 482
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
494-710 |
7.83e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 70.14 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQSDMNFDVlTV 573
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLS----------ILASVKGIPANNIIQEVQKvlldlDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:TIGR00958 572 RENIAygltdtpdeeIMAAAKAANAHDFIMEFPN-----GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 644 GMDPCSRHIVWNLLKyrKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSIFLKSKWGIGYRL 710
Cdd:TIGR00958 647 ALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1319-1516 |
7.95e-12 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 69.81 E-value: 7.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG-----DYgshsneDDES-TKCMGYCPQTNPLWPD---- 1388
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirDL------TLESlRRQIGVVPQDTFLFSGtire 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1389 -ITLqehfeiygavkGMSSGDMKEVISRITKAldlkeHLQKTVKKLPAGI---------------KRKLCFALSMLGNPQ 1452
Cdd:COG1132 433 nIRY-----------GRPDATDEEVEEAAKAA-----QAHEFIEALPDGYdtvvgergvnlsggqRQRIAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTAFKNkkRAALLTTHYMEEAEAvCDRVAIMVSGQLRCIGT 1516
Cdd:COG1132 497 ILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1319-1491 |
8.24e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.13 E-value: 8.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFlgdYGSHSNEDDEST--KCMGYCPQTNPLWPDITLQEH-- 1394
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEIL---FERQSIKKDLCTyqKQLCFVGHRSGINPYLTLRENcl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEIYgavkgMSSGDMKevISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRA 1474
Cdd:PRK13540 97 YDIH-----FSPGAVG--ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 27368659 1475 IRtAFKNKKRAALLTTH 1491
Cdd:PRK13540 170 IQ-EHRAKGGAVLLTSH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
493-691 |
1.08e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.31 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICP----QSDMNF 568
Cdd:PRK15439 275 TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrqSSGLYL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVltveenlSILASVKGIPANNI---IQEVQ-KVLLDLDMQAI------KDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK15439 355 DA-------PLAWNVCALTHNRRgfwIKPAReNAVLERYRRALnikfnhAEQAARTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1319-1516 |
1.16e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 67.95 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYgsHSNEDDESTKCMGYCPQTN-----PLWPDITLQE 1393
Cdd:PRK13631 45 ISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDI--YIGDKKNNHELITNPYSKKiknfkELRRRVSMVF 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEIYGAVK--------------GMSSGDMKEVISRITKALDLKE-HLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDE 1458
Cdd:PRK13631 123 QFPEYQLFKdtiekdimfgpvalGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1459 PSTGMDPRAKQHMWRAIRTAfKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK13631 203 PTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
503-685 |
1.16e-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: 66.66 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfeaRKMIGICPQSDMnfdvlTVEENLSILAS 582
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS--------YKPQYIKADYEG-----TVRDLLSSITK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 583 VKGIPA---NNIIQEVQkvlldldMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK- 658
Cdd:cd03237 88 DFYTHPyfkTEIAKPLQ-------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRr 160
|
170 180
....*....|....*....|....*...
gi 27368659 659 YRKANRVTVFST-HFMDEADILADRKAV 685
Cdd:cd03237 161 FAENNEKTAFVVeHDIIMIDYLADRLIV 188
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1309-1529 |
1.46e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 69.31 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1309 RKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEP---TSGKIFLgdyGSHSNEDDESTKCMGYCPQTNPL 1385
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLL---NGMPIDAKEMRAISAYVQQDDLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 WPDITLQEHFEIYGAVKgmssgdMKEVISRITKALDLKEHLQKT---------------VKKLPAGIKRKLCFALSMLGN 1450
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLR------MPRRVTKKEKRERVDEVLQALglrkcantrigvpgrVKGLSGGERKRLAFASELLTD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1451 PQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHyMEEAEAVC--DRVAIMVSGQLRCIGTVQHLKSKFGKGY 1528
Cdd:TIGR00955 185 PPLLFCDEPTSGLDSFMAYSVVQVLK-GLAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSDLG 262
|
.
gi 27368659 1529 F 1529
Cdd:TIGR00955 263 H 263
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1323-1493 |
1.57e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygshsnedDESTKcMGYCPQTNPLWPDITLQEHFEiygAVK 1402
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------------DPELK-ISYKPQYIKPDYDGTVEDLLR---SIT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1403 GMSSGDMkeVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNK 1482
Cdd:PRK13409 426 DDLGSSY--YKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170
....*....|...
gi 27368659 1483 KRAALLTTH--YM 1493
Cdd:PRK13409 504 EATALVVDHdiYM 516
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1319-1519 |
1.66e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG----DYGSHSNEDD--ESTKCMGYCPQTNPLWPDITLQ 1392
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfDFSKTPSDKAirELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHF-EIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:PRK11124 101 QNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27368659 1472 WRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:PRK11124 181 VSIIR-ELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1319-1465 |
1.78e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 66.19 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYG-SHSNEDDESTKCM-----GYCPQTNPLWPDITLQ 1392
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfDFSQKPSEKAIRLlrqkvGMVFQQYNLWPHLTVM 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1393 EHF-EIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:COG4161 101 ENLiEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1294-1516 |
1.84e-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: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKkDFLHSrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVG--DVEPTSGKIFLGdygshsNED-- 1369
Cdd:COG0396 5 NLHVSVEGK-EILKG----------VNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLD------GEDil 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 ----DE-STKCMGYCPQTNPLWPDITLqEHF--EIYGAVKG--MSSGDMKEVISRITKALDL-KEHLQKTVKklpAG--- 1436
Cdd:COG0396 68 elspDErARAGIFLAFQYPVEIPGVSV-SNFlrTALNARRGeeLSAREFLKLLKEKMKELGLdEDFLDRYVN---EGfsg 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1437 --IKRKLCFALSMLgNPQVTLLDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHY---MEEAEAvcDRVAIMVSGQL 1511
Cdd:COG0396 144 geKKRNEILQMLLL-EPKLAILDETDSGLDIDALRIVAEGVN-KLRSPDRGILIITHYqriLDYIKP--DFVHVLVDGRI 219
|
....*
gi 27368659 1512 RCIGT 1516
Cdd:COG0396 220 VKSGG 224
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1289-1464 |
2.02e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 68.38 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1289 AIMVYNLHKEYDDKKDFlhsrkttkvatKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgDYGSHSNe 1368
Cdd:PRK15064 319 ALEVENLTKGFDNGPLF-----------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---KWSENAN- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1369 ddestkcMGYCPQ--TNPLWPDITLQEHFEIYGAVKgmssGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALS 1446
Cdd:PRK15064 384 -------IGYYAQdhAYDFENDLTLFDWMSQWRQEG----DDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKL 452
|
170
....*....|....*...
gi 27368659 1447 MLGNPQVTLLDEPSTGMD 1464
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD 470
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
496-646 |
2.84e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.06 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDvLTVEE 575
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIED 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSI----------LASVKGIPANNIIqevQKVLLDLDMQAikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PRK13657 428 NIRVgrpdatdeemRAAAERAQAHDFI---ERKPDGYDTVV--GERGRQLSGGERQRLAIARALLKDPPILILDEATSAL 502
|
.
gi 27368659 646 D 646
Cdd:PRK13657 503 D 503
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1294-1550 |
3.19e-11 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 66.98 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygSHSNEDDEST 1373
Cdd:PRK11000 8 NVTKAYGDV-----------VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE--KRMNDVPPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 KCMGYCPQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQV 1453
Cdd:PRK11000 75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1454 TLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL----KSKFGKGY- 1528
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGFi 234
|
250 260
....*....|....*....|....*...
gi 27368659 1529 ------FLEIKlkdwIENLEIDRLQREI 1550
Cdd:PRK11000 235 gspkmnFLPVK----VTATAIEQVQVEL 258
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
477-646 |
3.21e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 68.21 E-value: 3.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARK 556
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV---LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGICPQ-----SDMNFDVLTVEENLSilasvkgipANNIIQEVQKVLLDLDMQAIKD-------NQAKKLSGGQKRKLS 624
Cdd:PRK10790 416 GVAMVQQdpvvlADTFLANVTLGRDIS---------EEQVWQALETVQLAELARSLPDglytplgEQGNNLSVGQKQLLA 486
|
170 180
....*....|....*....|..
gi 27368659 625 LGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10790 487 LARVLVQTPQILILDEATANID 508
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1259-1483 |
3.34e-11 |
|
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: 67.89 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1259 PINEDEDEDVKAERLKVK-----ELM-GCQCCEEK-P--AIMVYNLHKEYDDKKdfLHSRKTTkvatkyvSF------CV 1323
Cdd:COG1245 26 PVNRTGKEAIEIDEDDGKpviseELCiGCGICVKKcPfdAISIVNLPEELEEDP--VHRYGEN-------GFrlyglpVP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1324 KKGEILGLLGPNGAGKSTIINILVGDVEPTsgkifLGDYgshsneDDEstkcmgycpqtnPLWPDI-------TLQEHFE 1396
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDY------DEE------------PSWDEVlkrfrgtELQDYFK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 ------------------IYGAVKGMSS---------GDMKEVISRitkaLDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:COG1245 154 klangeikvahkpqyvdlIPKVFKGTVRellekvderGKLDELAEK----LGLENILDRDISELSGGELQRVAIAAALLR 229
|
250 260 270
....*....|....*....|....*....|....
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKK 1483
Cdd:COG1245 230 DADFYFFDEPSSYLDIYQRLNVARLIRELAEEGK 263
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1313-1526 |
4.02e-11 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 65.49 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsnED------DESTKCMGYCPQtNPLW 1386
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG------KDvtklpeYKRAKYIGRVFQ-DPMM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 ---PDITLQEHFEI-------YGAVKGMSSGDMKEVISRITK-ALDLKEHLQKTVKKLPAGiKRKlcfALSML----GNP 1451
Cdd:COG1101 92 gtaPSMTIEENLALayrrgkrRGLRRGLTKKRRELFRELLATlGLGLENRLDTKVGLLSGG-QRQ---ALSLLmatlTKP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1452 QVTLLDEPSTGMDPR-AKQHMwRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVaIM---------VSGQLRCIGTVQHLK 1521
Cdd:COG1101 168 KLLLLDEHTAALDPKtAALVL-ELTEKIVEENNLTTLMVTHNMEQALDYGNRL-IMmhegriildVSGEEKKKLTVEDLL 245
|
....*
gi 27368659 1522 SKFGK 1526
Cdd:COG1101 246 ELFEE 250
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1319-1520 |
4.50e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 64.93 E-value: 4.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVE-----PTSGKIFLGDYGSHSNEDDESTKCMGYCPQT-NPLwPDITLQ 1392
Cdd:PRK14247 22 VNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIELRRRVQMVFQIpNPI-PNLSIF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIyGAVKGMSSGDMKEVISRITKALD-------LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:PRK14247 101 ENVAL-GLKLNRLVKSKKELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDP 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1466 RAKQHMwRAIRTAFKnKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK14247 180 ENTAKI-ESLFLELK-KDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
488-692 |
4.78e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 4.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE------MFEARKMIGIC 561
Cdd:PRK10619 12 HKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkVADKNQLRLLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 562 PQSDMNFDVLTVEENLSILASVKGIPANNI----IQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNP 633
Cdd:PRK10619 92 TRLTMVFQHFNLWSHMTVLENVMEAPIQVLglskQEARERAVKYLAKVGIDERAQGKypvhLSGGQQQRVSIARALAMEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 634 KILLLDEPTAGMDPcsrHIVWNLL----KYRKANRVTVFSTHFMDEADILADRKAVISQGMLK 692
Cdd:PRK10619 172 EVLLFDEPTSALDP---ELVGEVLrimqQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
473-646 |
4.82e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 4.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 473 IGKEAIRISGIQKAyrkknetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDE 550
Cdd:COG1129 252 PGEVVLEVEGLSVG--------GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 551 MFEA--------RKMIGICPQsdmnfdvLTVEENLSiLASVKGIPANNII------QEVQKVLLDLDmqaIK----DNQA 612
Cdd:COG1129 324 AIRAgiayvpedRKGEGLVLD-------LSIRENIT-LASLDRLSRGGLLdrrrerALAEEYIKRLR---IKtpspEQPV 392
|
170 180 190
....*....|....*....|....*....|....
gi 27368659 613 KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID 426
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1319-1503 |
5.66e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 5.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSNEddESTKCMGYCPQTNPLWPDiTLQEHFE 1396
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEgeDISTLKPE--IYRQQVSYCAQTPTLFGD-TVYDNLI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVKGMSSgDMKEVISRITKaLDLKEH-LQKTVKKLPAGIKRKlcfaLSMLGN----PQVTLLDEPSTGMDPRAKQHM 1471
Cdd:PRK10247 103 FPWQIRNQQP-DPAIFLDDLER-FALPDTiLTKNIAELSGGEKQR----ISLIRNlqfmPKVLLLDEITSALDESNKHNV 176
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 1472 WRAIRTAFKNKKRAALLTTHYMEEAEAvCDRV 1503
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1319-1491 |
6.21e-11 |
|
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: 63.67 E-value: 6.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMgYCPQTNPLWPDITLQEHFEIY 1398
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLL-YLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMSSgdmkevisrITKALDLK-----EHLqkTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD----PRAKQ 1469
Cdd:cd03231 98 HADHSDEQ---------VEEALARVglngfEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDkagvARFAE 166
|
170 180
....*....|....*....|..
gi 27368659 1470 HMwrAIRTAfknKKRAALLTTH 1491
Cdd:cd03231 167 AM--AGHCA---RGGMVVLTTH 183
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1323-1510 |
6.86e-11 |
|
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: 62.97 E-value: 6.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTsgkiflgdygshsNEDDEstkcmgycpqtnplWPDITLqehfeiygAVK 1402
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN-------------GDNDE--------------WDGITP--------VYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1403 GmssgdmkevisritkaldlkehlQKTvkKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNK 1482
Cdd:cd03222 67 P-----------------------QYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*...
gi 27368659 1483 KRAALLTTHYMEEAEAVCDRVaIMVSGQ 1510
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1288-1512 |
6.98e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 64.67 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1288 PAIMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTII------NILVGDVEpTSGKI-FLG 1360
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-----------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVR-VEGRVeFFN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1361 D--YGSHSNEDDESTKCMGYCPQTNpLWPdITLQEHFEiYGA--VKGMSSGDMKEVISRITKALDL----KEHLQKTVKK 1432
Cdd:PRK14258 74 QniYERRVNLNRLRRQVSMVHPKPN-LFP-MSVYDNVA-YGVkiVGWRPKLEIDDIVESALKDADLwdeiKHKIHKSALD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1433 LPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:PRK14258 151 LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENR 230
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1290-1464 |
7.81e-11 |
|
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: 66.88 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsned 1369
Cdd:TIGR03719 323 IEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE-------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 desTKCMGYCPQT-NPLWPDITLQEhfEIYGAVKGMSSGDmKEVISRIT------KALDlkehLQKTVKKLPAGIKRKLC 1442
Cdd:TIGR03719 384 ---TVKLAYVDQSrDALDPNKTVWE--EISGGLDIIKLGK-REIPSRAYvgrfnfKGSD----QQKKVGQLSGGERNRVH 453
|
170 180
....*....|....*....|..
gi 27368659 1443 FALSMLGNPQVTLLDEPSTGMD 1464
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1315-1564 |
9.61e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 64.62 E-value: 9.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1315 ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSnEDDESTKCMGYCPQtNPLWPDI--T 1390
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFS-KLQGIRKLVGIVFQ-NPETQFVgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1391 LQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQH 1470
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1471 MWRAIRTaFKNKKRAALLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGKGYfLEIKLKDWIENLEidRLQR-E 1549
Cdd:PRK13644 175 VLERIKK-LHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQT-LGLTPPSLIELAE--NLKMhG 249
|
250
....*....|....*
gi 27368659 1550 IQYIFPNASRQESFS 1564
Cdd:PRK13644 250 VVIPWENTSSPSSFA 264
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
490-646 |
1.25e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE----------IDEMFEARKMIG 559
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangIVYISEDRKRDG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 IcpqsdmnfdVL--TVEENLSILA----SVKGIPANNIiQEVQKVLLDLDMQAIK----DNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK10762 341 L---------VLgmSVKENMSLTAlryfSRAGGSLKHA-DEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGL 410
|
170
....*....|....*..
gi 27368659 630 LGNPKILLLDEPTAGMD 646
Cdd:PRK10762 411 MTRPKVLILDEPTRGVD 427
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1319-1529 |
1.32e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 66.00 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGSHSNEDDEST--KCMGYCPQTnplwPDI---TLQE 1393
Cdd:PRK11160 359 LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLN--GQPIADYSEAAlrQAISVVSQR----VHLfsaTLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 HFEIygAVKGMSSGDMKEVISRI--TKALDLKEHLQKTV----KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRA 1467
Cdd:PRK11160 433 NLLL--AAPNASDEALIEVLQQVglEKLLEDDKGLNAWLgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAET 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1468 KQHMWRAIRTAFKNKkrAALLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGkGYF 1529
Cdd:PRK11160 511 ERQILELLAEHAQNK--TVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG-RYY 568
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
488-691 |
1.33e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.96 E-value: 1.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVealRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQSDMN 567
Cdd:PRK09700 273 SRDRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRD 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 ---FDVLTVEENLSILASVK--------GIPANNI---IQEVQKVLLDLDMQAIKDNqAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK09700 350 ngfFPNFSIAQNMAISRSLKdggykgamGLFHEVDeqrTAENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 634 KILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1285-1540 |
1.44e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 1.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1285 EEKPAIMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVG--DVEPTSGKIFLGDY 1362
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE-----------ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1363 GSHSNEDDESTKCMGYCPQTNPL-WPDITLQEHFEIYGAVKGMSSGDMK-------EVISRITKALDLKEH-LQKTVKKL 1433
Cdd:CHL00131 72 SILDLEPEERAHLGIFLAFQYPIeIPGVSNADFLRLAYNSKRKFQGLPEldpleflEIINEKLKLVGMDPSfLSRNVNEG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1434 PAGIKRKLCFALSM-LGNPQVTLLDEPSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVC-DRVAIMVSGQL 1511
Cdd:CHL00131 152 FSGGEKKRNEILQMaLLDSELAILDETDSGLDIDALKIIAEGINK-LMTSENSIILITHYQRLLDYIKpDYVHVMQNGKI 230
|
250 260
....*....|....*....|....*....
gi 27368659 1512 RCIGTVQHLKSkfgkgyfLEIKLKDWIEN 1540
Cdd:CHL00131 231 IKTGDAELAKE-------LEKKGYDWLKQ 252
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
495-646 |
1.67e-10 |
|
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: 62.43 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMNFDVlTVE 574
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 575 ENLSILasvkgipanNIIQEVQkVLLDLDMQAIKDNqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03369 100 SNLDPF---------DEYSDEE-IYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
497-653 |
2.01e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.02 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcPPSDGFasIYGH-RVSEIDEMFEARKMI-GICPQSDMNFDVLTVE 574
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGY--IEGDiRISGFPKKQETFARIsGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLsILASVKGIPANNIIQE----VQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PLN03140 972 ESL-IYSAFLRLPKEVSKEEkmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
....*...
gi 27368659 646 DPCSRHIV 653
Cdd:PLN03140 1051 DARAAAIV 1058
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
492-646 |
2.12e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 2.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 492 ETVEALRNLSFDIY-------------EGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmI 558
Cdd:PRK10575 9 DTTFALRNVSFRVPgrtllhplsltfpAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-V 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GICPQSDMNFDVLTVEEnlsiLASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK10575 88 AYLPQQLPAAEGMTVRE----LVAIGRYPWHGALgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVA 163
|
170
....*....|....*.
gi 27368659 631 GNPKILLLDEPTAGMD 646
Cdd:PRK10575 164 QDSRCLLLDEPTSALD 179
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
507-671 |
2.46e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 65.29 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 507 GQITALLGHSGTGKSTLMNILCGLCPPSD--GFASIYGHRVSEidemfEARKMIGICPQSDMNFDVLTVEENL------- 577
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVRETLvfcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 578 ---SILASVKGIPANNIIQEVQkvLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH-IV 653
Cdd:PLN03211 169 lpkSLTKQEKILVAESVISELG--LTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246
|
170
....*....|....*...
gi 27368659 654 WNLLKYRKANRVTVFSTH 671
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMH 264
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1314-1504 |
2.58e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 62.88 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1314 VATKYVSFCVKKGEILGLLGPNGAGKSTIINIL--VGDVEPT---SGKIFLGDYGSHSNEDD--ESTKCMGYCPQT-NPL 1385
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNLYAPDVDpvEVRRRIGMVFQKpNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 WPDItlqeHFEI-YGA-VKGMSsGDMKEVISRITK--AL--DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEP 1459
Cdd:PRK14243 104 PKSI----YDNIaYGArINGYK-GDMDELVERSLRqaALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 1460 STGMDPRAKqhmwRAIRTAFKNKKR--AALLTTHYMEEAEAVCDRVA 1504
Cdd:PRK14243 179 CSALDPIST----LRIEELMHELKEqyTIIIVTHNMQQAARVSDMTA 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1319-1511 |
2.72e-10 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 62.59 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEI 1397
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIvFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEENLAM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGAVkgmssGDMKEVISRITKALDLKEHLQ----KTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWR 1473
Cdd:PRK11614 104 GGFF-----AERDQFQERIKWVYELFPRLHerriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 27368659 1474 AIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11614 179 TIEQ-LREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1319-1526 |
2.84e-10 |
|
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: 62.25 E-value: 2.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDiTLQEHFEiY 1398
Cdd:cd03251 21 ISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND-TVAENIA-Y 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAvkgmSSGDMKEVIS--RITKALDLKEHLQK---TV-----KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK 1468
Cdd:cd03251 99 GR----PGATREEVEEaaRAANAHEFIMELPEgydTVigergVKLSGGQRQRIAIARALLKDPPILILDEATSALDTESE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1469 QHMWRAIRTAFKNkkRAALLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGK 1526
Cdd:cd03251 175 RLVQAALERLMKN--RTTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEELLAQGGV 229
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1303-1557 |
3.24e-10 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 62.72 E-value: 3.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRkttkvATKYVSFCVKKGEILGLLGPNGAGKSTII----NILVGDVEPTSGKIFLGDY----GSHSNEDDESTK 1374
Cdd:PRK09984 12 KTFNQHQ-----ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTvqreGRLARDIRKSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1375 CMGYCPQTNPLWPDITLQEHFEIyGA----------VKGMSSGDMKEVISRITKaLDLKEHLQKTVKKLPAGIKRKLCFA 1444
Cdd:PRK09984 87 NTGYIFQQFNLVNRLSVLENVLI-GAlgstpfwrtcFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1445 LSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLkskf 1524
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF---- 240
|
250 260 270
....*....|....*....|....*....|...
gi 27368659 1525 gkgyfleiklkdwiENLEIDRLQREIQYIFPNA 1557
Cdd:PRK09984 241 --------------DNERFDHLYRSINRVEENA 259
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
455-712 |
3.98e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 3.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 455 INGNISLNEIVEP-VSSEFI---------GKEAIRISGIQKAYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLM 524
Cdd:PLN03232 582 VNANVSLQRIEELlLSEERIlaqnpplqpGAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 525 NILCGLCPPSDgfasiyghrvseiDEMFEARKMIGICPQSDMNFDVlTVEENLSILASVKGIPANNIIqEVQKVLLDLDM 604
Cdd:PLN03232 661 SAMLGELSHAE-------------TSSVVIRGSVAYVPQVSWIFNA-TVRENILFGSDFESERYWRAI-DVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 605 QAIKD-----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFST---HFMDe 675
Cdd:PLN03232 726 LPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTnqlHFLP- 804
|
250 260 270
....*....|....*....|....*....|....*..
gi 27368659 676 adiLADRKAVISQGMLKCVGSSIFLkSKWGIGYRLSM 712
Cdd:PLN03232 805 ---LMDRIILVSEGMIKEEGTFAEL-SKSGSLFKKLM 837
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
488-640 |
4.39e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 64.14 E-value: 4.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvseidemfeARKMIGIcpQSDMN 567
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAI--SSGLN 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 568 fDVLTVEENLSILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK13545 98 -GQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
495-696 |
4.61e-10 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 61.00 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlCP---PSDGfaSIY--GHRVSEIdEMFE-ARKMIGICPQSDMNF 568
Cdd:cd03217 14 EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEG--EILfkGEDITDL-PPEErARLGIFLAFQYPPEI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEEnlsilasvkgipanniiqevqkVLLDLDMqaikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03217 90 PGVKNAD----------------------FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 649 SRHIVWNLL-KYRKANRVTVFSTHFMDEAD-ILADRKAVISQGMLKCVGS 696
Cdd:cd03217 139 ALRLVAEVInKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1319-1529 |
4.92e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 4.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDIT------LQ 1392
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVrfnidpFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIyGAVKGMSSGDMKEVISRITKALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMW 1472
Cdd:PLN03232 1335 EHNDA-DLWEALERAHIKDVIDRNPFGLDAE--VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1473 RAIRTAFKNkkrAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYF 1529
Cdd:PLN03232 1412 RTIREEFKS---CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1323-1476 |
5.42e-10 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 60.72 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINIL-----VGDVEptsGKIFLGDYGShsneDDESTKCMGYCPQTNPLWPDITLQEHFEI 1397
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVREALRF 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1398 YGAVKGMSSGDmkevisritkaldlkehlqktvkklpagiKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIR 1476
Cdd:cd03232 103 SALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLK 152
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
497-646 |
5.96e-10 |
|
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: 64.07 E-value: 5.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEA-RKMIGICPQsdmnfDvlTVEE 575
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ--ASlRAAIGIVPQ-----D--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 576 NLSIlasvkgipANNII--------QEVQKVLldlDMQAIKDNQAK--------------KLSGGQKRKLslGIA--VLG 631
Cdd:COG5265 445 NDTI--------AYNIAygrpdaseEEVEAAA---RAAQIHDFIESlpdgydtrvgerglKLSGGEKQRV--AIArtLLK 511
|
170
....*....|....*
gi 27368659 632 NPKILLLDEPTAGMD 646
Cdd:COG5265 512 NPPILIFDEATSALD 526
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1319-1506 |
6.98e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 60.33 E-value: 6.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGS------HSNEDD------ESTKCMGycpqtnpLW 1386
Cdd:NF040873 11 VDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqRSEVPDslpltvRDLVAMG-------RW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 PDITLQEHFeiygavkgmsSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPR 1466
Cdd:NF040873 84 ARRGLWRRL----------TRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27368659 1467 AKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVcDRVAIM 1506
Cdd:NF040873 154 SRERIIALLA-EEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
493-689 |
8.60e-10 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 60.88 E-value: 8.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 493 TVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMfEARKMIGICPQSDMNFDV 570
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDER-LIRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 571 LTVEENLSI-LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK09493 92 LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27368659 650 RHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK09493 172 RHEVLKVMQDLAEEGMTmVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
500-647 |
1.12e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM--IGICPQSDMNFDVLtveENL 577
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMayLGHLPGLKADLSTL---ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 578 SILASVKGIPANniiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13543 104 HFLCGLHGRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
467-691 |
1.48e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 467 PVSSEFIGKEAIRISGIQKAYRKKNEtveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS 546
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAYQDNGF---SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 547 EiDEMFEARKMIgicpqSDMNFDVLTVEEnlsiLASVKGIPANNiiQEVQKVLLDLDMQ---AIKDNQAK--KLSGGQKR 621
Cdd:PRK10522 389 A-EQPEDYRKLF-----SAVFTDFHLFDQ----LLGPEGKPANP--ALVEKWLERLKMAhklELEDGRISnlKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1294-1517 |
1.55e-09 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 61.74 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDKKDFLHsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsneDDEst 1373
Cdd:PRK11153 6 NISKVFPQGGRTIH-------ALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLV---------DGQ-- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1374 kcmgycpqtnplwpDIT------LQE----------HFE------IYGAV------KGMSSGDMKeviSRITKALDLKEh 1425
Cdd:PRK11153 68 --------------DLTalsekeLRKarrqigmifqHFNllssrtVFDNValplelAGTPKAEIK---ARVTELLELVG- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1426 LQKTVKKLPA----------GIKRklcfALSMlgNPQVTLLDEPSTGMDPRAKqhmwRAIRTAFKNKKR----AALLTTH 1491
Cdd:PRK11153 130 LSDKADRYPAqlsggqkqrvAIAR----ALAS--NPKVLLCDEATSALDPATT----RSILELLKDINRelglTIVLITH 199
|
250 260
....*....|....*....|....*.
gi 27368659 1492 YMEEAEAVCDRVAIMVSGQLRCIGTV 1517
Cdd:PRK11153 200 EMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
496-689 |
1.62e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 60.32 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASiYGHR---VSEIDEMFEA-RKMI-----GICPQSDM 566
Cdd:PRK11701 21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-YRMRdgqLRDLYALSEAeRRRLlrtewGFVHQHPR 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 567 NFDVLTVEENLSILASVKGIPAN---NIIQE----VQKVLLDLDMQaikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:PRK11701 100 DGLRMQVSAGGNIGERLMAVGARhygDIRATagdwLERVEIDAARI---DDLPTTFSGGMQQRLQIARNLVTHPRLVFMD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 640 EPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11701 177 EPTGGLDVSVQARLLDLLRglVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
467-653 |
1.72e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 467 PVSSEFIGKEAIRISGIQKAYRKKnetVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGH 543
Cdd:PLN03140 154 PNAARNIAESALGMLGINLAKKTK---LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 544 RVSEidemFEARKMIGICPQSDMNFDVLTVEENLSILASVKGIPA----------------------------------- 588
Cdd:PLN03140 231 RLNE----FVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTrydllselarrekdagifpeaevdlfmkatamegv 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 589 -NNIIQEVQKVLLDLDM---QAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP--------CSRHIV 653
Cdd:PLN03140 307 kSSLITDYTLKILGLDIckdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyqivkCLQQIV 383
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1313-1522 |
1.80e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.49 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD--YGSHS--NEDD--ESTKCMGYCPQTNPLW 1386
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDvlLGGRSifNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 PDITLQEHFEIYGAVKGMSSGDMKEVI-SRITKA---LDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAqARLTEVglwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1463 MDPRAKQHMWRAIRTAfkNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:PRK14271 194 LDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
478-683 |
2.03e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.47 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYR-----KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmf 552
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 553 EARKmigicpqsDMNFDVLTV-EENLSILASVKGIPAnnIIQEVQKVLLDLDMQA-----------------IKDNQAKK 614
Cdd:PRK10419 82 AQRK--------AFRRDIQMVfQDSISAVNPRKTVRE--IIREPLRHLLSLDKAErlarasemlravdlddsVLDKRPPQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTH-------------FMDEADIL 679
Cdd:PRK10419 152 LSGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHdlrlverfcqrvmVMDNGQIV 231
|
....
gi 27368659 680 ADRK 683
Cdd:PRK10419 232 ETQP 235
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1294-1511 |
2.25e-09 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 60.86 E-value: 2.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYddkkdflHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKST---IINILvgdvE-PTSGKIFLGDYgshsned 1369
Cdd:COG1135 6 NLSKTF-------PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLL----ErPTSGSVLVDGV------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 destkcmgycpqtnplwpDIT------LQE----------HFE------IYGAV------KGMSSGDMKEvisRITKALD 1421
Cdd:COG1135 68 ------------------DLTalsereLRAarrkigmifqHFNllssrtVAENValpleiAGVPKAEIRK---RVAELLE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1422 L-----KEHlqktvkKLPA----------GIKRklcfALSMlgNPQVTLLDEPSTGMDPRAKQhmwrAIRTAFK--NKKR 1484
Cdd:COG1135 127 LvglsdKAD------AYPSqlsggqkqrvGIAR----ALAN--NPKVLLCDEATSALDPETTR----SILDLLKdiNREL 190
|
250 260
....*....|....*....|....*....
gi 27368659 1485 AA--LLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG1135 191 GLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1326-1520 |
2.26e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 60.19 E-value: 2.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1326 GEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEI-----YGA 1400
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 VKGMSSGDMKEVISRITkALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFK 1480
Cdd:PRK10575 117 LGRFGAADREKVEEAIS-LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27368659 1481 NKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK10575 196 ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1319-1511 |
3.15e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 60.11 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHFEI 1397
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdGELLTAENVWNLRRKIGMVFQNPDNQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRt 1477
Cdd:PRK13642 106 GMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVIH- 184
|
170 180 190
....*....|....*....|....*....|....*
gi 27368659 1478 AFKNKKRAALLT-THYMEEAeAVCDRVAIMVSGQL 1511
Cdd:PRK13642 185 EIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEI 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
489-657 |
3.20e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 60.36 E-value: 3.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 489 KKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGIC---PQ 563
Cdd:PRK11308 23 KPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVfqnPY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 564 SDMN-----FDVLtvEENLSILASVkgipanNIIQEVQKVLLDLDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK11308 103 GSLNprkkvGQIL--EEPLLINTSL------SAAERREKALAMMAKVGLRPEHYDRyphmFSGGQRQRIAIARALMLDPD 174
|
170 180
....*....|....*....|...
gi 27368659 635 ILLLDEPTAGMDPCSRHIVWNLL 657
Cdd:PRK11308 175 VVVADEPVSALDVSVQAQVLNLM 197
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1292-1511 |
3.63e-09 |
|
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: 60.07 E-value: 3.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKDFLHsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEP---TSGKIFLG--DYGSHS 1366
Cdd:COG0444 4 VRNLKVYFPTRRGVVK-------AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgeDLLKLS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1367 NEDDES--TKCMGYCPQ---T--NPLWP--DI---TLQEHfeiygavKGMSSgdmKEVISRITKALDL------KEHLqk 1428
Cdd:COG0444 77 EKELRKirGREIQMIFQdpmTslNPVMTvgDQiaePLRIH-------GGLSK---AEARERAIELLERvglpdpERRL-- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1429 tvKKLP----AGIKRKLCFALSMLGNPQVTLLDEPSTGMDP--RAK--QHMwRAIRTAFKNkkrAALLTTHYMEEAEAVC 1500
Cdd:COG0444 145 --DRYPhelsGGMRQRVMIARALALEPKLLIADEPTTALDVtiQAQilNLL-KDLQRELGL---AILFITHDLGVVAEIA 218
|
250
....*....|.
gi 27368659 1501 DRVAIMVSGQL 1511
Cdd:COG0444 219 DRVAVMYAGRI 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
497-646 |
3.93e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 3.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---------------------PPSDGFASIYGHrVSE-IDEMFEA 554
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdPPRNVEGTVYDF-VAEgIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIgicpqSDMNFDVLT--VEENLSILASVKGIPAN-------NIIQEVQKvLLDLDmqaiKDNQAKKLSGGQKRKLSL 625
Cdd:PRK11147 98 LKRY-----HDISHLVETdpSEKNLNELAKLQEQLDHhnlwqleNRINEVLA-QLGLD----PDAALSSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 27368659 626 GIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1313-1525 |
4.36e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.01 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGdveptsgkiFLGDYGS------HSNEDDEST--KCMGYCPQtNP 1384
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG---------FLPYQGSlkingiELRELDPESwrKHLSWVGQ-NP 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1385 LWPDITLQEHFEiygavkgMSSGDMKEviSRITKALDlKEHLQKTVKKLPAGIK---------------RKLCFALSMLG 1449
Cdd:PRK11174 433 QLPHGTLRDNVL-------LGNPDASD--EQLQQALE-NAWVSEFLPLLPQGLDtpigdqaaglsvgqaQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1450 NPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKkrAALLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
479-646 |
4.67e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 59.23 E-value: 4.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKNETVEalRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmI 558
Cdd:PRK10253 7 RLRGEQLTLGYGKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-I 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 559 GICPQSDMNFDVLTVEEnlsiLASVKGIPANNII--------QEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK10253 84 GLLAQNATTPGDITVQE----LVARGRYPHQPLFtrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170
....*....|....*.
gi 27368659 631 GNPKILLLDEPTAGMD 646
Cdd:PRK10253 160 QETAIMLLDEPTTWLD 175
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1319-1510 |
5.20e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 57.86 E-value: 5.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGShsneddestkcMGYCPQTnplwPDI---TLQE-- 1393
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--GS-----------IAYVSQE----PWIqngTIREni 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1394 ------HFEIYGAV----------KGMSSGDMKEVISR-ITkaldlkehlqktvkkLPAGIKRKLCFALSMLGNPQVTLL 1456
Cdd:cd03250 87 lfgkpfDEERYEKVikacalepdlEILPDGDLTEIGEKgIN---------------LSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 1457 DEPSTGMDPRAKQHMW-RAIRTAFKNKKrAALLTTHYMEEAEAvCDRVAIMVSGQ 1510
Cdd:cd03250 152 DDPLSAVDAHVGRHIFeNCILGLLLNNK-TRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1317-1523 |
6.13e-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: 59.10 E-value: 6.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEpTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDiTLQEHFE 1396
Cdd:cd03289 21 ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSG-TFRKNLD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGA------VKGMSSGDMKEVISRITKALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQH 1470
Cdd:cd03289 99 PYGKwsdeeiWKVAEEVGLKSVIEQFPGQLDFV--LVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1471 MWRAIRTAFKNKkrAALLTTHYMeEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:cd03289 177 IRKTLKQAFADC--TVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
486-671 |
6.57e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 6.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 486 AYRKKNETveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSD 565
Cdd:PRK11176 350 TYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY-TLASLRNQVALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 MNFDVlTVEENL-----------SILASVKGIPANNIIQEVQKVlLDldmQAIKDNQAkKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK11176 427 HLFND-TIANNIayarteqysreQIEEAARMAYAMDFINKMDNG-LD---TVIGENGV-LLSGGQRQRIAIARALLRDSP 500
|
170 180 190
....*....|....*....|....*....|....*..
gi 27368659 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1317-1511 |
6.63e-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: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsnedDEstKCMgycpqtnPLWPDITLQEHFE 1396
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLL----------DG--KPI-------SQYEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVKGMSSGDMKEVIS---------RITKALDlKEHLQKTVKKLPAGI---------------KRKLCFALSMLGNPQ 1452
Cdd:cd03248 92 LVGQEPVLFARSLQDNIAyglqscsfeCVKEAAQ-KAHAHSFISELASGYdtevgekgsqlsggqKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1453 VTLLDEPSTGMDPRAKQHMWRAIRTAfkNKKRAALLTTHYMEEAEAVcDRVAIMVSGQL 1511
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1319-1530 |
6.71e-09 |
|
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: 58.27 E-value: 6.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWpDITLQEHfeIY 1398
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRDN--IA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAVKGMssgDMKEVI--SRITKA----LDLKEHLQKTVKK----LPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAK 1468
Cdd:cd03252 98 LADPGM---SMERVIeaAKLAGAhdfiSELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1469 QHMWRAIRTAFKNkkRAALLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGKGYFL 1530
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1319-1499 |
9.07e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 57.49 E-value: 9.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEP---TSGKIFLgdygshsneDDES-------TKCMGYCPQTNPLWPd 1388
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLL---------NGRRltalpaeQRRIGILFQDDLLFP- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1389 itlqeHFEI-----YGAVKGMSSGDMKEvisRITKALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPS 1460
Cdd:COG4136 90 -----HLSVgenlaFALPPTIGRAQRRA---RVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPF 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1461 TGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAV 1499
Cdd:COG4136 162 SKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAA 200
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-642 |
9.40e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 60.08 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILcGLCPPSDGFASiyghrvSEIdeMFEARK 556
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPS------GSI--LFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 MIGiCPQSDMN----------FD--------VLTVEENLS-ILASVKGIPAnniiQEVQKVLLD-LDMQAIKDNQAK--- 613
Cdd:COG4172 78 LLG-LSERELRrirgnriamiFQepmtslnpLHTIGKQIAeVLRLHRGLSG----AAARARALElLERVGIPDPERRlda 152
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 614 ---KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG4172 153 yphQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1290-1464 |
9.50e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.13 E-value: 9.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygshsned 1369
Cdd:PRK11819 325 IEAENLSKSFGDR-----------LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE-------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 desTKCMGYCPQT-NPLWPDITLQEhfEIYGAVKGMSSGDmKEVISRIT------KALDlkehLQKTVKKLPAGIKRKLC 1442
Cdd:PRK11819 386 ---TVKLAYVDQSrDALDPNKTVWE--EISGGLDIIKVGN-REIPSRAYvgrfnfKGGD----QQKKVGVLSGGERNRLH 455
|
170 180
....*....|....*....|....*
gi 27368659 1443 FALsML---GNpqVTLLDEPSTGMD 1464
Cdd:PRK11819 456 LAK-TLkqgGN--VLLLDEPTNDLD 477
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
479-681 |
1.40e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.89 E-value: 1.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 479 RISGIQKAYRKKNETVE--ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCG--LCPPSDGFASIyghrvseidemfea 554
Cdd:COG2401 26 RVAIVLEAFGVELRVVEryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV-------------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 rkmigicpqSDMNFDV-LTVEENLSILASVKgipanniiqevQKVLLdLDMQAIKDNQA-----KKLSGGQKRKLSLGIA 628
Cdd:COG2401 92 ---------PDNQFGReASLIDAIGRKGDFK-----------DAVEL-LNAVGLSDAVLwlrrfKELSTGQKFRFRLALL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 629 VLGNPKILLLDEPTAGMDP-CSRHIVWNLLKY-RKANRVTVFSTHfmdEADILAD 681
Cdd:COG2401 151 LAERPKLLVIDEFCSHLDRqTAKRVARNLQKLaRRAGITLVVATH---HYDVIDD 202
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
476-647 |
1.52e-08 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 57.50 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 476 EAIRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvsEIDEMFEAR 555
Cdd:COG4598 7 PALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGG----EEIRLKPDR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 556 KmiGICPQSDM---------------NFDV---LTVEENLsILA--SVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKL 615
Cdd:COG4598 79 D--GELVPADRrqlqrirtrlgmvfqSFNLwshMTVLENV-IEApvHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHL 155
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4598 156 SGGQQQRAAIARALAMEPEVMLFDEPTSALDP 187
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1311-1511 |
1.62e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 57.89 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1311 TTKVATKYVSFCVKKGEILGLLGPNGAGKSTI---IN-ILVGDVEPTSGKIFLGDYGSHSNEDDESTKcMGYCPQTnplw 1386
Cdd:PRK13640 18 SKKPALNDISFSIPRGSWTALIGHNGSGKSTIsklINgLLLPDDNPNSKITVDGITLTAKTVWDIREK-VGIVFQN---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 PD-----ITLQEHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:PRK13640 93 PDnqfvgATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 1462 GMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEaVCDRVAIMVSGQL 1511
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1303-1493 |
1.91e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.81 E-value: 1.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRKttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDEST---KCMGYC 1379
Cdd:PRK10908 9 KAYLGGRQ----ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflrRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1380 PQTNPLWPDITLQEHFEIYGAVKGMSSGDMKEvisRITKALDlKEHLQKTVKKLP----AGIKRKLCFALSMLGNPQVTL 1455
Cdd:PRK10908 85 FQDHHLLMDRTVYDNVAIPLIIAGASGDDIRR---RVSAALD-KVGLLDKAKNFPiqlsGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190
....*....|....*....|....*....|....*...
gi 27368659 1456 LDEPSTGMDPRAKQHMWRAIRtAFKNKKRAALLTTHYM 1493
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFE-EFNRVGVTVLMATHDI 197
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1320-1498 |
1.92e-08 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 56.35 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGSHSNEDDEStkcmgycPQTNPLW--------PDITL 1391
Cdd:PRK13538 21 SFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQ--GEPIRRQRDE-------YHQDLLYlghqpgikTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1392 QEHFEIYGAVKGMSSGDmkevisRITKALD---LK--EHLqkTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDpr 1466
Cdd:PRK13538 92 LENLRFYQRLHGPGDDE------ALWEALAqvgLAgfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-- 161
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 1467 akqhmwrairtafknKKRAALLTTHYMEEAEA 1498
Cdd:PRK13538 162 ---------------KQGVARLEALLAQHAEQ 178
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1317-1509 |
1.95e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 58.91 E-value: 1.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGY-CPQTNPLWPDITLQEHF 1395
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1396 eIYGAVKGM-SSGDMKEVISRITKALDLkehlqktvkKLPAG-----------IKRKLcfalsmLGNPQVTLLDEPSTGM 1463
Cdd:PRK15439 108 -LFGLPKRQaSMQKMKQLLAALGCQLDL---------DSSAGslevadrqiveILRGL------MRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 1464 DPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK15439 172 TPAETERLFSRIR-ELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1319-1514 |
2.05e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 58.59 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdYGSHSN----------------EDDESTKCMGYCPQT 1382
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITL--HGKKINnhnaneainhgfalvtEERRSTGIYAYLDIG 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1383 -NPLWPDITlqehfEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKT-VKKLPAGIKRKLCFALSMLGNPQVTLLDEPS 1460
Cdd:PRK10982 345 fNSLISNIR-----NYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1461 TGMDPRAKQHMWRAIrTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK10982 420 RGIDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
486-694 |
2.43e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 58.56 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 486 AYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILCGL-CPP---SDGFASIYGHRVSEIDEMfEARK---- 556
Cdd:PRK15134 14 AFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLLHASEQ-TLRGvrgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 ---MIGICPQSDMNfDVLTVEENLS-ILASVKGI---PANNiiqevqKVLLDLDMQAIKdnQAKK--------LSGGQKR 621
Cdd:PRK15134 93 kiaMIFQEPMVSLN-PLHTLEKQLYeVLSLHRGMrreAARG------EILNCLDRVGIR--QAAKrltdyphqLSGGERQ 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGmlKCV 694
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLADRVAVMQNG--RCV 236
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
957-1224 |
2.68e-08 |
|
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: 57.79 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 957 LNVVQSEKDYVFTAVFNSTMVYSLPVMMNIISNYY----LYHLNVTDTIQIWSTPFIQEITDiVFKVELYFQAALLGIIV 1032
Cdd:pfam12698 90 SKDLLKGESATVTVYINSSNLLVSKLILNALQSLLqqlnASALVLLLEALSTSAPIPVESTP-LFNPQSGYAYYLVGLIL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1033 TAM----PPYFAMENAENHKIKAYTQLKLSGLLPSAYWIGQAVVDIPLFFVVLTLMLgsLFAFHHGLYFYpvKFLAVVFC 1108
Cdd:pfam12698 169 MIIiligAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL--LLLFGIGIPFG--NLGLLLLL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1109 LIAYVPSVILFTYIASFTFKKILNTKEFwSFIYSVTALACVAVTEITFFLGYGVTAVFHYtfciaIPIYPLLgclisfik 1188
Cdd:pfam12698 245 FLLYGLAYIALGYLLGSLFKNSEDAQSI-IGIVILLLSGFFGGLFPLEDPPSFLQWIFSI-----IPFFSPI-------- 310
|
250 260 270
....*....|....*....|....*....|....*.
gi 27368659 1189 gswkNIPKTENAYNPWDRLLVAVIMPYLQCVLWIFL 1224
Cdd:pfam12698 311 ----DGLLRLIYGDSLWEIAPSLIILLLFAVVLLLL 342
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1319-1511 |
2.78e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsNEDDESTKCmgycPQtNPLWPDIT-LQEHFEI 1397
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTL-------DGHEVVTRS----PQ-DGLANGIVyISEDRKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGAVKGMS---------------------SGDMKEVISRITKALDLKE-HLQKTVKKLPAGIKRKLCFALSMLGNPQVTL 1455
Cdd:PRK10762 339 DGLVLGMSvkenmsltalryfsraggslkHADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1456 LDEPSTGMDPRAKQHMWRAIrTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1317-1491 |
2.78e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGdvEPTSGKIfLGDY--GSHSNEDDESTKCMGYCPQTNPLWPDITLQEH 1394
Cdd:PLN03140 897 REVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI-EGDIriSGFPKKQETFARISGYCEQNDIHSPQVTVRES 973
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FeIYGAV----KGMSSGDMKEVISRITKALDLkEHLQKTVKKLPaGI-------KRKLCFALSMLGNPQVTLLDEPSTGM 1463
Cdd:PLN03140 974 L-IYSAFlrlpKEVSKEEKMMFVDEVMELVEL-DNLKDAIVGLP-GVtglsteqRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*...
gi 27368659 1464 DPRAKQHMWRAIRTAFkNKKRAALLTTH 1491
Cdd:PLN03140 1051 DARAAAIVMRTVRNTV-DTGRTVVCTIH 1077
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
480-646 |
3.32e-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: 58.41 E-value: 3.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 480 ISGIQKAYRKKNETveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKMIG 559
Cdd:TIGR03719 7 MNRVSKVVPPKKEI---LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------------EARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 IC-------PQSDMNFDVL-TVEENLS----ILASVKGIPAN-------------------NIIQEVQkvLLDLD----- 603
Cdd:TIGR03719 68 IKvgylpqePQLDPTKTVReNVEEGVAeikdALDRFNEISAKyaepdadfdklaaeqaelqEIIDAAD--AWDLDsqlei 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27368659 604 -MQAIK----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 146 aMDALRcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1328-1517 |
3.49e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 57.58 E-value: 3.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1328 ILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDygsHSNEDDESTKCM-------GYCPQTNPLWPditlqeHFEIYGA 1400
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAEKGICLppekrriGYVFQDARLFP------HYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1401 VK-GMsSGDMKEVISRITKALDLkEHLqktVKKLPA----GIKRKLCFALSMLGNPQVTLLDEPSTGMD-PRAKQHMWRA 1474
Cdd:PRK11144 97 LRyGM-AKSMVAQFDKIVALLGI-EPL---LDRYPGslsgGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPYL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27368659 1475 IRTAfKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTV 1517
Cdd:PRK11144 172 ERLA-REINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1511 |
4.22e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 4.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgDYGSHSNED 1369
Cdd:PRK13651 3 IKVKNIVKIFNKKL------PTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWP----------DITLQ----------EHFE-------IYGAVK-GMSSGDMKEVISRITKALD 1421
Cdd:PRK13651 74 KKKTKEKEKVLEKLVIQKtrfkkikkikEIRRRvgvvfqfaeyQLFEqtiekdiIFGPVSmGVSKEEAKKRAAKYIELVG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1422 LKE-HLQKTVKKLPAGIKRKLCFA--LSMlgNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKrAALLTTHYMEEAEA 1498
Cdd:PRK13651 154 LDEsYLQRSPFELSGGQKRRVALAgiLAM--EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLE 230
|
250
....*....|...
gi 27368659 1499 VCDRVAIMVSGQL 1511
Cdd:PRK13651 231 WTKRTIFFKDGKI 243
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1303-1506 |
4.34e-08 |
|
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: 55.52 E-value: 4.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDF-LHSRKTTK-VATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygSHSNEDDESTKC----- 1375
Cdd:COG4778 12 KTFtLHLQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV----RHDGGWVDLAQAsprei 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1376 -------MGYC-------PQTNPLwpDITLQEHFEiygavKGMSSGDMKEVISRITKALDLKEHLQKTVkklPA----GI 1437
Cdd:COG4778 88 lalrrrtIGYVsqflrviPRVSAL--DVVAEPLLE-----RGVDREEARARARELLARLNLPERLWDLP---PAtfsgGE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 1438 KRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAfknKKR-AALLT-THYMEEAEAVCDRVAIM 1506
Cdd:COG4778 158 QQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA---KARgTAIIGiFHDEEVREAVADRVVDV 225
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
473-692 |
4.57e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 4.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 473 IGKEAIRISGIQkAYRKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-PSDGFASIYGHRVS----- 546
Cdd:PRK13549 255 IGEVILEVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpq 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 547 -----EIDEMFEARKMIGICPqsdmnfdVLTVEENLSiLASVKGIPANNIIQEVQKvlLDLDMQAIKDNQAK-------- 613
Cdd:PRK13549 334 qaiaqGIAMVPEDRKRDGIVP-------VMGVGKNIT-LAALDRFTGGSRIDDAAE--LKTILESIQRLKVKtaspelai 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 614 -KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHfMDEADILADRKAVISQG 689
Cdd:PRK13549 404 aRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI-NQLVQQgvaIIVISSE-LPEVLGLSDRVLVMHEG 481
|
...
gi 27368659 690 MLK 692
Cdd:PRK13549 482 KLK 484
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1326-1467 |
5.17e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.97 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1326 GEILGLLGPNGAGKSTIINILVGDVEPTS--GKIFLGDygshSNEDDESTKCMGYCPQTNPLWPDITLQEHFeIYGAVKG 1403
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANN----RKPTKQILKRTGFVTQDDILYPHLTVRETL-VFCSLLR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1404 MSSGDMKEVISRITKALDLKEHLQKT---------VKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRA 1467
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1290-1511 |
6.65e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.75 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKKdflhsrkttkvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:PRK10619 6 LNVIDLHKRYGEHE-----------VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQ-EHFEIYG-------------AVKGMSSGDMKEVISRITKALDLKEHLQ-KTVKKLP 1434
Cdd:PRK10619 75 KDGQLKVADKNQLRLLRTRLTMVfQHFNLWShmtvlenvmeapiQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 1435 AGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRaIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10619 155 GGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1292-1366 |
7.08e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 7.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1292 VYNLHKEYDDKKDFLHsRKTTKvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-------GDYGS 1364
Cdd:PRK15112 7 VRNLSKTFRYRTGWFR-RQTVE-AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfGDYSY 84
|
..
gi 27368659 1365 HS 1366
Cdd:PRK15112 85 RS 86
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1319-1510 |
7.55e-08 |
|
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: 54.58 E-value: 7.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPT---SGKIflgDYGSHSNeDDESTKCMG---YCPQTNPLWPDITLQ 1392
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDI---HYNGIPY-KEFAEKYPGeiiYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIygavkgmssgdmkevisritkALDLKEHlqKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMW 1472
Cdd:cd03233 102 ETLDF---------------------ALRCKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27368659 1473 RAIRTaFKNKKRAALLTTHYM--EEAEAVCDRVAIMVSGQ 1510
Cdd:cd03233 159 KCIRT-MADVLKTTTFVSLYQasDEIYDLFDKVLVLYEGR 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1323-1511 |
9.34e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 54.71 E-value: 9.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTI---INILVgdvEPTSGKIFLGDYGSHSNEDDEST--KCMGYCPQTNPLWPDITLQEHFeI 1397
Cdd:PRK09493 24 IDQGEVVVIIGPSGSGKSTLlrcINKLE---EITSGDLIVDGLKVNDPKVDERLirQEAGMVFQQFYLFPHLTALENV-M 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGA--VKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAI 1475
Cdd:PRK09493 100 FGPlrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVM 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 1476 RTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK09493 180 QD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
494-695 |
9.78e-08 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 56.39 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQS---DMNFDV 570
Cdd:PRK09536 16 TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-AASRRVASVPQDtslSFEFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 571 LTVEE-----NLSILASVKgiPANNiiQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PRK09536 95 RQVVEmgrtpHRSRFDTWT--ETDR--AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27368659 646 DpcSRHIVWNLLKYRK---ANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK09536 171 D--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1328-1515 |
1.02e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 55.40 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1328 ILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNED----DESTKCMGYCPQTNPLWPDITlqehFEIYGAVK 1402
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWqGKPLDYSKRGllalRQQVATVFQDPEQQIFYTDID----SDIAFSLR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1403 GMSSGDmKEVISRITKAL---DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAF 1479
Cdd:PRK13638 105 NLGVPE-AEITRRVDEALtlvDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIV 183
|
170 180 190
....*....|....*....|....*....|....*.
gi 27368659 1480 KNKKRaALLTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK13638 184 AQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
478-642 |
1.09e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.55 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 478 IRISGIQKAYrkknETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:PRK10762 5 LQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----FNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 558 -----IGICPQsDMNF-DVLTVEENL----SILASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK10762 76 sqeagIGIIHQ-ELNLiPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170
....*....|....*
gi 27368659 628 AVLGNPKILLLDEPT 642
Cdd:PRK10762 155 VLSFESKVIIMDEPT 169
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1313-1511 |
1.20e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 54.67 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQ 1392
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIYGAV----KGMSSGDMKEVISRITKAL-------DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPST 1461
Cdd:PRK14246 103 PHLSIYDNIayplKSHGIKEKREIKKIVEECLrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 1462 GMDPRAKQHMWRAIrTAFKNKKrAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK14246 183 MIDIVNSQAIEKLI-TELKNEI-AIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1308-1464 |
1.21e-07 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 54.47 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1308 SRKTTKVaTKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQtNPLWP 1387
Cdd:cd03249 12 SRPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQ-EPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1388 DITLQEHFEiYGAvkgmSSGDMKEVISRITKA------LDLKEHLQKTV----KKLPAGIKRKLCFALSMLGNPQVTLLD 1457
Cdd:cd03249 90 DGTIAENIR-YGK----PDATDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLD 164
|
....*..
gi 27368659 1458 EPSTGMD 1464
Cdd:cd03249 165 EATSALD 171
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
488-646 |
1.25e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.04 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcpPSDGFA-------SIYGHRVSEIDEMFeaRKMIGI 560
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHigvegviTYDGITPEEIKKHY--RGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 561 CPQSDMNFDVLTVEENLSILASVKGiPANNII----QEVQKVLLDLDMQA----------IKDNQAKKLSGGQKRKLSLG 626
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKT-PQNRPDgvsrEEYAKHIADVYMATyglshtrntkVGNDFVRGVSGGERKRVSIA 221
|
170 180
....*....|....*....|
gi 27368659 627 IAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLD 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-658 |
1.44e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 55.48 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 490 KNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEARK---MIGICPQS 564
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSdiqMIFQDPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNfDVLTVEEnlsilasvkgipannIIQEVQKVLL-DLDMQAIKD---NQAKKL--------------SGGQKRKLSLG 626
Cdd:PRK15079 110 SLN-PRMTIGE---------------IIAEPLRTYHpKLSRQEVKDrvkAMMLKVgllpnlinryphefSGGQCQRIGIA 173
|
170 180 190
....*....|....*....|....*....|..
gi 27368659 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK15079 174 RALILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1317-1522 |
1.53e-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: 54.86 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygSHSNEddestkcMGYCPQTNPLWPDiTLQEHFe 1396
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI------KHSGR-------ISFSSQFSWIMPG-TIKENI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAvkgmsSGDMKEVISrITKALDLKEHLQKTVKK-----------LPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:cd03291 119 IFGV-----SYDEYRYKS-VVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1466 RAKQHMWRA-IRTAFKNKKRaaLLTTHYMEEAEaVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTR--ILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQS 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1319-1512 |
1.75e-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: 55.99 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPT-SGKIFL-GDYGSHSNEDD----------ESTKCMGYCPQTNpLW 1386
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFInGKPVDIRNPAQairagiamvpEDRKRHGIVPILG-VG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 PDITLQEhFEIYGAVKGMSSGDMKEVISRITKALDLKE-HLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:TIGR02633 358 KNITLSV-LKSFCFKMRIDAAAELQIIGSAIQRLKVKTaSPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 1466 RAKQHMWRAIrTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:TIGR02633 437 GAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1317-1523 |
1.82e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.46 E-value: 1.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIflgdygSHSNEddestkcMGYCPQTNPLWPDiTLQEHFe 1396
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI------KHSGR-------ISFSPQTSWIMPG-TIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 iygaVKGMSSGDMKevISRITKALDLKEHLQKTVKK-----------LPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:TIGR01271 508 ----IFGLSYDEYR--YTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1466 RAKQHMW-RAIRTAFKNKKRaaLLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:TIGR01271 582 VTEKEIFeSCLCKLMSNKTR--ILVTSKLEHLKKA-DKILLLHEGVCYFYGTFSELQAK 637
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-646 |
1.95e-07 |
|
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: 55.85 E-value: 1.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEID--EMFEARKMIGIC---P 562
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrrALRPLRRRMQVVfqdP 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 563 QSDMN--FDVL-TVEENLSILAsvKGIPANNIIQEVQKVL----LDLDMQaikDNQAKKLSGGQKRKLSlgIA---VLgN 632
Cdd:COG4172 372 FGSLSprMTVGqIIAEGLRVHG--PGLSAAERRARVAEALeevgLDPAAR---HRYPHEFSGGQRQRIA--IAralIL-E 443
|
170
....*....|....
gi 27368659 633 PKILLLDEPTAGMD 646
Cdd:COG4172 444 PKLLVLDEPTSALD 457
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1317-1525 |
2.04e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 55.88 E-value: 2.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshSNEDDESTKCMGYCPQTNplwpdITLQEHFE 1396
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL------DGVPLVQYDHHYLHRQVA-----LVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1397 IYGAVK-----GMSSGDMKEV------------ISRITKALD--LKEHLQktvkKLPAGIKRKLCFALSMLGNPQVTLLD 1457
Cdd:TIGR00958 567 FSGSVReniayGLTDTPDEEImaaakaanahdfIMEFPNGYDteVGEKGS----QLSGGQKQRIAIARALVRKPRVLILD 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1458 EPSTGMDPRAKQhmwrAIRTAFKNKKRAALLTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:TIGR00958 643 EATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
497-697 |
2.55e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.94 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemfeARKMIGICPQSD--MN------- 567
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-------RVW-------AERSIAYVPQQAwiMNatvrgni 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 --FDvltvEENLSILASVkgipanniiqeVQKVLLDLDMQAIKD-------NQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PTZ00243 742 lfFD----EEDAARLADA-----------VRVSQLEADLAQLGGgleteigEKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 639 DEPTAGMDP-CSRHIVWNLLKYRKANRVTVFSTHfmdEADIL--ADRKAVISQGMLKCVGSS 697
Cdd:PTZ00243 807 DDPLSALDAhVGERVVEECFLGALAGKTRVLATH---QVHVVprADYVVALGDGRVEFSGSS 865
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1287-1359 |
2.80e-07 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 54.35 E-value: 2.80e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1287 KPAIMVYNLHKEYDDKKDFLhSRKTTKV-ATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:COG4608 5 EPLLEVRDLKKHFPVRGGLF-GRTVGVVkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILF 77
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1329-1464 |
3.62e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.25 E-value: 3.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1329 LGLLGPNGAGKSTIINILVGDVEPTSGKIF------LGDYGSHSNED-DESTKCMGYCPQTNPLWPDITLQEHFEIYGav 1401
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrMAVFSQHHVDGlDLSSNPLLYMMRCFPGVPEQKLRAHLGSFG-- 615
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1402 kgmssgdmkevisrITKALDLKehlqkTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PLN03073 616 --------------VTGNLALQ-----PMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
455-696 |
3.66e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.51 E-value: 3.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 455 INGNISLNEIVEPVSSEF----------IGKEAIRISGIQKAYRKKNETvEALRNLSFDIYEGQITALLGHSGTGKSTLM 524
Cdd:PLN03130 582 VNANVSLKRLEELLLAEErvllpnpplePGLPAISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 525 NILCGLCPP-SDGFASIYGH--RVSEIDEMFEArkmigicpqsdmnfdvlTVEENLSILASVKGIPANNIIqEVQKVLLD 601
Cdd:PLN03130 661 SAMLGELPPrSDASVVIRGTvaYVPQVSWIFNA-----------------TVRDNILFGSPFDPERYERAI-DVTALQHD 722
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 602 LDMQAIKD-----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSRHIVWNLLK--YRKANRVTVFST-HF 672
Cdd:PLN03130 723 LDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKdeLRGKTRVLVTNQlHF 802
|
250 260
....*....|....*....|....
gi 27368659 673 MDEadilADRKAVISQGMLKCVGS 696
Cdd:PLN03130 803 LSQ----VDRIILVHEGMIKEEGT 822
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
488-646 |
4.15e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 488 RKKNETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSDMN 567
Cdd:PLN03232 1243 RYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSPVL 1321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 FDVlTVEENLSILAS------VKGIPANNIIQEVQKVLLDLDMQAIKDNQakKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PLN03232 1322 FSG-TVRFNIDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEGGE--NFSVGQRQLLSLARALLRRSKILVLDEA 1398
|
....*
gi 27368659 642 TAGMD 646
Cdd:PLN03232 1399 TASVD 1403
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
497-667 |
4.21e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 51.39 E-value: 4.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFasiyghrvseidemfearkmIGICPQSDMNFdvltveen 576
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR--------------------IGMPEGEDLLF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 lsilasvkgIPanniiqevQKVLLDLD--MQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVW 654
Cdd:cd03223 69 ---------LP--------QRPYLPLGtlREQLIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131
|
170
....*....|...
gi 27368659 655 NLLKYRKANRVTV 667
Cdd:cd03223 132 QLLKELGITVISV 144
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1317-1515 |
5.41e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 52.92 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIIN-----ILVGDVEPTSGKIFLGDYGSHSNEDD--ESTKCMGYCPQTNPLWPDI 1389
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVRLFGRNIYSPDVDpiEVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1390 TLQEHFEIYGAVKGMSSGDmKEVISRITKAL-------DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSK-KELDERVEWALkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1463 MDPRAKQHMWRAIrtaFKNKKRAAL-LTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK14267 180 IDPVGTAKIEELL---FELKKEYTIvLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1319-1494 |
5.50e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 54.92 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVgDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQT------------NPL- 1385
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQKvfifsgtfrknlDPYe 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 -WPDitlQEHFEIYGAVkgmssgDMKEVISRITKALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:TIGR01271 1317 qWSD---EEIWKVAEEV------GLKSVIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190
....*....|....*....|....*....|
gi 27368659 1465 PRAKQHMWRAIRTAFKNKkrAALLTTHYME 1494
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSNC--TVILSEHRVE 1413
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1294-1360 |
5.78e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 5.78e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1294 NLHKEYDDK---KDFlhsrkttkvatkyvSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG 1360
Cdd:PRK11147 324 NVNYQIDGKqlvKDF--------------SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG 379
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1319-1510 |
5.94e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLG---DYGShSNEDDESTKCMGY--------CPQTNPLW 1386
Cdd:PRK10982 17 VNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlFQGkeiDFKS-SKEALENGISMVHqelnlvlqRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1387 pditLQEHfeiygAVKGM--SSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PRK10982 96 ----LGRY-----PTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 1465 PRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:PRK10982 167 EKEVNHLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1319-1525 |
6.76e-07 |
|
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: 54.57 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGdyGShsneddestkcMGYCPQTNPLWPDiTLQEHFeIY 1398
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMK--GS-----------VAYVPQQAWIQND-SLRENI-LF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GavKGMSSGDMKEVISRITKALDLK--------EHLQKTVkKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQH 1470
Cdd:TIGR00957 722 G--KALNEKYYQQVLEACALLPDLEilpsgdrtEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1471 MWRAI---RTAFKNKKRaaLLTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:TIGR00957 799 IFEHVigpEGVLKNKTR--ILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1309-1491 |
7.32e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 7.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1309 RKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVepTSGKIFLGDYGSHSNEDDES-TKCMGYCPQTNPLWP 1387
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSSfQRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1388 DITLQEHFEIYGAVKGMSSGDMKE---VISRITKALDLKEHLQKTVKKLPAGI----KRKLCFALSMLGNPQVTL-LDEP 1459
Cdd:TIGR00956 850 TSTVRESLRFSAYLRQPKSVSKSEkmeYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....
gi 27368659 1460 STGMDPRAKqhmWRAIRTAFK--NKKRAALLTTH 1491
Cdd:TIGR00956 930 TSGLDSQTA---WSICKLMRKlaDHGQAILCTIH 960
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-696 |
9.39e-07 |
|
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: 54.18 E-value: 9.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSDMnFDVLTVEEN 576
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAW-IQNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 LsILASVKGIPANNIIQEVQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSR 650
Cdd:TIGR00957 719 I-LFGKALNEKYYQQVLEACALLPDLEILPSGDRteigeKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVGK 797
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27368659 651 HIVWNLL--KYRKANRVTVFSTH---FMDEADILadrkAVISQGMLKCVGS 696
Cdd:TIGR00957 798 HIFEHVIgpEGVLKNKTRILVTHgisYLPQVDVI----IVMSGGKISEMGS 844
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1323-1510 |
1.01e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 53.47 E-value: 1.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHF----EI 1397
Cdd:PRK10762 27 VYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIflgrEF 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1398 YGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAG------IKRKLCFalsmlgNPQVTLLDEPSTGMDPRAKQHM 1471
Cdd:PRK10762 107 VNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGeqqmveIAKVLSF------ESKVIIMDEPTDALTDTETESL 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 27368659 1472 WRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:PRK10762 181 FRVIR-ELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1308-1508 |
1.10e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1308 SRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVE--PTSGKIFLGDygshsneddestkcmgycpqtNPL 1385
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPD---------------------NQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 WPDITLQEHFEIYGAVKgmssgDMKEVISRI---TKALdlkehLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTG 1462
Cdd:COG2401 97 GREASLIDAIGRKGDFK-----DAVELLNAVglsDAVL-----WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27368659 1463 MDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVS 1508
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
1.21e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 51.10 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQSDMNfDVLTVEEN 576
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRSGIN-PYLTLREN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 577 lsilaSVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS-RHIVWN 655
Cdd:PRK13540 95 -----CLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSlLTIITK 169
|
170
....*....|....*.
gi 27368659 656 LLKYRKANRVTVFSTH 671
Cdd:PRK13540 170 IQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1319-1533 |
1.33e-06 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 52.05 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDY--GSHS-NEDDEST-KCMGYCPQ--TNPLWPDITLQ 1392
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTliTSTSkNKDIKQIrKKVGLVFQfpESQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EhfEIYGAVKGMSSGDMKEVISRITKAL-DLKEHL-QKTVKKLPAGIKRKLCFA--LSMlgNPQVTLLDEPSTGMDPRAK 1468
Cdd:PRK13649 106 D--VAFGPQNFGVSQEEAEALAREKLALvGISESLfEKNPFELSGGQMRRVAIAgiLAM--EPKILVLDEPTAGLDPKGR 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1469 qhmwRAIRTAFKNKKRAAL---LTTHYMEEAEAVCDRVAIMVSGQLRCIGTVqhlKSKFGKGYFLEIK 1533
Cdd:PRK13649 182 ----KELMTLFKKLHQSGMtivLVTHLMDDVANYADFVYVLEKGKLVLSGKP---KDIFQDVDFLEEK 242
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1319-1526 |
1.44e-06 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 51.61 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLG-DYGSHSNEDDESTKcmgycpqtnplwPDITL--QEH 1394
Cdd:PRK10419 31 VSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVsWRGePLAKLNRAQRKAFR------------RDIQMvfQDS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FeiyGAVK-----------------GMSSGDMKEVISRITKALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLL 1456
Cdd:PRK10419 99 I---SAVNprktvreiireplrhllSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27368659 1457 DEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL---RCIGTVQHLKSKFGK 1526
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFSSPAGR 248
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1305-1520 |
1.48e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1305 FLHSRKTTKvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG------------DYGSHSNEDDES 1372
Cdd:PRK10261 22 FMQEQQKIA-AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrsrqviELSEQSAAQMRH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1373 TK----CMGYCPQTNPLWPDITLQEhfEIYGAVKGMSSGDMKEVISRITKALDL------KEHLQKTVKKLPAGIKRKLC 1442
Cdd:PRK10261 101 VRgadmAMIFQEPMTSLNPVFTVGE--QIAESIRLHQGASREEAMVEAKRMLDQvripeaQTILSRYPHQLSGGMRQRVM 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1443 FALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK10261 179 IAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
497-677 |
1.57e-06 |
|
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: 50.79 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDEMFEA-----RKMIGICPQSDMNFDVl 571
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 572 TVEENLSIlasvkGIPANN----IIQEVQKVLLDLDMQAIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:cd03290 94 TVEENITF-----GSPFNKqrykAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27368659 643 AGMD-PCSRHIVW-NLLKY-RKANRVTVFSTH---FMDEAD 677
Cdd:cd03290 169 SALDiHLSDHLMQeGILKFlQDDKRTLVLVTHklqYLPHAD 209
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1290-1518 |
1.61e-06 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 51.24 E-value: 1.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1290 IMVYNLHKEYDDKkdflhsrkttkVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNED 1369
Cdd:COG4604 2 IEIKNVSKRYGGK-----------VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1370 DESTKCMGYCPQTNPLWPDITLQE--HFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGiKRKLCF-ALS 1446
Cdd:COG4604 71 RELAKRLAILRQENHINSRLTVRElvAFGRFPYSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFiAMV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1447 MLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
499-642 |
1.70e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.81 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 499 NLSFdiYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKM----IGICPQS---DMNFDVL 571
Cdd:PRK11819 27 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------------EARPApgikVGYLPQEpqlDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 572 -TVEENLS----ILASVKGIPAN-------------------NIIQevQKVLLDLD------MQAIK----DNQAKKLSG 617
Cdd:PRK11819 89 eNVEEGVAevkaALDRFNEIYAAyaepdadfdalaaeqgelqEIID--AADAWDLDsqleiaMDALRcppwDAKVTKLSG 166
|
170 180
....*....|....*....|....*
gi 27368659 618 GQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK11819 167 GERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
491-647 |
2.08e-06 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.83 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 491 NETVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-----DGFasiyghRVSEIDEM----FEARKMIG-- 559
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDRF------RWNGIDLLklspRERRKIIGre 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 IC-----PQSDMNfDVLTVEENLsilasVKGIPANN---------------IIQEVQKVlldldmqAIKDNQA------K 613
Cdd:COG4170 91 IAmifqePSSCLD-PSAKIGDQL-----IEAIPSWTfkgkwwqrfkwrkkrAIELLHRV-------GIKDHKDimnsypH 157
|
170 180 190
....*....|....*....|....*....|....
gi 27368659 614 KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4170 158 ELTEGECQKVMIAMAIANQPRLLIADEPTNAMES 191
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1319-1512 |
2.38e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 2.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGdVEP--TSGKIFL-GDYGSHSNEDD----------ESTKCMGYCPQTnPL 1385
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIdGKPVKIRNPQQaiaqgiamvpEDRKRDGIVPVM-GV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1386 WPDITLQ--EHFeiygaVKGMSSGDMKEV--ISRITKALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPS 1460
Cdd:PRK13549 359 GKNITLAalDRF-----TGGSRIDDAAELktILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27368659 1461 TGMDPRAKQHMWRAIrTAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:PRK13549 434 RGIDVGAKYEIYKLI-NQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-658 |
2.57e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 52.12 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIygHRVSEIDEMFEARK--MIG------IC-PQSDMN 567
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RI--ARPAGARVLFLPQRpyLPLgtlreaLLyPATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 568 FDVLTVEEnlsILASVkGIPAnniiqevqkvLLD-LDMQAikdNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG4178 455 FSDAELRE---ALEAV-GLGH----------LAErLDEEA---DWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517
|
170
....*....|..
gi 27368659 647 PCSRHIVWNLLK 658
Cdd:COG4178 518 EENEAALYQLLR 529
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1319-1523 |
2.61e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWP----------- 1387
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSgtvrfnldpfn 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1388 ---DITLQEHFEiygavkgmsSGDMKEVISRITKALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PLN03130 1338 ehnDADLWESLE---------RAHLKDVIRRNSLGLDAE--VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD 1406
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1465 PRAKQHMWRAIRTAFKNKkrAALLTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:PLN03130 1407 VRTDALIQKTIREEFKSC--TMLIIAHRLNTI-IDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
441-646 |
2.73e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 51.86 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 441 SKNK---RNYKELSEGNINGNISLNEIVEPVSsEFIGKEAIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSG 517
Cdd:TIGR03719 284 AKSKarlARYEELLSQEFQKRNETAEIYIPPG-PRLGDKVIEAENLTKAFGDK----LLIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 518 TGKSTLMNILCGLCPPSDGFASIyGHRVSeidemfearkmIGICPQSDMNFDvltveenlsilasvkgiPANNIIQEVQK 597
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEI-GETVK-----------LAYVDQSRDALD-----------------PNKTVWEEISG 409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 598 VLLDLDMQAIKDN--------------QAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 410 GLDIIKLGKREIPsrayvgrfnfkgsdQQKKvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1313-1464 |
2.75e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1313 KVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQ 1392
Cdd:PRK10253 20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGDITVQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 E--------HFEIYGAVKgmssGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PRK10253 100 ElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
501-689 |
3.12e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIygHRVSeidemFEA-RKMIGICPQsDMNFDVLTVE 574
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqFSHI--TRLS-----FEQlQKLVSDEWQ-RNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSilasvkGIPANNIIQE-------VQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK10938 95 EDDT------GRTTAEIIQDevkdparCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27368659 648 CSRHIVWNLLKYRKANRVTV------FST--HFMDEADILADRkAVISQG 689
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLvlvlnrFDEipDFVQFAGVLADC-TLAETG 217
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-646 |
3.34e-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: 52.22 E-value: 3.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQSDMNFDVlTVEEN 576
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 577 LSILASVKGIPANNIIQEVQkVLLDLDMQAIKDNQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQ-LEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
496-691 |
3.77e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE------IDEMF----EARKMIGICPQSD 565
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINHGFalvtEERRSTGIYAYLD 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 MNFDVLTveENLSILASVKGIPANNIIQEvqkvlldlDMQAIKDNQAKK----------LSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK10982 343 IGFNSLI--SNIRNYKNKVGLLDNSRMKS--------DTQWVIDSMRVKtpghrtqigsLSGGNQQKVIIGRWLLTQPEI 412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 636 LLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10982 413 LMLDEPTRGIDVGAKFEIYQLiAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1319-1464 |
4.18e-06 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 49.84 E-value: 4.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGdVEPTSGKIFL-----GDYGSHsneddESTKCMGYCPQTNPLWPDITLQE 1393
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLngrplSDWSAA-----ELARHRAYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1394 HFEIYGAVKGMSSGDmKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSML-----GNP--QVTLLDEPSTGMD 1464
Cdd:COG4138 89 YLALHQPAGASSEAV-EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMNSLD 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-646 |
4.72e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 50.06 E-value: 4.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 506 EGQITALLGHSGTGKSTLMNILCG-----LC----PPS-DGFASIYghRVSEIDEMFEARKmigicpqsDMNFDVLTVEE 575
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnLGkfddPPDwDEILDEF--RGSELQNYFTKLL--------EGDVKVIVKPQ 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 576 NLSIL-ASVKGIPANNIIQEVQKVLLD-----LDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03236 95 YVDLIpKAVKGKVGELLKKKDERGKLDelvdqLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1319-1464 |
4.84e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.93 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGdVEPTSGKIF-----LGDYgSHSneddESTKCMGY-CPQTNPL-----WP 1387
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQfagqpLEAW-SAA----ELARHRAYlSQQQTPPfampvFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1388 DITLQEHfeiygavKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSML-----GNP--QVTLLDEPS 1460
Cdd:PRK03695 89 YLTLHQP-------DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPM 161
|
....
gi 27368659 1461 TGMD 1464
Cdd:PRK03695 162 NSLD 165
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1326-1511 |
4.88e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 50.06 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1326 GEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDesTKCMGYCPQTNPlWPDItlqehfeIYGAVKGMS 1405
Cdd:PRK11247 38 GQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEARED--TRLMFQDARLLP-WKKV-------IDNVGLGLK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1406 sGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRA 1485
Cdd:PRK11247 108 -GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFT 186
|
170 180
....*....|....*....|....*.
gi 27368659 1486 ALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11247 187 VLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
497-651 |
6.62e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 49.83 E-value: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-------GFASIYGHRVSEIDEMFEARkMIGICPQSDMNF 568
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLAR-LRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 569 DVLTVEENLSI----LASVKGIPANNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAV---------LGNPKI 635
Cdd:PRK13547 96 FAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170
....*....|....*.
gi 27368659 636 LLLDEPTAGMDPCSRH 651
Cdd:PRK13547 176 LLLDEPTAALDLAHQH 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
496-689 |
7.55e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQSDMNF-DvlTVE 574
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVVSQTPFLFsD--TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 575 ENLSI---LASVKGIPANNIIQEVQKVLLDLDmQAIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:PRK10789 407 NNIALgrpDATQQEIEHVARLASVHDDILRLP-QGYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27368659 649 SRH-IVWNLLKYRKaNRVTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK10789 486 TEHqILHNLRQWGE-GRTVIISAHRL-SALTEASEILVMQHG 525
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
497-653 |
7.81e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.40 E-value: 7.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpsDGFAS---IYGHRVSEIDEMFEARKMIG-ICPQSDMNFDVLT 572
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYSNdltLFGRRRGSGETIWDIKKHIGyVSSSLHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 573 VEENLSILASVKGIpanNIIQEV---QKVLLD--LDMQAIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK10938 354 SVRNVILSGFFDSI---GIYQAVsdrQQKLAQqwLDILGIDKRTADApfhsLSWGQQRLALIVRALVKHPTLLILDEPLQ 430
|
170
....*....|
gi 27368659 644 GMDPCSRHIV 653
Cdd:PRK10938 431 GLDPLNRQLV 440
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1319-1465 |
9.02e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 49.38 E-value: 9.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLGDYGSHSNEDD--ESTKCMGYCPQTNPLWPDIT----- 1390
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDMNvfdnv 105
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1391 ---LQEHFEIYGAVkgmssgdMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDP 1465
Cdd:PRK11831 106 aypLREHTQLPAPL-------LHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
497-646 |
1.16e-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: 49.08 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhRVSeidemfearkmigICPQSDMNFDVlTVEEN 576
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-RIS-------------FSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 577 LSILASVKGIPANNIIQEVQkvlLDLDMQAI--KDNQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03291 118 IIFGVSYDEYRYKSVVKACQ---LEEDITKFpeKDNTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1323-1494 |
1.34e-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: 48.10 E-value: 1.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1323 VKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIF----LGDYGSHSNEDDESTKCMGYCPQtNPLWPDITLQEHFeIY 1398
Cdd:cd03290 24 IPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ-KPWLLNATVEENI-TF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1399 GAvkGMSSGDMKEVIS--RITKALDLKEHLQKTVK-----KLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQH- 1470
Cdd:cd03290 102 GS--PFNKQRYKAVTDacSLQPDIDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLSDHl 179
|
170 180
....*....|....*....|....
gi 27368659 1471 MWRAIRTAFKNKKRAALLTTHYME 1494
Cdd:cd03290 180 MQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
494-532 |
1.36e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.79 E-value: 1.36e-05
10 20 30
....*....|....*....|....*....|....*....
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP 52
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
503-646 |
1.37e-05 |
|
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: 49.78 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARkmIGICPQ---SDMNfdvLTVEENLSi 579
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDE--DLK--ISYKPQyisPDYD---GTVEEFLR- 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27368659 580 LASVKGIPANNIIQEVQKvllDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1245 424 SANTDDFGSSYYKTEIIK---PLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1319-1516 |
1.52e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.54 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGdVEPT---SGKI-FLGDYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEH 1394
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIiFEGEELQASNIRDTERAGIAIIHQELALVKELSVLEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 F----EI-------YGAVKGMSSGDMKEV---ISRITKALDLKEHLQKTVKklpagIKRKLcfalsmlgNPQVTL--LDE 1458
Cdd:PRK13549 103 IflgnEItpggimdYDAMYLRAQKLLAQLkldINPATPVGNLGLGQQQLVE-----IAKAL--------NKQARLliLDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1459 PSTGMDPRAKQHMWRAIRTaFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGqlRCIGT 1516
Cdd:PRK13549 170 PTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1326-1475 |
1.60e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1326 GEILGLLGPNGAGKSTIINILVGDVEPTSGK------IFLGDYGSHSNE---DDESTkcmgyCPQTNPLWPDITLQEHFE 1396
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiglakgIKLGYFAQHQLEflrADESP-----LQHLARLAPQELEQKLRD 412
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27368659 1397 IYGAVkGMSSGDMKEVISRITkaldlkehlqktvkklpAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAI 1475
Cdd:PRK10636 413 YLGGF-GFQGDKVTEETRRFS-----------------GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
494-646 |
1.86e-05 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 48.57 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRV-----SEIDEM-FEARKMIGICPQS 564
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREIlnlpeKELNKLrAEQISMIFQDPMT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 565 DMNFDVLTVEENLSILASVKGIPANNIIQEVQKVLldldmQAIKDNQAKK--------LSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK09473 109 SLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRML-----DAVKMPEARKrmkmypheFSGGMRQRVMIAMALLCRPKLL 183
|
170
....*....|
gi 27368659 637 LLDEPTAGMD 646
Cdd:PRK09473 184 IADEPTTALD 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
494-653 |
2.03e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.64 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY-----GHRVSEIDEMFEARKMIG--------- 559
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFknehtNDMTNEQDYQGDEEQNVGmknvnefsl 1260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 560 -------------------------ICpqsDMN-------FDVLTVEE---NLSILASVKGIPANNIIQEVQKV----LL 600
Cdd:PTZ00265 1261 tkeggsgedstvfknsgkilldgvdIC---DYNlkdlrnlFSIVSQEPmlfNMSIYENIKFGKEDATREDVKRAckfaAI 1337
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 601 DLDMQAIKDNQ-------AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIV 653
Cdd:PTZ00265 1338 DEFIESLPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1319-1519 |
2.32e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 48.75 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL-GDYGSHSNEDDESTKCMGYCPQ---TNPLWPDITLQEH 1394
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLdGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEIyGAVKGMSSGDMkeVISRITKALDLKEHLQKTVKKLPAGikRKLCFALSMlGNPQ-------------VTLLDEPST 1461
Cdd:PRK11288 352 INI-SARRHHLRAGC--LINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSG-GNQQkailgrwlsedmkVILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1462 GMDPRAKQHMWRAIRtAFKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQLRciGTVQH 1519
Cdd:PRK11288 426 GIDVGAKHEIYNVIY-ELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1319-1357 |
2.37e-05 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.19 E-value: 2.37e-05
10 20 30
....*....|....*....|....*....|....*....
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI 1357
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRI 392
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
489-529 |
2.59e-05 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 47.01 E-value: 2.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27368659 489 KKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:cd01854 71 KTGEGLDELREL----LKGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
489-529 |
2.77e-05 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 47.80 E-value: 2.77e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27368659 489 KKNETVEALRnlsfDIYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:COG1162 152 KTGEGLDELR----ELLKGKTSVLVGQSGVGKSTLINALLP 188
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
504-646 |
3.11e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 504 IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASiyghrvSEIDemfearkmIGICPQ-----SDMnfdvlTVEENLS 578
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PELK--------ISYKPQyikpdYDG-----TVEDLLR 422
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 579 ilaSVKGIPANNIIQEvqKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK13409 423 ---SITDDLGSSYYKS--EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1303-1529 |
7.50e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.80 E-value: 7.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1303 KDFLHSRKTTKVAT-KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVE----PTSGKIflgDYGSHSNEDDES--TKC 1375
Cdd:TIGR00956 63 RKLKKFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDgfhiGVEGVI---TYDGITPEEIKKhyRGD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1376 MGYCPQTNPLWPDITLQEHFEIYGAVKGmsSGDMKEVISRITKALDLKE---------HLQKT------VKKLPAGIKRK 1440
Cdd:TIGR00956 140 VVYNAETDVHFPHLTVGETLDFAARCKT--PQNRPDGVSREEYAKHIADvymatyglsHTRNTkvgndfVRGVSGGERKR 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1441 LCFALSMLGNPQVTLLDEPSTGMDPRAKQHMWRAIRTAFKNKKRAALLTTHY-MEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQcSQDAYELFDKVIVLYEGYQIYFGPADK 297
|
250
....*....|.
gi 27368659 1520 LKSKFGK-GYF 1529
Cdd:TIGR00956 298 AKQYFEKmGFK 308
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1330-1359 |
8.50e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 8.50e-05
10 20 30
....*....|....*....|....*....|
gi 27368659 1330 GLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1319-1511 |
9.49e-05 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 46.94 E-value: 9.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLG--DYGSHSNEddESTKC-MGYCP---QTNPLWPDITLQ 1392
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeDITGLSPR--ERRRLgVAYIPedrLGRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 E-----HFEIYGAVKG--MSSGDMKEVISRITKALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:COG3845 355 EnlilgRYRRPPFSRGgfLDRKAIRAFAEELIEEFDVRtPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLD 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27368659 1465 PRAKQHMWRAIRTAfKNKKRAALLTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG3845 435 VGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
477-646 |
1.23e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 477 AIRISGIQKAYRKKnetvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEMFEARk 556
Cdd:PRK15064 319 ALEVENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 557 mIGICPQ-SDMNFDV-LTVEENLSILASVKGIpanniIQEVQKVLLDLDMQA--IKdNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:PRK15064 384 -IGYYAQdHAYDFENdLTLFDWMSQWRQEGDD-----EQAVRGTLGRLLFSQddIK-KSVKVLSGGEKGRMLFGKLMMQK 456
|
170
....*....|....
gi 27368659 633 PKILLLDEPTAGMD 646
Cdd:PRK15064 457 PNVLVMDEPTNHMD 470
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1319-1361 |
2.01e-04 |
|
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: 45.94 E-value: 2.01e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD 1361
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1319-1359 |
2.46e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 45.73 E-value: 2.46e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL 382
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
487-646 |
2.55e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.09 E-value: 2.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 487 YRKKNETVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQSD- 565
Cdd:TIGR00957 1294 YREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG-LHDLRFKITIIPQDPv 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 566 -------MNFDVLTVEENLSI-----LASVKGIpanniiqeVQKVLLDLDMQAIKDNQakKLSGGQKRKLSLGIAVLGNP 633
Cdd:TIGR00957 1371 lfsgslrMNLDPFSQYSDEEVwwaleLAHLKTF--------VSALPDKLDHECAEGGE--NLSVGQRQLVCLARALLRKT 1440
|
170
....*....|...
gi 27368659 634 KILLLDEPTAGMD 646
Cdd:TIGR00957 1441 KILVLDEATAAVD 1453
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1317-1491 |
2.90e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.49 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1317 KYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGDYGSHSNEDDESTKC----MGYCPQTNPLWPDITLQ 1392
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1393 EHFEIYGAVKGMSSGDMKEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMDPRAKQHMw 1472
Cdd:PRK10535 105 QNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV- 183
|
170
....*....|....*....
gi 27368659 1473 RAIRTAFKNKKRAALLTTH 1491
Cdd:PRK10535 184 MAILHQLRDRGHTVIIVTH 202
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1319-1359 |
3.30e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.17 E-value: 3.30e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGdVEPT---SGKIFL 1359
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILF 62
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1285-1360 |
3.36e-04 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 44.70 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1285 EEKPAIM-VYNLHKEYD--DKKDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI-FLG 1360
Cdd:PRK15079 3 EGKKVLLeVADLKVHFDikDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLG 82
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
489-529 |
3.41e-04 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 43.30 E-value: 3.41e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27368659 489 KKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:pfam03193 92 KTGEGIEALKEL----LKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
4.10e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.32 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFearkmigiCPQSDMNFDV---LTV 573
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--------CTYIGHNLGLkleMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 574 EENLSILASVKgipanNIIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIV 653
Cdd:PRK13541 88 FENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170 180
....*....|....*....|
gi 27368659 654 WNLLKYrKANR--VTVFSTH 671
Cdd:PRK13541 163 NNLIVM-KANSggIVLLSSH 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1294-1359 |
4.47e-04 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 44.19 E-value: 4.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1294 NLHKEYDDKKDFLHSRKTTKvATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:PRK11308 10 DLKKHYPVKRGLFKPERLVK-ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY 74
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
473-527 |
5.52e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 44.04 E-value: 5.52e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27368659 473 IGKEAIRISGiqkayrKKNETVEALRNLsfdiYEGQITALLGHSGTGKSTLMNIL 527
Cdd:PRK00098 140 IGYDVLELSA------KEGEGLDELKPL----LAGKVTVLAGQSGVGKSTLLNAL 184
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
498-665 |
6.73e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.59 E-value: 6.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 498 RNLSFDIYEGqITALLGHSGTGKSTLMNILcglcppsdgFASIYGHRVSEIDEMFEARKMIGICP---QSDMNFDV---- 570
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEAL---------KYALTGELPPNSKGGAHDPKLIREGEvraQVKLAFENangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 571 -LTVEENLSILASVKGIPanniiQEVQKVLLdLDMqaikdnqAKKLSGGQKRKLSLGI------AVLGNPKILLLDEPTA 643
Cdd:cd03240 84 kYTITRSLAILENVIFCH-----QGESNWPL-LDM-------RGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTT 150
|
170 180
....*....|....*....|...
gi 27368659 644 GMDPCSRHIVW-NLLKYRKANRV 665
Cdd:cd03240 151 NLDEENIEESLaEIIEERKSQKN 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1294-1360 |
7.59e-04 |
|
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: 43.90 E-value: 7.59e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27368659 1294 NLHKEYDDKKDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGdVEPTSGKI-FLG 1360
Cdd:COG4172 280 DLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIrFDG 346
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1288-1341 |
8.90e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.93 E-value: 8.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1288 PAIMVYNLHKEYDDKKDFLHSRKTTKVATKYVSFCVKKGEILGLLGPNGAGKST 1341
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST 327
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1325-1361 |
9.07e-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: 41.59 E-value: 9.07e-04
10 20 30
....*....|....*....|....*....|....*..
gi 27368659 1325 KGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFLGD 1361
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID 37
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1284-1357 |
9.89e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 42.99 E-value: 9.89e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27368659 1284 CEEKPAIMVYNLHKEYDDKKDFLHsrkttkvatkyVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI 1357
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRD-----------VSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1320-1489 |
1.34e-03 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 43.58 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1320 SFCVKKGEILGLLGPNGAGKSTIINILvGDVEPTsgkiflgdYGSHSNEDDESTkcMGYCPQtNPLWPDITLQEHFeIYg 1399
Cdd:TIGR00954 472 SFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPV--------YGGRLTKPAKGK--LFYVPQ-RPYMTLGTLRDQI-IY- 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1400 avkGMSSGDMKE------VISRITKALDLKEHLQKTV---------KKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:TIGR00954 538 ---PDSSEDMKRrglsdkDLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVS 614
|
170 180
....*....|....*....|....*
gi 27368659 1465 PRAKQHMWRAIRtafknKKRAALLT 1489
Cdd:TIGR00954 615 VDVEGYMYRLCR-----EFGITLFS 634
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
507-647 |
1.43e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 40.82 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 507 GQITALLGHSGTGKSTLMNILCGLCPPSdgfasiyGHRVSEIDemfearkmigicpqsdmnfdvltveenlsilasvkgi 586
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP-------GGGVIYID------------------------------------- 37
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27368659 587 panniIQEVQKVLLDLDMQAIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:smart00382 38 -----GEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDA 93
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
613-689 |
1.57e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.81 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 613 KKLSGGQKRKLS----LGIAVLGNPKILLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH---FMDEADILADRKA 684
Cdd:cd03227 76 LQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQaLAEAILEHLVKGAQVIVITHlpeLAELADKLIHIKK 155
|
....*
gi 27368659 685 VISQG 689
Cdd:cd03227 156 VITGV 160
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
497-646 |
1.69e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.85 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 497 LRNLSFDIYEGQITALLGHSGTGKSTL-MNIlcglcppsdgFASIYGHRVS--------EID-------------EMFEA 554
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSV----------FGRSYGRNISgtvfkdgkEVDvstvsdaidaglaYVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 555 RKMIGIcpqsdmnfdVL--TVEENLSiLASVKGIPANNIIQEVQKVLLDLDMQA---IK----DNQAKKLSGGQKRKLSL 625
Cdd:NF040905 346 RKGYGL---------NLidDIKRNIT-LANLGKVSRRGVIDENEEIKVAEEYRKkmnIKtpsvFQKVGNLSGGNQQKVVL 415
|
170 180
....*....|....*....|.
gi 27368659 626 GIAVLGNPKILLLDEPTAGMD 646
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGID 436
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1330-1459 |
2.56e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1330 GLLGPNGAGKSTIINILVGDVEPTSGKIFLgdygshsnedDESTKCmGYCPQTNPLWPDIT---------------LQEH 1394
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKV-GYLPQEPQLDPEKTvrenveegvaevkaaLDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1395 FEIYGAVkGMSSGDMKEVISRITK---------ALDLKEHLQ------------KTVKKLPAGIKRK--LCFALsmLGNP 1451
Cdd:PRK11819 106 NEIYAAY-AEPDADFDALAAEQGElqeiidaadAWDLDSQLEiamdalrcppwdAKVTKLSGGERRRvaLCRLL--LEKP 182
|
....*...
gi 27368659 1452 QVTLLDEP 1459
Cdd:PRK11819 183 DMLLLDEP 190
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1319-1359 |
2.88e-03 |
|
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: 42.11 E-value: 2.88e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27368659 1319 VSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKIFL 1359
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI 417
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1310-1357 |
3.34e-03 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 42.01 E-value: 3.34e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 27368659 1310 KTTKVATKYVSFCVKKGEILGLLGPNGAGKSTIINILVGDVEPTSGKI 1357
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI 372
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1333-1464 |
4.62e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 40.24 E-value: 4.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27368659 1333 GPNGAGKSTIINILVGDVEPTSGKIflgdYGSHSNEDDESTKCMGYCPQTNPLWPDITLQEHF----EIYGAVkgmssgd 1408
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNI----YYKNCNINNIAKPYCTYIGHNLGLKLEMTVFENLkfwsEIYNSA------- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 27368659 1409 mkEVISRITKALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQVTLLDEPSTGMD 1464
Cdd:PRK13541 102 --ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| |
