|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
84-1618 |
3.81e-136 |
|
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: 469.11 E-value: 3.81e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 84 VTNITSSIMqKVSTDHLPDVIIT--EEYTNEKEMLTSSLS--KPSNF-VGVVFKD----------SMSYELRFFPDMI-- 146
Cdd:TIGR01257 502 IFNITDRFL-RLANQYLECLVLDkfESYDDEVQLTQRALSllEENRFwAGVVFPDmypwtsslppHVKYKIRMDIDVVek 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 147 --PVSSIYMDS--RAgcsKSCEAAQYWSSGFTVLQASIDAAI----IQLKTNVSLWKELESTKAVIMGETAVVEIDTFPr 218
Cdd:TIGR01257 581 tnKIKDRYWDSgpRA---DPVEDFRYIWGGFAYLQDMVEQGItrsqMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFP- 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 219 gvilIYLVIAFSPFGYFLAIHIVAEKEKKIKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATASLLFPQSSSIV 298
Cdd:TIGR01257 657 ----IFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFI 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 299 IFLLFFLYGLSSVFFALMLTPLFKKSKHV----GIVEFFV----TVAFGFIGLMIILIesfpKSLVWLFSPfchCTFVIG 370
Cdd:TIGR01257 733 LFLFLLAFSTATIMQCFLLSTFFSKASLAaacsGVIYFTLylphILCFAWQDRMTADL----KTAVSLLSP---VAFGFG 805
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 371 IAQVMHLEDFNEGASFSNLTAGP-----YPLIITIIMLTLNSIFYVLLAVYLDQVIPGEFGLRRSSLYFLKPSYW----- 440
Cdd:TIGR01257 806 TEYLVRFEEQGLGLQWSNIGNSPlegdeFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWlggeg 885
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 441 --SKSKRNYEELSEgnVNGNISFSEIIEPVSSEFVGKE------AIRISGIQKTYRKKGEnvEALRNLSFDIYEGQITAL 512
Cdd:TIGR01257 886 csTREERALEKTEP--LTEEMEDPEHPEGINDSFFERElpglvpGVCVKNLVKIFEPSGR--PAVDRLNITFYENQITAF 961
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 513 LGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEA-RKMIGICPQLDIHFDVLTVEENLSILASIKGIPANNI 591
Cdd:TIGR01257 962 LGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIETNLDAvRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEA 1038
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 592 IQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR01257 1039 QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTH 1118
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 672 FMDEADILADRKAVISQGMLKCVGSSMFLKSKWGIGYRLSMY------------IDKYCATES----------------- 722
Cdd:TIGR01257 1119 HMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVrkmkniqsqrggCEGTCSCTSkgfstrcparvdeitpe 1198
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 723 ---------LSSLVKQHIPGATLLQQNDQQLVYSLPFKDMDK--FSGLFSAL-DSHSNLGVISYGVSMTTLEDVFLKL-- 788
Cdd:TIGR01257 1199 qvldgdvneLMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQraYASLFRELeETLADLGLSSFGISDTPLEEIFLKVte 1278
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 789 -----------------------------EVEAEIDQADYSVFT---------QQPLEEEMDSKSFDEMEQslLILSETK 830
Cdd:TIGR01257 1279 dadsgslfaggaqqkrenanlrhpcsgptEKAGQTPQASHTCSPgqpaahpegQPPPEPEDPGVPLNTGAR--LILQHVQ 1356
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 831 AALVS----TMSLWKQ---QMYTIAKFHFFTLKReskSVRSVLLLLLIFFTVQIFMFLVHHSFKNAVVP----IKLVPDL 899
Cdd:TIGR01257 1357 ALLVKrfqhTIRSHKDflaQIVLPATFVFLALML---SIIIPPFGEYPALTLHPWMYGQQYTFFSMDEPnsehLEVLADV 1433
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 900 YFLKPGDKPHKYKTSLLLQ-----------NSADSDISDLI------------SFFTSQNIMVTMI-------------- 942
Cdd:TIGR01257 1434 LLNKPGFGNRCLKEEWLPEypcgnstpwktPSVSPNITHLFqkqkwtaahpspSCRCSTREKLTMLpecpegagglpppq 1513
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 943 ---------------NDSDYVsVAPHSAALNVMHSEKDYV----FAAVFNSTMVYSLPI----LVNIISNY--------- 990
Cdd:TIGR01257 1514 rtqrsteilqdltdrNISDFL-VKTYPALIRSSLKSKFWVneqrYGGISIGGKLPAIPItgeaLVGFLSDLgqmmnvsgg 1592
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 991 ------------YLYHLNVTETIQIW---------------------------------------STPF------FQEIT 1013
Cdd:TIGR01257 1593 pvtreaskempdFLKHLETEDNIKVWfnnkgwhalvsflnvahnailraslpkdrdpeeygitviSQPLnltkeqLSEIT 1672
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1014 DIVFKIElyfqaALLGIIV----TAMPPYFAMENAENHKIKAYTQLKLSGLLPSAYWIGQAVVDIPLFFIILILMLGSLL 1089
Cdd:TIGR01257 1673 VLTTSVD-----AVVAICVifamSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFI 1747
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1090 AFHYGLYFYTVKFLAVVFCLIGYVPSVILFTYIASFTFkkilntkEFWSFIYsvAALAC------IAITEITFFMGY--T 1161
Cdd:TIGR01257 1748 GFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLF-------DVPSTAY--VALSCanlfigINSSAITFVLELfeN 1818
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1162 IATILHY-----AFCIIIPIYPLLGCLISfIKISwknvRKNVDTY---------NP--WDRLSVAVISPYLQCVLWIFLL 1225
Cdd:TIGR01257 1819 NRTLLRFnamlrKLLIVFPHFCLGRGLID-LALS----QAVTDVYaqfgeehsaNPfqWDLIGKNLVAMAVEGVVYFLLT 1893
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1226 QYYEKKYggrsirkdpFFrnlstkskNRKLPEPPDNE--DEDEDVKAERLKVkeLMGcqcceekpsimvsnlhkeyDDKK 1303
Cdd:TIGR01257 1894 LLIQHHF---------FL--------SRWIAEPAKEPifDEDDDVAEERQRI--ISG-------------------GNKT 1935
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1304 DFLLSRKVKKV-------ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSlKCM 1376
Cdd:TIGR01257 1936 DILRLNELTKVysgtsspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-QNM 2014
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1377 GYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLL 1456
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1457 DEPSTGMDPKAKQHMWRAIRTAFKnRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKLKD 1536
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIR-EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKS 2173
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1537 WIENL--EVDRLQREIQYIFPNASRQESFSSILAYKIPKedvQSLSQSFFKLEEAKHAFAIEEYSFSQATLEQVFVELTK 1614
Cdd:TIGR01257 2174 PKDDLlpDLNPVEQFFQGNFPGSVQRERHYNMLQFQVSS---SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAK 2250
|
....
gi 27262626 1615 EQEE 1618
Cdd:TIGR01257 2251 QQTE 2254
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1290-1521 |
9.75e-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: 270.53 E-value: 9.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYddkkdfllsRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETsED 1369
Cdd:cd03263 1 LQIRNLTKTY---------KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03263 71 KAARQSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLK 1521
Cdd:cd03263 151 GPSVLLLDEPTSGLDPASRRAIWDLILEVRKG--RSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
478-701 |
2.52e-82 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 269.37 E-value: 2.52e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrKKGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03263 1 LQIRNLTKTY-KKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT--DRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSSMFLK 701
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1290-1524 |
5.36e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.88 E-value: 5.36e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETsED 1369
Cdd:COG1131 1 IEVRGLTKRYGDK-----------TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:COG1131 69 AEVRRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLR-ELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
478-696 |
9.20e-69 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 231.11 E-value: 9.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG1131 1 IEVRGLTKRYGDK----TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA--EVRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 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 |
1.10e-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: 197.00 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDdkkdfllsrkvKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSED 1369
Cdd:COG4555 2 IEVENLSKKYG-----------KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDV-RKEP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:COG4555 70 REARRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGK 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 |
8.70e-55 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 188.76 E-value: 8.70e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVseIDEMFEARKM 557
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI--KKEPEEVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLsilasikgipanniiqevqkvlldldmqtikdnqakKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLI 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 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 |
1.18e-53 |
|
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: 187.19 E-value: 1.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSED 1369
Cdd:cd03265 1 IEVENLVKKYGDF-----------EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV-VREP 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03265 69 REVRRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLK 1521
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1314-1613 |
7.68e-53 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 187.98 E-value: 7.68e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSEDDDSLKCMGYCPQINPLWPDTTLQE 1393
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDV-VREPRKVRRSIGIVPQYASVDEDLTGRE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:TIGR01188 86 NLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1474 AIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGyFLEIKLKDWIE-NLEVDRLQREIQY 1552
Cdd:TIGR01188 166 YIR-ALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD-TLESRPRDIQSlKVEVSMLIAELGE 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1553 IFPNASRQESFSSILAYKIPKEDVQsLSQSFFKLEEAKhaFAIEEYSFSQATLEQVFVELT 1613
Cdd:TIGR01188 244 TGLGLLAVTVDSDRIKILVPDGDET-VPEIVEAAIRNG--IRIRSISTERPSLDDVFLKLT 301
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
478-695 |
2.03e-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: 177.77 E-value: 2.03e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGqITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK--QPQKLRRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQldiHFDV---LTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:cd03264 74 IGYLPQ---EFGVypnFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
478-696 |
2.96e-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: 178.51 E-value: 2.96e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKkgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:COG4555 2 IEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRaLKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGS 215
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1292-1511 |
1.23e-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: 173.74 E-value: 1.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSEDDD 1371
Cdd:cd03230 3 VRNLSKRYGKKT-----------ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 SLKCMGYCPQINPLWPDTTLQEHFeiygavkgmsasdmkevisrithaldlkehlqktvkKLPAGIKRKLCFALSMLGNP 1451
Cdd:cd03230 71 VKRRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDP 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03230 115 ELLILDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
489-701 |
1.51e-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: 1.51e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 489 KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKMIGICPQLDIHF 568
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR--EPREVRRRIGIVFQDLSVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03265 86 DELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQ 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 649 SRHIVWNLL-KYRKANRVTVF-STHFMDEADILADRKAVISQGMLKCVGSSMFLK 701
Cdd:cd03265 166 TRAHVWEYIeKLKEEFGMTILlTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1292-1618 |
1.02e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.21 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysseTSEDDD 1371
Cdd:COG4152 4 LKGLTKRFGDKT-----------AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG----EPLDPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 SLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:COG4152 69 DRRRIGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFlE 1531
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIR-ELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTL-R 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1532 IKLK---DWIENLevdrlqreiqyifPNASRQESFSSILAYKIPKE-DVQSLsqsffkLEEAKHAFAIEEYSFSQATLEQ 1607
Cdd:COG4152 227 LEADgdaGWLRAL-------------PGVTVVEEDGDGAELKLEDGaDAQEL------LRALLARGPVREFEEVRPSLNE 287
|
330
....*....|.
gi 27262626 1608 VFVELTKEQEE 1618
Cdd:COG4152 288 IFIEVVGEKAE 298
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1290-1545 |
9.74e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 162.56 E-value: 9.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDK----------KDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVfl 1359
Cdd:COG4586 2 IEVENLSKTYRVYekepglkgalKGLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1360 gdyssetsedddslKCMGYCP----------------QINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLK 1423
Cdd:COG4586 80 --------------RVLGYVPfkrrkefarrigvvfgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1424 EHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfkNRKRAA--ILTTHYMEEAEAVCD 1501
Cdd:COG4586 146 ELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEY--NRERGTtiLLTSHDMDDIEALCD 223
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 27262626 1502 RVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKLKDWIENLEVDR 1545
Cdd:COG4586 224 RVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPR 267
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1313-1515 |
2.56e-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: 157.44 E-value: 2.56e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1313 KVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSEDDDSlkcMGYCPQINPLWPDTTLQ 1392
Cdd:cd03269 13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLF-DGKPLDIAARNR---IGYLPEERGLYPKMKVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:cd03269 89 DQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1473 RAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03269 169 DVIRE-LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
486-689 |
1.61e-42 |
|
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: 154.93 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQld 565
Cdd:cd03225 6 SFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK-LSLKELRRKVGLVFQ-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 iHFDV----LTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:cd03225 83 -NPDDqffgPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27262626 642 TAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKAEGKTiIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
478-695 |
2.22e-42 |
|
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: 154.83 E-value: 2.22e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARKM 557
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRqLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
478-696 |
2.47e-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: 155.18 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKM 557
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK-KNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGIC---P--QLdihFDvLTVEE-------NLsilasikGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSL 625
Cdd:COG1122 77 VGLVfqnPddQL---FA-PTVEEdvafgpeNL-------GLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 626 -GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1122 146 aGVLAM-EPEVLVLDEPTAGLDPRGRRELLELLKrLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
478-691 |
1.51e-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: 151.99 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKM 557
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG---KSYQKNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIiqevQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 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 |
1.53e-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: 152.64 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--- 554
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQldiHF---DVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:cd03255 81 RRHIGFVFQ---SFnllPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 632 NPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03255 158 DPKIILADEPTGNLDSETGKEVMELLRelNKEAGTTIVVVTHDPELAE-YADRIIELRDG 216
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
478-687 |
7.11e-41 |
|
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: 150.70 E-value: 7.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfEARKM 557
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 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 |
9.83e-41 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 150.04 E-value: 9.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDdkkdfllsrkvKKVATKYISFCVKKGeILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSseTSED 1369
Cdd:cd03264 1 LQLENLTKRYG-----------KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD--VLKQ 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSL-KCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSML 1448
Cdd:cd03264 67 PQKLrRRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALV 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1449 GNPQITLLDEPSTGMDPKAkqhmwraiRTAFKN------RKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:cd03264 147 GDPSILIVDEPTAGLDPEE--------RIRFRNllselgEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1290-1511 |
1.25e-39 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 147.48 E-value: 1.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYD----------DKKDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL 1359
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1360 GDYSSetSEDDDSLK-----CMGycpQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLP 1434
Cdd:cd03267 81 AGLVP--WKRRKKFLrrigvVFG---QKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1435 AGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03267 156 LGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
478-688 |
3.04e-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: 145.31 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARkm 557
Cdd:COG4133 3 LEAENLSCRR---GERL-LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIiqEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 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 |
3.99e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 3.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA 554
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 ---RKMIGICPQlDIH-FDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:COG1136 82 rlrRRHIGFVFQ-FFNlLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 631 GNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADIlADRKAVISQGML 691
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1289-1509 |
4.42e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 146.51 E-value: 4.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGdySSETS 1367
Cdd:PRK13536 41 AIDLAGVSKSYGDK-----------AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKItVLG--VPVPA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSM 1447
Cdd:PRK13536 108 RARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARAL 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK13536 188 INDPQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
479-689 |
4.81e-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: 4.81e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 479 RISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMI 558
Cdd:cd00267 1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-LEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 559 GICPQLdihfdvltveenlsilasikgipanniiqevqkvlldldmqtikdnqakklSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTViIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
497-643 |
1.18e-37 |
|
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: 138.93 E-value: 1.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEaRKMIGICPQLDIHFDVLTVEEN 576
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 577 LSILASIKGIPANNIIQEVQKVLLDLDMQTIKD----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1290-1515 |
1.66e-37 |
|
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: 140.97 E-value: 1.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLlsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSED 1369
Cdd:cd03266 2 ITADALTKRFRDVKKTV-------QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKcMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03266 75 EARRR-LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVH 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03266 154 DPPVLLLDEPTTGLDVMATRALREFIR-QLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1288-1510 |
5.74e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 142.25 E-value: 5.74e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETS 1367
Cdd:PRK13537 6 APIDFRNVEKRYGDK-----------LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKcMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSM 1447
Cdd:PRK13537 75 ARHARQR-VGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKnRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:PRK13537 154 VNDPDVLVLDEPTTGLDPQARHLMWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1102-1626 |
1.66e-36 |
|
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: 152.09 E-value: 1.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1102 FLAVVFCLIG----YVPSVILFTYIASFTFKKILNTKEFWSFiYSVAALA--CIAITEITFFMGYT--------IATILH 1167
Cdd:TIGR01257 713 FLLTIFIMHGrilhYSDPFILFLFLLAFSTATIMQCFLLSTF-FSKASLAaaCSGVIYFTLYLPHIlcfawqdrMTADLK 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1168 YAFCIIIPIYPLLGC--LISF----IKISWKNVRKNVDTYNPW-----------DRLSVAVISPYLQCVL---------W 1221
Cdd:TIGR01257 792 TAVSLLSPVAFGFGTeyLVRFeeqgLGLQWSNIGNSPLEGDEFsfllsmkmmllDAALYGLLAWYLDQVFpgdygtplpW 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1222 IFLLQ-YYEKKYGGRSIRKDPFFRNLSTKSKNRKLPEPPDNEDedeDVKAERlkvkELMGCQcceekPSIMVSNLHKEYD 1300
Cdd:TIGR01257 872 YFLLQeSYWLGGEGCSTREERALEKTEPLTEEMEDPEHPEGIN---DSFFER----ELPGLV-----PGVCVKNLVKIFE 939
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1301 dkkdfllsrKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSlKCMGYCP 1380
Cdd:TIGR01257 940 ---------PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVR-QSLGMCP 1009
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1381 QINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPS 1460
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPT 1089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1461 TGMDPKAKQHMWRAIrtaFKNRK-RAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEI--KLK-- 1535
Cdd:TIGR01257 1090 SGVDPYSRRSIWDLL---LKYRSgRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLvrKMKni 1166
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1536 -------------------------------DWIENLEVDRLQREIQYIFPNASRQESFSSILAYKIPKEDVQ--SLSQS 1582
Cdd:TIGR01257 1167 qsqrggcegtcsctskgfstrcparvdeitpEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKqrAYASL 1246
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 27262626 1583 FFKLEEAKHAFAIEEYSFSQATLEQVFVELTkeqeeEDNSCGTL 1626
Cdd:TIGR01257 1247 FRELEETLADLGLSSFGISDTPLEEIFLKVT-----EDADSGSL 1285
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1307-1512 |
1.81e-36 |
|
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: 137.35 E-value: 1.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1307 LSRKVKKV-ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSEDddsLKCMGYCPQINP 1384
Cdd:cd03268 6 LTKTYGKKrVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEItFDGKSYQKNIEA---LRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1385 LWPDTTLQEHFEIYGAVKGMSASDMKEVISRIthalDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRIDEVLDVV----GLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 1465 PKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:cd03268 159 PDGIKELRELIL-SLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
4.92e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 140.74 E-value: 4.92e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARK 556
Cdd:PRK13536 41 AIDLAGVSKSYGDK----AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ---LDIHFdvlTVEENLSILASIKGIPANNIiQEVQKVLLDL-DMQTIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:PRK13536 115 RIGVVPQfdnLDLEF---TVRENLLVFGRYFGMSTREI-EAVIPSLLEFaRLESKADARVSDLSGGMKRRLTLARALIND 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:PRK13536 191 PQLLILDEPTTGLDPHARHLIWERLRSLLARGKTIlLTTHFMEEAERLCDRLCVLEAG 248
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
477-689 |
1.91e-35 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 136.37 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------PGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ---LdihFDVLTVEENLSILASIKGIPANNIIQEVQKVL--LDLDmqtikdNQAKK----LSGGQKRKLSLGI 627
Cdd:COG1116 81 DRGVVFQepaL---LPWLTVLDNVALGLELRGVPKAERRERARELLelVGLA------GFEDAyphqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDeLLRLWQETGKTVlFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
478-689 |
5.63e-35 |
|
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: 134.17 E-value: 5.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:cd03261 1 IELRGLTKSF---GGRT-VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEvqKVLLDLDMQTIKDNQAKK---LSGGQKRKLSLGIAVLGN 632
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIRE--IVLEKLEAVGLRGAEDLYpaeLSGGMKKRVALARALALD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:cd03261 155 PELLLYDEPTAGLDPIASGVIDDLiRSLKKELGLTSIMvTHDLDTAFAIADRIAVLYDG 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
478-689 |
1.14e-34 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 133.05 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFE-ARK 556
Cdd:cd03218 1 LRAENLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKrARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITdHNVRETLSITDRAYIIYEG 209
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1288-1491 |
1.53e-34 |
|
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: 131.83 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKKdfLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDySSETS 1367
Cdd:COG4133 1 MMLEAENLSCRRGERL--LFSG---------LSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNG-EPIRD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDmkEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSM 1447
Cdd:COG4133 69 AREDYRRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTH 1491
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIA-AHLARGGAVLLTTH 189
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-689 |
2.24e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 134.47 E-value: 2.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARK 556
Cdd:COG4152 1 MLELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIG-------ICPQLdihfdvlTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:COG4152 72 RIGylpeergLYPKM-------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG4152 145 LHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTViFSSHQMELVEELCDRIVIINKG 205
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
477-689 |
2.40e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.55 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidEMFEARK 556
Cdd:PRK13537 7 PIDFRNVEKRY---GDKL-VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS--RARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILlTTHFMEEAERLCDRLCVIEEG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1290-1518 |
2.80e-34 |
|
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: 132.07 E-value: 2.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLlsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYssETSED 1369
Cdd:COG1122 1 IELENLSFSYPGGTPAL----------DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGK--DITKK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DdsLKCM----GYCPQiNplwPD-----TTLQEhfEI-YGAV-KGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIK 1438
Cdd:COG1122 69 N--LRELrrkvGLVFQ-N---PDdqlfaPTVEE--DVaFGPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1439 RKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:COG1122 141 QRVAIAgvLAM--EPEVLVLDEPTAGLDPRGRRELLELLK-RLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
..
gi 27262626 1517 VQ 1518
Cdd:COG1122 218 PR 219
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
497-691 |
3.73e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 3.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEARKMIGICPQ-LDIHFDvlTV 573
Cdd:COG4619 16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSG--EIYldGKPLSAMP-PPEWRRQVAYVPQePALWGG--TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSILASIKGIPAN--NIIQEVQKVLLDLDmqtIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:COG4619 91 RDNLPFPFQLRERKFDreRALELLERLGLPPD---ILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 652 IVWNLLK-YRKANRVTVFS-THFMDEADILADRKAVISQGML 691
Cdd:COG4619 168 RVEELLReYLAEEGRAVLWvSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1292-1510 |
5.03e-34 |
|
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: 130.66 E-value: 5.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKDFLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDD 1371
Cdd:cd03225 2 LKNLSFSYPDGARPALDD---------ISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 SLKCMGYCPQiNplwPD-----TTLQEhfEI-YGAVK-GMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFA 1444
Cdd:cd03225 73 LRRKVGLVFQ-N---PDdqffgPTVEE--EVaFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1445 LSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03225 147 GVLAMDPDILLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
478-689 |
6.44e-34 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 131.16 E-value: 6.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQldiHFDVL---TVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03258 82 RRIGMIFQ---HFNLLssrTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALL--RDINRelgLTiVLITHEMEVVKRICDRVAVMEKG 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
478-689 |
1.63e-33 |
|
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: 127.50 E-value: 1.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03228 1 IEFKNVSFSY--PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQlDIH-FDvLTVEENLsilasikgipanniiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03228 78 IAYVPQ-DPFlFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
478-689 |
1.80e-33 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 129.18 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKkgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfEARKM 557
Cdd:cd03259 1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP---PERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03259 74 IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 638 LDEPTAGMDPCSR-HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03259 154 LDEPLSALDAKLReELREELKELQRELGITtIYVTHDQEEALALADRIAVMNEG 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
478-689 |
1.93e-33 |
|
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: 128.94 E-value: 1.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKkgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:cd03269 1 LEVENVTKRFGR----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-----IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03269 72 IGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 638 LDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03269 152 LDEPFSGLDPVNVELLKDvIRELARAGKTVILSTHQMELVEELCDRVLLLNKG 204
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
478-696 |
2.67e-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: 129.73 E-value: 2.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKV--LLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELlaLVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
475-691 |
4.79e-33 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 128.60 E-value: 4.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFea 554
Cdd:cd03267 15 KEPGLIGSLKSLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKF-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGIC----PQLdiHFDvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:cd03267 93 LRRIGVVfgqkTQL--WWD-LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKeYNRERGTTVlLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
477-689 |
1.15e-32 |
|
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: 127.79 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG1127 5 MIEVRNLTKSF---GDRV-VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQ---LdihFDVLTVEENLSI-LASIKGIPANNIIQEVQKVLLDLDMqtikDNQAKK----LSGGQKRKLSLG 626
Cdd:COG1127 81 RRRIGMLFQggaL---FDSLTVFENVAFpLREHTDLSEAEIRELVLEKLELVGL----PGAADKmpseLSGGMRKRVALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFS-THFMDEADILADRKAVISQG 689
Cdd:COG1127 154 RALALDPEILLYDEPTAGLDPITSAVIDELiRELRDELGLTSVVvTHDLDSAFAIADRVAVLADG 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1294-1515 |
3.14e-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: 125.32 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1294 NLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSEDDD 1371
Cdd:cd03259 5 GLSKTYGSV-----------RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDgrDVTGVPPERRN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 slkcMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:cd03259 74 ----IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03259 150 SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1292-1510 |
7.50e-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: 122.35 E-value: 7.50e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKDFllsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDD 1371
Cdd:cd00267 2 IENLSFRYGGRTAL-----------DNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 SLKCMGYCPQinplwpdttlqehfeiygavkgmsasdmkevisrithaldlkehlqktvkkLPAGIKRKLCFALSMLGNP 1451
Cdd:cd00267 71 LRRRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNP 99
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd00267 100 DLLLLDEPTSGLDPASRERLLELLR-ELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
478-689 |
1.53e-31 |
|
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: 124.16 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEAR 555
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQ-----LDIHFDVLT-VEENLSILASIKGIPANNIIQEVQKVLLDLDmQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:cd03257 82 KEIQMVFQdpmssLNPRMTIGEqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLP-EEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKkLQEELGLTLlFITHDLGVVAKIADRVAVMYAG 222
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
474-689 |
6.07e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 129.25 E-value: 6.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 474 GKEAIRISGIQKTYR-KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID- 549
Cdd:COG1123 257 AEPLLEVRNLSKRYPvRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSG--SILfdGKDLTKLSr 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 550 -EMFEARKMIGICPQ-----LDIHFDVL-TVEENLSILasiKGIPANNIIQEVQKVL----LDLDMqtikdnqAKK---- 614
Cdd:COG1123 335 rSLRELRRRVQMVFQdpyssLNPRMTVGdIIAEPLRLH---GLLSRAERRERVAELLervgLPPDL-------ADRyphe 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 405 LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdLQRELGLTyLFISHDLAVVRYIADRVAVMYDG 481
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
477-696 |
6.35e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 123.56 E-value: 6.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKGENveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARK 556
Cdd:PRK13632 7 MIKVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK-ENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ-LDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13632 84 KIGIIFQnPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 636 LLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFS-THFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13632 164 IIFDESTSMLDPKGKReIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
478-691 |
2.98e-30 |
|
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: 120.36 E-value: 2.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-----PSDGFASIYGHRVSEIDEMF 552
Cdd:cd03260 1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 553 EA-RKMIGICPQLDIHFDvLTVEENLSILASIKGIPANNIIQE-VQKVLLDLDM-QTIKDNQ-AKKLSGGQKRKLSLGIA 628
Cdd:cd03260 77 LElRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
477-710 |
3.39e-30 |
|
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: 127.96 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4987 333 SLELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED-DLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQlDIH-FDVlTVEENLSIlasikgipANN------IIQEVQKVLLD---------LDmqTIKDNQAKKLSGGQK 620
Cdd:COG4987 410 RIAVVPQ-RPHlFDT-TLRENLRL--------ARPdatdeeLWAALERVGLGdwlaalpdgLD--TWLGEGGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 621 RKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSMFL 700
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEEL 556
|
250
....*....|
gi 27262626 701 KSKWGIGYRL 710
Cdd:COG4987 557 LAQNGRYRQL 566
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
477-691 |
4.52e-30 |
|
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: 120.29 E-value: 4.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK-AFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ-----LDIHFdvlTVEENLSILASIKGIPanNIIQEVQKVLLDLDM-QTIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:COG1124 80 RVQMVFQdpyasLHPRH---TVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKdLREERGLTyLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
478-691 |
5.29e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.39 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:COG2884 2 IRFENVSKRY---PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrREIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQlDIH--FDvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:COG2884 79 RRIGVVFQ-DFRllPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 634 KILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADILADRKA---VISQGML 691
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiATH---DLELVDRMPKrvlELEDGRL 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
479-671 |
5.92e-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: 118.51 E-value: 5.92e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 479 RISGIQKTYRKKGEnveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemFEARKMI 558
Cdd:cd03226 1 RIENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 559 GICPQ-LDIHFDVLTVEENLSIlaSIKGIPANNiiQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03226 74 GYVMQdVDYQLFTDSVREELLL--GLKELDAGN--EQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190
....*....|....*....|....*....|....*
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STH 671
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIvITH 184
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1314-1519 |
7.65e-30 |
|
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: 119.46 E-value: 7.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLKcmgycP------------Q 1381
Cdd:cd03219 14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG------EDITGLP-----PheiarlgigrtfQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1382 INPLWPDTTLQE-------HFEIYGAVKGMSASDMKEVISRITHALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:cd03219 83 IPRLFPELTVLEnvmvaaqARTGSGLLLARARREEREARERAEELLErvgLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIR-ELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
497-671 |
9.73e-30 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 117.65 E-value: 9.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-GFASIYGHRVSeideMFEARKMIGICPQLDIHFDVLTVE 574
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrRTGLGVsGEVLINGRPLD----KRSFRKIIGYVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 575 ENLSILASIKGIpanniiqevqkvlldldmqtikdnqakklSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVW 654
Cdd:cd03213 101 ETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170
....*....|....*...
gi 27262626 655 NLLK-YRKANRVTVFSTH 671
Cdd:cd03213 152 SLLRrLADTGRTIICSIH 169
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
1.18e-29 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 119.04 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEidemfeARK 556
Cdd:COG1121 6 AIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ---LDIHFdVLTVEE----NLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:COG1121 76 RIGYVPQraeVDWDF-PITVRDvvlmGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTIlVVTHDLGAVREYFDRVLLLNRGLV 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
477-710 |
2.25e-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: 126.87 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIqkTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDeMFEA 554
Cdd:COG2274 473 DIELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSG--RILidGIDLRQID-PASL 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQlDIHfdvL---TVEENLSILASikGIPANNIIQ---------EVQKvlLDLDMQTIKDNQAKKLSGGQKRK 622
Cdd:COG2274 548 RRQIGVVLQ-DVF---LfsgTIRENITLGDP--DATDEEIIEaarlaglhdFIEA--LPMGYDTVVGEGGSNLSGGQRQR 619
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGSSMFLK 701
Cdd:COG2274 620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAH--RLSTIrLADRIIVLDKGRIVEDGTHEELL 697
|
....*....
gi 27262626 702 SKWGIGYRL 710
Cdd:COG2274 698 ARKGLYAEL 706
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
478-689 |
3.26e-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: 115.75 E-value: 3.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-SEIDEMFEARK 556
Cdd:cd03229 1 LELKNVSKRYGQK----TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQLDIHFDVLTVEENLSILasikgipanniiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANR-VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSLQAQLgITVvLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1319-1461 |
3.44e-29 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 114.67 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:pfam00005 4 VSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENLRLG 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1399 GAVKGMSASDMKEVISRITHALDL----KEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPST 1461
Cdd:pfam00005 84 LLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
494-689 |
3.94e-29 |
|
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: 116.76 E-value: 3.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-----EIdemfeARKMIGICPQLDIHF 568
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphER-----ARAGIGYVPEGRRIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENLsILASIKGIPANN--IIQEVqkvlLDL--DMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:cd03224 88 PELTVEENL-LLGAYARRRAKRkaRLERV----YELfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 645 MDPCSRHIVWNLLKYRKANRVTVF-STHFMDEADILADRKAVISQG 689
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEGVTILlVEQNARFALEIADRAYVLERG 208
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
475-689 |
4.05e-29 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.58 E-value: 4.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIqkTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEA 554
Cdd:PRK13635 3 EEIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE-ETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQ-LDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSL-GIAVLgN 632
Cdd:PRK13635 80 RRQVGMVFQnPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIaGVLAL-Q 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKAN-RVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQkGITVLSiTHDLDEA-AQADRVIVMNKG 216
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
477-689 |
4.18e-29 |
|
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: 123.86 E-value: 4.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVSEIDEmFE 553
Cdd:COG1123 4 LLEVRDLSVRYP--GGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE-AL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 ARKMIGICPQ-LDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:COG1123 81 RGRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTtvLLITHDLGVVAEIADRVVVMDDG 219
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
477-689 |
5.41e-29 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 117.47 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEA 554
Cdd:COG3638 2 MLELRNLSKRY---PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQldiHFDV---LTVEEN--------LSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKL 623
Cdd:COG3638 79 RRRIGMIFQ---QFNLvprLSVLTNvlagrlgrTSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 624 slGIA--VLGNPKILLLDEPTAGMDPCSRHIVWNLLkyRKANR---VTV-FSTHFMDEADILADRKAVISQG 689
Cdd:COG3638 156 --AIAraLVQEPKLILADEPVASLDPKTARQVMDLL--RRIARedgITVvVNLHQVDLARRYADRIIGLRDG 223
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
478-704 |
6.69e-29 |
|
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: 117.94 E-value: 6.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGEN-VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEA 554
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGIC---P--QLdihFDvLTVEE-------NLsilasikGIPANNIIQEVQKVL--LDLDmQTIKDNQAKKLSGGQK 620
Cdd:TIGR04521 81 RKKVGLVfqfPehQL---FE-ETVYKdiafgpkNL-------GLSEEEAEERVKEALelVGLD-EEYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 621 RKLSlgIA-VLG-NPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:TIGR04521 149 RRVA--IAgVLAmEPEVLILDEPTAGLDPKGRKEILDLFKrlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGT 226
|
250
....*....|
gi 27262626 697 SM--FLKSKW 704
Cdd:TIGR04521 227 PRevFSDVDE 236
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
478-689 |
8.88e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 119.41 E-value: 8.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEID--EMFE 553
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSG--SVLvdGVDLTALSerELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 ARKMIGICPQldiHFDVL---TVEENLSILASIKGIPANNIIQEVQKvLLDL-DMQTIKDNQAKKLSGGQKRKlsLGIA- 628
Cdd:COG1135 80 ARRKIGMIFQ---HFNLLssrTVAENVALPLEIAGVPKAEIRKRVAE-LLELvGLSDKADAYPSQLSGGQKQR--VGIAr 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 629 VL-GNPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG1135 154 ALaNNPKVLLCDEATSALDPETTRSILDLLK--DINRelgLTiVLITHEMDVVRRICDRVAVLENG 217
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
478-656 |
1.03e-28 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 116.28 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFE-ARK 556
Cdd:COG1137 4 LEAENLVKSYGKR----TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP-MHKrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170 180
....*....|....*....|....
gi 27262626 637 LLDEPTAGMDPCS----RHIVWNL 656
Cdd:COG1137 159 LLDEPFAGVDPIAvadiQKIIRHL 182
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
478-689 |
1.10e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 119.14 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQldiHFDVL---TVEENLSILASIKGIPANNIIQEVQKvLLDL-DMQTIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK11153 82 RQIGMIFQ---HFNLLssrTVFDNVALPLELAGTPKAEIKARVTE-LLELvGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 632 NPKILLLDEPTAGMDPCSRHIVWNLLKyrKANR---VT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLK--DINRelgLTiVLITHEMDVVKRICDRVAVIDAG 217
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
477-696 |
1.11e-28 |
|
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: 116.68 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG1120 1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRR-ELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ-LDIHFDvLTVEE--------NLSILASikgiPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:COG1120 76 RIAYVPQePPAPFG-LTVRElvalgrypHLGLFGR----PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRrlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
478-695 |
4.44e-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: 113.50 E-value: 4.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfEARKM 557
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQ---LDIHfdvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:cd03301 74 IAMVFQnyaLYPH---MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 635 ILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
494-689 |
5.45e-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: 114.07 E-value: 5.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---F--ASIYGHRVSEIdemfeARKmiGIC-----PQ 563
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGsvlFdgEDITGLPPHEI-----ARL--GIGrtfqiPR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 LdihFDVLTVEENLSI-------LASIKGIPANNIIQEVQKV--LLD-LDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:cd03219 86 L---FPELTVLENVMVaaqartgSGLLLARARREEREARERAeeLLErVGLADLADRPAGELSYGQQRRLEIARALATDP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 634 KILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03219 163 KLLLLDEPAAGLNPEETEELAELIRELRERGITVlLVEHDMDVVMSLADRVTVLDQG 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1290-1521 |
5.76e-28 |
|
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: 113.75 E-value: 5.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETS 1367
Cdd:cd03261 1 IELRGLTKSFGGR-----------TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDgeDISGLSE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKC-MGYCPQINPLWPDTT--------LQEHFEiygavkgMSASDMKEVISRITHALDLKEhlqkTVKKLPA--- 1435
Cdd:cd03261 70 AELYRLRRrMGMLFQSGALFDSLTvfenvafpLREHTR-------LSEEEIREIVLEKLEAVGLRG----AEDLYPAels 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1436 -GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:cd03261 139 gGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAE 218
|
....*..
gi 27262626 1515 GTVQHLK 1521
Cdd:cd03261 219 GTPEELR 225
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
496-676 |
1.02e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 122.16 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemFEARKMIGICPQldiHFDV---LT 572
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGD--IATRRRVGYMSQ---AFSLygeLT 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:NF033858 356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435
|
170 180
....*....|....*....|....*.
gi 27262626 653 VWNLL-KYRKANRVTVF-STHFMDEA 676
Cdd:NF033858 436 FWRLLiELSREDGVTIFiSTHFMNEA 461
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1314-1511 |
1.14e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 113.60 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLKcmgycP------------Q 1381
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG------RDITGLP-----PhriarlgiartfQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1382 INPLWPDTTLQEHFEI-------YGAVKGM-----SASDMKEVISRITHALD---LKEHLQKTVKKLPAGIKRKLCFALS 1446
Cdd:COG0411 87 NPRLFPELTVLENVLVaaharlgRGLLAALlrlprARREEREARERAEELLErvgLADRADEPAGNLSYGQQRRLEIARA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1447 MLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1289-1517 |
1.57e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.87 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEY-------DDKKDFLLSRKVKKVATKY----ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV 1357
Cdd:COG1134 4 MIEVENVSKSYrlyhepsRSLKELLLRRRRTRREEFWalkdVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1358 FL-GDYSS--ETSedddslkcMGYcpqiNplwPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLP 1434
Cdd:COG1134 84 EVnGRVSAllELG--------AGF----H---PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1435 AGIKRKLCFALSMLGNPQITLLDEP-STGmDP----KAKQHMwrairTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVlAVG-DAafqkKCLARI-----RELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
....*...
gi 27262626 1510 QLRCIGTV 1517
Cdd:COG1134 223 RLVMDGDP 230
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
478-676 |
1.66e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.64 E-value: 1.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRK-KGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK 556
Cdd:COG1101 2 LELKNLSKTFNPgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 --------MIGICPQLdihfdvlTVEENLSiLASIKG-----IPANNI--IQEVQKVL--LDLDMQTIKDNQAKKLSGGQ 619
Cdd:COG1101 82 igrvfqdpMMGTAPSM-------TIEENLA-LAYRRGkrrglRRGLTKkrRELFRELLatLGLGLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 620 KRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR-KANRVTVFS-THFMDEA 676
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMvTHNMEQA 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
477-696 |
2.03e-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: 112.43 E-value: 2.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfeaRK 556
Cdd:cd03296 2 SIEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQLDIHFDVLTVEENLSILASIKGI----PANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:cd03296 75 NVGFVFQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03296 155 PKVLLLDEPFGALDAKVRKELRRWLRrlHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
477-696 |
3.38e-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: 118.71 E-value: 3.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARK 556
Cdd:COG4988 336 SIELEDVSFSY---PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPA-SWRR 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQlDIHFDVLTVEENLSILASikGIPANNIIQEVQKVLLD---------LDMQtIKDNqAKKLSGGQKRKLSLGI 627
Cdd:COG4988 412 QIAWVPQ-NPYLFAGTIRENLRLGRP--DASDEELEAALEAAGLDefvaalpdgLDTP-LGEG-GRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHfmDEADI-LADRKAVISQGMLKCVGS 696
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1289-1520 |
4.31e-27 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 111.60 E-value: 4.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDdkkdfllSRKVkkvaTKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYssetse 1368
Cdd:TIGR04406 1 TLVAENLIKSYK-------KRKV----VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQ------ 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 dDDSLKCM--------GYCPQINPLWPDTTLQEHFEiygAVKGMSASDMKEVISRITHALdLKEHLQKTVKKLPA----- 1435
Cdd:TIGR04406 64 -DITHLPMherarlgiGYLPQEASIFRKLTVEENIM---AVLEIRKDLDRAEREERLEAL-LEEFQISHLRDNKAmslsg 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1436 GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:TIGR04406 139 GERRRVEIARALATNPKFILLDEPFAGVDPIAVGDIKKIIKH-LKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEG 217
|
....*
gi 27262626 1516 TVQHL 1520
Cdd:TIGR04406 218 TPAEI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1290-1510 |
4.31e-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: 109.58 E-value: 4.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETS 1367
Cdd:cd03229 1 LELKNVSKRYGQKT-----------VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgeDLTDLED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKCMGYCPQINPLWPDTTlqehfeiygavkgmsasdmkeVISRITHALDlkehlqktvkklpAGIKRKLCFALSM 1447
Cdd:cd03229 70 ELPPLRRRIGMVFQDFALFPHLT---------------------VLENIALGLS-------------GGQQQRVALARAL 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03229 116 AMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
478-689 |
4.35e-27 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 111.51 E-value: 4.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDEMFEAR 555
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQldiHFDV---LTVEEN-----LSILASIKGIPANNIIQEVQKVLLDLDMQTIKD---NQAKKLSGGQKRKLS 624
Cdd:cd03256 78 RQIGMIFQ---QFNLierLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALERVGLLDkayQRADQLSGGQQQRVA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:cd03256 155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKriNREEGITVIVSLHQVDLAREYADRIVGLKDG 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1290-1515 |
4.81e-27 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 111.09 E-value: 4.81e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEY-------DDKKDFLLSRKVKKVATKY----ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVf 1358
Cdd:cd03220 1 IELENVSKSYptykggsSSLKKLGILGRKGEVGEFWalkdVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1359 lgdyssETSEDDDSLKCMGYCPQinplwPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIK 1438
Cdd:cd03220 80 ------TVRGRVSSLLGLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMK 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1439 RKLCFALSMLGNPQITLLDEP-STGmDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03220 149 ARLAFAIATALEPDILLIDEVlAVG-DAAFQEKCQRRLR-ELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1290-1516 |
4.94e-27 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 111.17 E-value: 4.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGdyssetseD 1369
Cdd:cd03300 1 IELENVSKFYGGF-----------VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLD--------G 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQEHFEIYGAV------KGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCF 1443
Cdd:cd03300 62 KDITNLPPHKRPVNTVFQNYALFPHLTVFENIafglrlKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAI 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1444 ALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03300 142 ARALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1319-1506 |
5.29e-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: 110.32 E-value: 5.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSEtseddDSLKCMGYCPQ---INPLWPDT------ 1389
Cdd:cd03235 18 VSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE-----KERKRIGYVPQrrsIDRDFPISvrdvvl 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1390 -TLQEHfeiYGAVKGMSASDMKevisRITHALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDP 1465
Cdd:cd03235 93 mGLYGH---KGLFRRLSKADKA----KVDEALErvgLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27262626 1466 KAKQHMWRAIRTAfKNRKRAAILTTHYMEEAEAVCDRVAIM 1506
Cdd:cd03235 166 KTQEDIYELLREL-RREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1292-1516 |
5.48e-27 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 111.10 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDdkkdfllsrkvKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSE-DD 1370
Cdd:cd03218 3 AENLSKRYG-----------KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1371 DSLKCMGYCPQINPLWPDTTLQEHfeIYGAVKGMSASDmKEVISRITHALDL--KEHLQKTV-KKLPAGIKRKLCFALSM 1447
Cdd:cd03218 72 RARLGIGYLPQEASIFRKLTVEEN--ILAVLEIRGLSK-KEREEKLEELLEEfhITHLRKSKaSSLSGGERRRVEIARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03218 149 ATNPKFLLLDEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1288-1519 |
5.84e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 111.33 E-value: 5.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSEts 1367
Cdd:COG1121 5 PAIELENLTVSYGGR-----------PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 eddDSLKCMGYCPQ---INPLWP----DTTLQEHFEIYGAVKGMSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRK 1440
Cdd:COG1121 72 ---RARRRIGYVPQraeVDWDFPitvrDVVLMGRYGRRGLFRRPSRAD-REAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1441 LCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVaIMVSGQLRCIGTVQH 1519
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLR-ELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
477-696 |
9.77e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 113.63 E-value: 9.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVSEIDEmfeA 554
Cdd:COG3839 3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSG--EILigGRDVTDLPP---K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG3839 74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 635 ILLLDEPTAGMDPCSRhivWNL---LKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG3839 154 VFLLDEPLSNLDAKLR---VEMraeIKRlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
493-691 |
1.15e-26 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 109.55 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfeaRKMIGICPQ-LDIHFDV- 570
Cdd:cd03235 11 GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE------RKRIGYVPQrRSIDRDFp 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 571 LTVEE--NLSILASIKGIPANNII--QEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03235 85 ISVRDvvLMGLYGHKGLFRRLSKAdkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 647 PCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03235 165 PKTQEDIYELLReLRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
499-691 |
1.21e-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: 1.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFDIyEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVseideMFEARKMIGICPQlDIH----------F 568
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVL-NGTV-----LFDSRKKINLPPQ-QRKiglvfqqyalF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENlsILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:cd03297 88 PHLNVREN--LAFGLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27262626 649 SRHIVWNLLKYRKA--NRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03297 166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
477-788 |
1.35e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 112.49 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYR--KKGE---------------NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFAS 539
Cdd:COG4586 1 IIEVENLSKTYRvyEKEPglkgalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 540 IYGHRVSEIDEMFeaRKMIGIC----PQLdiHFDvLTVEENLSILASIKGIPaNNIIQEVQKVLLD-LDMQTIKDNQAKK 614
Cdd:COG4586 81 VLGYVPFKRRKEF--ARRIGVVfgqrSQL--WWD-LPAIDSFRLLKAIYRIP-DAEYKKRLDELVElLDLGELLDTPVRQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVF-STHFMDeaDI--LADRKAVISQGM 690
Cdd:COG4586 155 LSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKeYNRERGTTILlTSHDMD--DIeaLCDRVIVIDHGR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 691 LKCVGSSMFLKSKWGIGYRLSMYIDKYCATESLSslvkqhiPGATLLQQNDQQLVYSlpFKDMDKFSGLFSALDSHSNLG 770
Cdd:COG4586 233 IIYDGSLEELKERFGPYKTIVLELAEPVPPLELP-------RGGEVIEREGNRVRLE--VDPRESLAEVLARLLARYPVR 303
|
330
....*....|....*...
gi 27262626 771 VISygVSMTTLEDVFLKL 788
Cdd:COG4586 304 DLT--IEEPPIEEVIRRI 319
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
496-696 |
1.39e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 111.43 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFAS---IYGHRVSEiDEMFEARKMIGICPQ-LDIHFDVL 571
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTA-KTVWDIREKVGIVFQnPDNQFVGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 TVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSL-GIAVLGnPKILLLDEPTAGMDPCSR 650
Cdd:PRK13640 101 TVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIaGILAVE-PKIIILDESTSMLDPAGK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 651 HIVWNLL-KYRKANRVTVFS-THFMDEADiLADRKAVISQGMLKCVGS 696
Cdd:PRK13640 180 EQILKLIrKLKKKNNLTVISiTHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
478-694 |
1.65e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 111.29 E-value: 1.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGE-NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDE---MFE 553
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSG--KIIIDGVDITDKkvkLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 ARKMIGICPQLDIH--FDVlTVEENLSILASIKGIPANNIIQEVQKV--LLDLDMQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK13637 81 IRKKVGLVFQYPEYqlFEE-TIEKDIAFGPINLGLSEEEIENRVKRAmnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGmlKCV 694
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKLADRIIVMNKG--KCE 224
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1319-1518 |
1.74e-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: 110.13 E-value: 1.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSL------KCMGYCPQINPLWPDTTLQ 1392
Cdd:COG1120 20 VSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG------RDLASLsrrelaRRIAYVPQEPPAPFGLTVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 E--------HFeiyGAVKGMSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:COG1120 94 ElvalgrypHL---GLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1465 PKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG1120 170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
478-696 |
1.99e-26 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 107.13 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEMFEARKM 557
Cdd:cd03216 1 LELRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 -IGICPQldihfdvltveenlsilasikgipanniiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03216 76 gIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAViFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
477-689 |
2.19e-26 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 112.50 E-value: 2.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEARK 556
Cdd:COG3842 5 ALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL----PPEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 -MIGICPQ---LdihFDVLTVEEN----LsilaSIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLG-- 626
Cdd:COG3842 77 rNVGMVFQdyaL---FPHLTVAENvafgL----RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALAra 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 627 IAVlgNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:COG3842 150 LAP--EPRVLLLDEPLSALDAKLREEMREELRrLQRELGITfIYVTHDQEEALALADRIAVMNDG 212
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
478-689 |
3.08e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 112.16 E-value: 3.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRkkgeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRVSEIDEMFEARKm 557
Cdd:COG1118 3 IEVRNISKRFG----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVL-NGRDLFTNLPPRERR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQldiHFDV---LTVEENLSILASIKGIPANNIIQEVQKvLLDL-DMQTIKD---NQakkLSGGQKRKLSLGIAVL 630
Cdd:COG1118 77 VGFVFQ---HYALfphMTVAENIAFGLRVRPPSKAEIRARVEE-LLELvQLEGLADrypSQ---LSGGQRQRVALARALA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG1118 150 VEPEVLLLDEPFGALDAKVRKELRRWLRrlHDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1290-1506 |
3.20e-26 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 108.33 E-value: 3.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSE 1368
Cdd:cd03293 1 LEVRNVSKTYGGGG-------GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVlVDGEPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DddslkcMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSML 1448
Cdd:cd03293 74 D------RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1449 GNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIM 1506
Cdd:cd03293 148 VDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
494-647 |
4.06e-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: 109.36 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKmiGIC-----PQ 563
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGrilFDgrDITGLPPHRI-----ARL--GIArtfqnPR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 LdihFDVLTVEENL----------SILASIKGIPAN-----NIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:COG0411 90 L---FPELTVLENVlvaaharlgrGLLAALLRLPRArreerEARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARA 166
|
170
....*....|....*....
gi 27262626 629 VLGNPKILLLDEPTAGMDP 647
Cdd:COG0411 167 LATEPKLLLLDEPAAGLNP 185
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
479-695 |
4.07e-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: 106.75 E-value: 4.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 479 RISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMI 558
Cdd:cd03214 1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPK-ELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 559 GICPQldihfdvltveenlsilasikgipanniiqevqkVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 639 DEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRrlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1307-1523 |
6.18e-26 |
|
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: 108.19 E-value: 6.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1307 LSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSEDDDslkcMGYCPQINP 1384
Cdd:cd03299 6 LSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkDITNLPPEKRD----ISYVPQNYA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1385 LWPDTTLQEHFEiYG-AVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:cd03299 82 LFPHMTVYKNIA-YGlKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1464 DPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:cd03299 161 DVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
495-689 |
6.37e-26 |
|
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: 108.00 E-value: 6.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQLDIHFDVLTVE 574
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRLTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 575 ENLSILASIKGIPANNIIQEVQK---VLLDLdmqtiKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPcsrH 651
Cdd:TIGR03410 94 ENLLTGLAALPRRSRKIPDEIYElfpVLKEM-----LGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP---S 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 652 IVWN----LLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:TIGR03410 166 IIKDigrvIRRLRAEGGMAIlLVEQYLDFARELADRYYVMERG 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1292-1511 |
7.02e-26 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 107.59 E-value: 7.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfllsRKVKKVatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSEDD 1370
Cdd:cd03257 4 VKNLSVSFPTGG-----GSVKAL--DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIiFDGKDLLKLSRRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1371 DSL--KCMGYCPQ-----INPLWpdtTLQEHFE--IYGAVKGMSASDMKEVISRITHALDLKEHLqktVKKLPA----GI 1437
Cdd:cd03257 77 RKIrrKEIQMVFQdpmssLNPRM---TIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEV---LNRYPHelsgGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1438 KRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
488-671 |
1.03e-25 |
|
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: 106.97 E-value: 1.03e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 488 RKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGH-----RVSEIDEMfeaRKMIGICP 562
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGR---VEGGGTTSGQilfngQPRKPDQF---QKCVAYVR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QLDIHFDVLTVEENLSILASIKG--IPANNIIQEV--QKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:cd03234 88 QDDILLPGLTVRETLTYTAILRLprKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167
|
170 180 190
....*....|....*....|....*....|....
gi 27262626 639 DEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH 671
Cdd:cd03234 168 DEPTSGLDSFTALnLVSTLSQLARRNRIVILTIH 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
493-647 |
1.50e-25 |
|
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: 106.99 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FA--SIYGHRVSEIdemfeARKMIGICPQ-LDI 566
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGsirFDgeDITGLPPHRI-----ARLGIGYVPEgRRI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 hFDVLTVEENLsILASIKGIPANNIIQEVQKVLlDL--DMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:COG0410 90 -FPSLTVEENL-LLGAYARRDRAEVRADLERVY-ELfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLG 166
|
...
gi 27262626 645 MDP 647
Cdd:COG0410 167 LAP 169
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
486-689 |
1.54e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 106.52 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQlD 565
Cdd:cd03245 9 SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVPQ-D 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDVLTVEENLS----------ILASIKGIPANNIiqeVQKVLLDLDMQtIKDnQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03245 87 VTLFYGTLRDNITlgapladderILRAAELAGVTDF---VNKHPNGLDLQ-IGE-RGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 636 LLLDEPTAGMDPCS-RHIVWNLLKYRkANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:cd03245 162 LLLDEPTSAMDMNSeERLKERLRQLL-GDKTLIIITHRPSLLD-LVDRIIVMDSG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
484-691 |
1.98e-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: 105.95 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 484 QKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGIC 561
Cdd:cd03292 4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 562 PQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27262626 642 TAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKkINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1286-1516 |
2.84e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.42 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1286 EKPSIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYS 1363
Cdd:COG3842 2 AMPALELENVSKRYGDV-----------TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDgrDVT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1364 SETSEDDDslkcMGYCPQINPLWPDTTLQEHfeI-YG-AVKGMSASDMKEvisRITHALD---LKEHLQKTVKKLPAG-- 1436
Cdd:COG3842 71 GLPPEKRN----VGMVFQDYALFPHLTVAEN--VaFGlRMRGVPKAEIRA---RVAELLElvgLEGLADRYPHQLSGGqq 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1437 ----IKRklcfALSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:COG3842 142 qrvaLAR----ALAP--EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
....
gi 27262626 1513 CIGT 1516
Cdd:COG3842 216 QVGT 219
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
496-695 |
3.22e-25 |
|
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: 106.96 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQldiHFDVL- 571
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkELRELRrKKISMVFQ---SFALLp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 --TVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:cd03294 116 hrTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLI 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 650 RHIVWN-LLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03294 196 RREMQDeLLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
478-696 |
6.60e-25 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 105.01 E-value: 6.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP---HKRP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 638 LDEPTAGMDpcsrhivwnlLKYRKANRVT------------VFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:cd03300 154 LDEPLGALD----------LKLRKDMQLElkrlqkelgitfVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
497-689 |
8.66e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 105.97 E-value: 8.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-LDIHFDVLTVEE 575
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE-ENVWDIRHKIGMVFQnPDNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR-HIVW 654
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRlELIK 181
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 655 NLLKYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13650 182 TIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNG 216
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1319-1511 |
9.43e-25 |
|
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: 103.88 E-value: 9.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEdddSLKCMGYCPQiNP---LWPDTTLQEhf 1395
Cdd:cd03226 19 LSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQ-DVdyqLFTDSVREE-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYGAvkgMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAI 1475
Cdd:cd03226 93 LLLGL---KELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELI 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 1476 RTAfKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03226 170 REL-AAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
478-689 |
1.09e-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: 102.29 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIqkTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPN-ELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDvltveenlsilASIkgipANNIiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03246 78 VGYLPQDDELFS-----------GSI----AENI-----------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMdEADILADRKAVISQG 689
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATrIVIAHRP-ETLASADRILVLEDG 171
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1310-1522 |
1.24e-24 |
|
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: 104.05 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1310 KVKKVATKY--------ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLKC------ 1375
Cdd:cd03224 2 EVENLNAGYgksqilfgVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG------RDITGLPPherara 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1376 -MGYCPQINPLWPDTTLQEHFEI--YGAVKGMSASDMKEVISRIThalDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQ 1452
Cdd:cd03224 76 gIGYVPEGRRIFPELTVEENLLLgaYARRRAKRKARLERVYELFP---RLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1453 ITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
478-689 |
1.54e-24 |
|
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: 104.30 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI--DEMFEAR 555
Cdd:TIGR02315 2 LEVENLSKVY---PNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgKKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQldiHFDV---LTVEEN-----LSILASIKGIPANNIIQEVQKVLLDLDMQTIKD---NQAKKLSGGQKRKLS 624
Cdd:TIGR02315 79 RRIGMIFQ---HYNLierLTVLENvlhgrLGYKPTWRSLLGRFSEEDKERALSALERVGLADkayQRADQLSGGQQQRVA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRinKEDGITVIINLHQVDLAKKYADRIVGLKAG 222
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
492-676 |
1.58e-24 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 102.50 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 492 ENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEID----EMFEARKMIGICPQ-LDI 566
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDG---EPLDysrkGLLERRQRVGLVFQdPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 HFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR01166 80 QLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLD 159
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 647 PCSRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:TIGR01166 160 PAGREQMLAILrRLRAEGMTVVISTHDVDLA 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
497-675 |
1.78e-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: 104.40 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF-ASIYGHRVSEIDeMFEARKMIGIC-PQLDIHFDV-LTV 573
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGED-VWELRKRIGLVsPALQLRFPRdETV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EEnlSIL----ASIkGIPAN---NIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1119 98 LD--VVLsgffDSI-GLYREptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLD 174
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 647 PCSRHIVWNLLKY--RKANRVTVFSTHFMDE 675
Cdd:COG1119 175 LGARELLLALLDKlaAEGAPTLVLVTHHVEE 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1292-1515 |
2.07e-24 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 101.74 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKkdFLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDD 1371
Cdd:cd03214 2 VENLSVGYGGR--TVLDD---------LSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 SLKCMGYCPQInplwpdttlqehfeiygavkgmsasdMKEVisRITHaldLKEhlqKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:cd03214 71 LARKIAYVPQA--------------------------LELL--GLAH---LAD---RPFNELSGGERQRVLLARALAQEP 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03214 117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
488-695 |
3.12e-24 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 103.18 E-value: 3.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 488 RKKGENVEaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQLDIH 567
Cdd:cd03299 7 SKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDITNLPPEKRDISYVPQNYAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:cd03299 83 FPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 648 CSRHIVWNLLK-YRKANRVTVFS-THFMDEADILADRKAVISQGMLKCVG 695
Cdd:cd03299 163 RTKEKLREELKkIRKEFGVTVLHvTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
477-696 |
3.14e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.32 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdemfEAR- 555
Cdd:PRK10851 2 SIEIANIKKSF----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL----HARd 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQLDIHFDVLTVEEN----LSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK10851 74 RKVGFVFQHYALFRHMTVFDNiafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 632 NPKILLLDEPTAGMDPCSRHIV--W-----NLLKYrkanrVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10851 154 EPQILLLDEPFGALDAQVRKELrrWlrqlhEELKF-----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1290-1510 |
3.25e-24 |
|
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: 100.92 E-value: 3.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSED 1369
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVL---------KDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTtlqehfeiygavkgmsasdmkevisrithaldLKEHLqktvkkLPAGIKRKLCFALSMLG 1449
Cdd:cd03228 72 ESLRKNIAYVPQDPFLFSGT--------------------------------IRENI------LSGGQRQRIAIARALLR 113
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAvCDRVAIMVSGQ 1510
Cdd:cd03228 114 DPPILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1314-1516 |
3.47e-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: 100.58 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYssetsedddslkcmgycpqinplwpdttlqe 1393
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGK------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 hfeiygAVKGMSASDMKEviSRIThaldlkehlqkTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:cd03216 63 ------EVSFASPRDARR--AGIA-----------MVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFK 123
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1474 AIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGqlRCIGT 1516
Cdd:cd03216 124 VIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDG--RVVGT 163
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
459-682 |
5.04e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.53 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 459 ISFSEIIEPVSSEFVGKEAIRISGIQKTYRKKGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFA 538
Cdd:TIGR02857 301 LDAAPRPLAGKAPVTAAPASSLEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSI 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 539 SIYGHRVSEIDEMFeARKMIGICPQLDIHFDVlTVEENlsILASIKGIPANNIIQEVQKVLLD-------LDMQTIKDNQ 611
Cdd:TIGR02857 380 AVNGVPLADADADS-WRDQIAWVPQHPFLFAG-TIAEN--IRLARPDASDAEIREALERAGLDefvaalpQGLDTPIGEG 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 612 AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR-HIVWNLLKYRKaNRVTVFSTHfmDEADI-LADR 682
Cdd:TIGR02857 456 GAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEaEVLEALRALAQ-GRTVLLVTH--RLALAaLADR 525
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
486-689 |
5.99e-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: 109.19 E-value: 5.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQlD 565
Cdd:TIGR03375 470 SFAYPGQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQID-PADLRRNIGYVPQ-D 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IhfdVL---TVEENL----------SILASIKGIPANNIIQEVQKvllDLDMQTIKDNQAkkLSGGQKRKLSLGIAVLGN 632
Cdd:TIGR03375 548 P---RLfygTLRDNIalgapyaddeEILRAAELAGVTEFVRRHPD---GLDMQIGERGRS--LSGGQRQAVALARALLRD 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQG 689
Cdd:TIGR03375 620 PPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTLVLVTHRTSLLD-LVDRIIVMDNG 675
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1288-1521 |
7.28e-24 |
|
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: 102.37 E-value: 7.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDK---KDfllsrkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DY 1362
Cdd:COG1127 4 PMIEVRNLTKSFGDRvvlDG--------------VSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDgqDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1363 SSETSEDDDSL-KCMGYCPQINPLWPDTT--------LQEHFeiygavkGMSASDMKEVISRITHALDLKEHLqktvKKL 1433
Cdd:COG1127 70 TGLSEKELYELrRRIGMLFQGGALFDSLTvfenvafpLREHT-------DLSEAEIRELVLEKLELVGLPGAA----DKM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1434 PA----GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:COG1127 139 PSelsgGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADG 218
|
250
....*....|..
gi 27262626 1510 QLRCIGTVQHLK 1521
Cdd:COG1127 219 KIIAEGTPEELL 230
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1290-1511 |
9.68e-24 |
|
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: 101.03 E-value: 9.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDdkkdfllSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD----YSSE 1365
Cdd:cd03255 1 IELKNLSKTYG-------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGtdisKLSE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1366 TSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFAL 1445
Cdd:cd03255 74 KELAAFRRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1446 SMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAvCDRVAIMVSGQL 1511
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1287-1520 |
1.11e-23 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 107.30 E-value: 1.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1287 KPSIMVSNLHKEYDDKKDFLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPT---SGQVFLGDYS 1363
Cdd:COG1123 2 TPLLEVRDLSVRYPGGDVPAV---------DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1364 SETSEDDDSLKCMGYCPQ-----INPLWPDTTLQEHFEIygavKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIK 1438
Cdd:COG1123 73 LLELSEALRGRRIGMVFQdpmtqLNPVTVGDQIAEALEN----LGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1439 RKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG1123 149 QRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPE 228
|
..
gi 27262626 1519 HL 1520
Cdd:COG1123 229 EI 230
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1325-1515 |
1.33e-23 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 100.83 E-value: 1.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1325 KGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysseTSEDDDSLKC--------MGYCPQINPLWPDTTLQEHFE 1396
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG----TVLFDSRKKInlppqqrkIGLVFQQYALFPHLNVRENLA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 iYGAvKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIR 1476
Cdd:cd03297 98 -FGL-KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 27262626 1477 TAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03297 176 QIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1312-1515 |
1.44e-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: 100.41 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYcpQINPLWPDTTL 1391
Cdd:cd03301 12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF--QNYALYPHMTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:cd03301 90 YDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQM 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 1472 WRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:cd03301 170 RAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
487-696 |
1.61e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.47 E-value: 1.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 487 YRKKGENVE--ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQL 564
Cdd:PRK13633 14 YESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHFDVLT-VEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK13633 94 PDNQIVATiVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 644 GMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEAdILADRKAVISQGMLKCVGS 696
Cdd:PRK13633 174 MLDPSGRREVVNTIKelNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGT 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1288-1523 |
2.11e-23 |
|
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: 106.77 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKKdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETS 1367
Cdd:COG4988 335 PSIELEDVSFSYPGGR----------PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSLKCMGYCPQiNPLWPDTTLQEHFEIYGAvkGMSASDMKEVIsRITHALDLkehlqktVKKLPAGI---------- 1437
Cdd:COG4988 405 DPASWRRQIAWVPQ-NPYLFAGTIRENLRLGRP--DASDEELEAAL-EAAGLDEF-------VAALPDGLdtplgeggrg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1438 -----KRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAvCDRVAIMVSGQLR 1512
Cdd:COG4988 474 lsggqAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLAQ-ADRILVLDDGRIV 550
|
250
....*....|.
gi 27262626 1513 CIGTVQHLKSK 1523
Cdd:COG4988 551 EQGTHEELLAK 561
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1288-1520 |
2.42e-23 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 100.49 E-value: 2.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYddKKdfllsRKVkkvaTKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssets 1367
Cdd:COG1137 2 MTLEAENLVKSY--GK-----RTV----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1368 EDDDSL-------KCMGYCPqinplwpdttlQEH--FeiygavKGMSASD--M---------KEVISRITHALdLKE-HL 1426
Cdd:COG1137 65 EDITHLpmhkrarLGIGYLP-----------QEAsiF------RKLTVEDniLavlelrklsKKEREERLEEL-LEEfGI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1427 QKtVKKLPA-----GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAK---QHMwraIRTAfKNRKRAAILTTHYMEEAEA 1498
Cdd:COG1137 127 TH-LRKSKAyslsgGERRRVEIARALATNPKFILLDEPFAGVDPIAVadiQKI---IRHL-KERGIGVLITDHNVRETLG 201
|
250 260
....*....|....*....|..
gi 27262626 1499 VCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:COG1137 202 ICDRAYIISEGKVLAEGTPEEI 223
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
496-689 |
3.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.98 E-value: 3.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ--------LDIH 567
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHIGIVFQnpdnqfvgSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLSIlasikgiPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMD 646
Cdd:PRK13648 103 YDVAFGLENHAV-------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIaGVLAL-NPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27262626 647 PCSRHIVWNLLKYRKANR-VTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHnITIISiTHDLSEA-MEADHVIVMNKG 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
478-710 |
4.13e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 100.00 E-value: 4.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKM 557
Cdd:cd03251 1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDY-TLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQlDIHFDVLTVEENLS----------ILASIKGIPANNIIQEvqkvlLDLDMQTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:cd03251 78 IGLVSQ-DVFLFNDTVAENIAygrpgatreeVEEAARAANAHEFIME-----LPEGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQGMLKCVGSSMFLKSK 703
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAHrlstIEN-----ADRIVVLEDGKIVERGTHEELLAQ 226
|
....*..
gi 27262626 704 WGIGYRL 710
Cdd:cd03251 227 GGVYAKL 233
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
478-689 |
1.34e-22 |
|
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: 98.07 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:cd03254 3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVlTVEENLS----------ILASIKGIPANNIIQEVQKvlldlDMQTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRlgrpnatdeeVIEAAKEAGAHDFIMKLPN-----GYDTVLGENGGNLSQGERQLLAIAR 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMD---EAD--ILADRKAVISQG 689
Cdd:cd03254 153 AMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNADkiLVLDDGKIIEEG 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
486-710 |
1.36e-22 |
|
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: 98.33 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKMIGICPQLD 565
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAW-LRRQVGVVLQEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDvLTVEENLS----------ILASIKGIPANNIIQEvqkvlLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03252 86 VLFN-RSIRDNIAladpgmsmerVIEAAKLAGAHDFISE-----LPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLKCVGSSMFLKSKWGIGYRL 710
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
489-689 |
1.80e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 99.40 E-value: 1.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 489 KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-LDIH 567
Cdd:PRK13642 15 EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA-ENVWNLRRKIGMVFQnPDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13642 94 FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 648 CSRHIVWNLL-KYRKANRVTVFS-THFMDEAdILADRKAVISQG 689
Cdd:PRK13642 174 TGRQEIMRVIhEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
486-691 |
1.88e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 99.52 E-value: 1.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGenveaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGICP 562
Cdd:PRK13641 17 PMEKKG-----LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpeTGNKNLKKLRKKVSLVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QldihFDVLTVEENlSILASIKGIPAN----------NIIQEVQKVLLDLDMQtikDNQAKKLSGGQKRKLSLGIAVLGN 632
Cdd:PRK13641 92 Q----FPEAQLFEN-TVLKDVEFGPKNfgfsedeakeKALKWLKKVGLSEDLI---SKSPFELSGGQMRRVAIAGVMAYE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 633 PKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13641 164 PEILCLDEPAAGLDPEGRKEMMQLFKdYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
496-696 |
3.23e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 3.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE-------IDEMFEARKMigicpqldihF 568
Cdd:PRK11607 34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHvppyqrpINMMFQSYAL----------F 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:PRK11607 104 PHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKK 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 649 SR----HIVWNLLKYRKANRVTVfsTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11607 184 LRdrmqLEVVDILERVGVTCVMV--THDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
495-689 |
4.76e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 97.84 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS-EIDEMFEARKMIGICPQ-LDIHFDVLT 572
Cdd:PRK13639 16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQnPDDQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK13639 96 VEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQ 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 27262626 653 VWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13639 176 IMKLLYDLNKEGITiIISTHDVDLVPVYADKVYVMSDG 213
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
214-416 |
6.35e-22 |
|
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: 99.39 E-value: 6.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 214 DTFPRGVILIYLVIAFSPFGYFLAIHIVAEKEKKIKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATAsLLFPQ 293
Cdd:pfam12698 157 SGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFG-IGIPF 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 294 SSSIVIFLLFFLYGLSSVFFALMLTPLFKKSKHVGIVEFFVTVAFGFIGLMIILIESFPKSLVWLFSPFCHCTFVIGIAQ 373
Cdd:pfam12698 236 GNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDGLLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 374 VmhledfnegasfsNLTAGPYPLIITIIMLTLNSIFYVLLAVY 416
Cdd:pfam12698 316 L-------------IYGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1319-1522 |
7.94e-22 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 96.20 E-value: 7.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLKC-------MGYCPQINPLWPDTTL 1391
Cdd:COG0410 22 VSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG------EDITGLPPhriarlgIGYVPEGRRIFPSLTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIyGAVKGMSASDMKEVISRItHAL--DLKEHLqktvkKLPAGikrklcfALS-----ML-------GNPQITLLD 1457
Cdd:COG0410 96 EENLLL-GAYARRDRAEVRADLERV-YELfpRLKERR-----RQRAG-------TLSggeqqMLaigralmSRPKLLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1458 EPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
478-695 |
8.19e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 8.19e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK09700 6 ISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSI----LASIKGIPA---NNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVL 630
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 631 GNPKILLLDEPTAGM-DPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK09700 162 LDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
477-689 |
8.70e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 97.11 E-value: 8.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmFEARK 556
Cdd:PRK13647 4 IIEVEDLHFRYK---DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENE-KWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ-LDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13647 80 KVGLVFQdPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILdRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
476-689 |
1.10e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.47 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 476 EAIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDemfeAR 555
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----AD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KmiGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:COG4525 78 R--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 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 |
1.23e-21 |
|
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: 97.95 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 512 LLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQLDIHFDVLTVEENLSILASIKGIPANNI 591
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPP---HLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 592 IQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFS 669
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKtiQEQLGITFVFV 157
|
170 180
....*....|....*....|....*...
gi 27262626 670 THFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:TIGR01187 158 THDQEEAMTMSDRIAIMRKGKIAQIGTP 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
496-696 |
1.49e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 95.95 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARkmIGIC-----PQLdihFDV 570
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIAR--LGIGrkfqkPTV---FEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 571 LTVEENL--------SILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG4674 100 LTVFENLelalkgdrGVFASLFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
477-682 |
1.74e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 100.09 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRkkgeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVsEIDEMFEARK 556
Cdd:COG1129 4 LLEMRGISKSFG----GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV-RFRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 M-IGICPQ-LDIhFDVLTVEENLSI---LASIKGIPANNIIQEVQKVL----LDLDMQTIkdnqAKKLSGGQKRKLSLGI 627
Cdd:COG1129 79 AgIAIIHQeLNL-VPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLarlgLDIDPDTP----VGDLSVAQQQLVEIAR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADR 682
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAiIYISHRLDEVFEIADR 209
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
478-689 |
2.49e-21 |
|
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: 94.13 E-value: 2.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:cd03262 1 IEIKNLHKSF---GDF-HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkkNINEL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 aRKMIGICPQldiHFDV---LTVEENLsILASIK--GIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIA 628
Cdd:cd03262 75 -RQKVGMVFQ---QFNLfphLTVLENI-TLAPIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTmVVVTHEMGFAREVADRVIFMDDG 211
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
473-696 |
3.05e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 96.84 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 473 VGKEAIRISGIQKTYRKKGEN-VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASI----------- 540
Cdd:PRK13631 17 SDDIILRVKNLYCVFDEKQENeLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 541 ----YGHRVSEIDEMFEARKMIGIC---PQLDIHFDvlTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQ-TIKDNQA 612
Cdd:PRK13631 97 heliTNPYSKKIKNFKELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 613 KKLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFS-THFMDEADILADRKAVISQGM 690
Cdd:PRK13631 175 FGLSGGQKRRVAIaGILAI-QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFViTHTMEHVLEVADEVIVMDKGK 253
|
....*.
gi 27262626 691 LKCVGS 696
Cdd:PRK13631 254 ILKTGT 259
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1319-1510 |
3.05e-21 |
|
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: 94.77 E-value: 3.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF--LG-DYSSETSEDddsLKC-MGYCpqinplwpDTTLQEH 1394
Cdd:COG1119 22 ISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVrlFGeRRGGEDVWE---LRKrIGLV--------SPALQLR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 FEiygavKGMSASDMkeVIS---------------------RITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQI 1453
Cdd:COG1119 91 FP-----RDETVLDV--VLSgffdsiglyreptdeqrerarELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPEL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1454 TLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:COG1119 164 LILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
497-658 |
3.65e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 100.12 E-value: 3.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGHRVsEIDEMfeaRKMIGICPQLDIHFDVLTV 573
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPI-DAKEM---RAISAYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSILASIK---GIPANNIIQEVQKVLLDLDMQTIKD------NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:TIGR00955 117 REHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170
....*....|....
gi 27262626 645 MDPCSRHIVWNLLK 658
Cdd:TIGR00955 197 LDSFMAYSVVQVLK 210
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
478-647 |
4.60e-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: 93.91 E-value: 4.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMfe 553
Cdd:COG1126 2 IEIENLHKSF---GDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskkDINKL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 aRKMIGICPQldiHFDV---LTVEENLsILASIK--GIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQK------RK 622
Cdd:COG1126 76 -RRKVGMVFQ---QFNLfphLTVLENV-TLAPIKvkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQqrvaiaRA 150
|
170 180
....*....|....*....|....*
gi 27262626 623 LSLgiavlgNPKILLLDEPTAGMDP 647
Cdd:COG1126 151 LAM------EPKVMLFDEPTSALDP 169
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
475-703 |
6.59e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 94.07 E-value: 6.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCP--PSDGFASIYGHRV-SEI 548
Cdd:PRK14239 3 EPILQVSDLSVYYNKK----KALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIySPR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 549 DEMFEARKMIGICPQLDIHFDvLTVEENLSILASIKGIPANNIIQE-VQKVLLDLDM-QTIKD---NQAKKLSGGQKRKL 623
Cdd:PRK14239 79 TDTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEaVEKSLKGASIwDEVKDrlhDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SMFLK 701
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDtkQMFMN 237
|
..
gi 27262626 702 SK 703
Cdd:PRK14239 238 PK 239
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
491-696 |
7.95e-21 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.70 E-value: 7.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 491 GENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQlDIH-FD 569
Cdd:COG1132 350 PGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIGVVPQ-DTFlFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 570 vLTVEENLSIlasikGIP-ANNiiQEVQKVL-----------LDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG1132 428 -GTIRENIRY-----GRPdATD--EEVEEAAkaaqahefieaLPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 638 LDEPTAGMDPCS-RHIVWNLLKYRKaNRVTVFSTH----FMDeadilADRKAVISQGMLKCVGS 696
Cdd:COG1132 500 LDEATSALDTETeALIQEALERLMK-GRTTIVIAHrlstIRN-----ADRILVLDDGRIVEQGT 557
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1258-1530 |
8.37e-21 |
|
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: 99.14 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1258 PPDNEDEDEDVKAERLKvkelmgcqcceekPSIMVSNLHKEYDDKKDFLLSRkvkkvatkyISFCVKKGEILGLLGPNGA 1337
Cdd:COG2274 455 PPEREEGRSKLSLPRLK-------------GDIELENVSFRYPGDSPPVLDN---------ISLTIKPGERVAIVGRSGS 512
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1338 GKSTIINILVGDIEPTSGQVFLGDYSSEtSEDDDSL-KCMGYCPQINPLWPDT-----TLqehfeiygavkGMSASDMKE 1411
Cdd:COG2274 513 GKSTLLKLLLGLYEPTSGRILIDGIDLR-QIDPASLrRQIGVVLQDVFLFSGTireniTL-----------GDPDATDEE 580
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1412 VI--SRITHALDLKEHLQK---TV-----KKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKN 1481
Cdd:COG2274 581 IIeaARLAGLHDFIEALPMgydTVvgeggSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKG 660
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 27262626 1482 RKRaaILTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFL 1530
Cdd:COG2274 661 RTV--IIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
477-647 |
9.27e-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: 9.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS---EIDE--M 551
Cdd:COG4161 2 SIQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 FEARKMIGICPQ---LDIHfdvLTVEENLsILASIK--GIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLG 626
Cdd:COG4161 78 RLLRQKVGMVFQqynLWPH---LTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180
....*....|....*....|.
gi 27262626 627 IAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALDP 174
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
478-689 |
9.84e-21 |
|
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: 92.56 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03244 3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG-LHDLRSR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQ------------LDIhFDVLTVEENLSILASIKgipannIIQEVQKVLLDLDMQtIKDNQaKKLSGGQKRKLSL 625
Cdd:cd03244 80 ISIIPQdpvlfsgtirsnLDP-FGEYSDEELWQALERVG------LKEFVESLPGGLDTV-VEEGG-ENLSVGQRQLLCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH----FMDeadilADRKAVISQG 689
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHrldtIID-----SDRILVLDKG 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
477-696 |
1.14e-20 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIY--GHRVsEIDEMFEA 554
Cdd:COG3845 5 ALELRGITKRF---G-GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSG--EILidGKPV-RIRSPRDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKM-IGICPQldiHF---DVLTVEENLsILASIKG----IPANNIIQEVQKVL------LDLDmQTIKDnqakkLSGGQK 620
Cdd:COG3845 78 IALgIGMVHQ---HFmlvPNLTVAENI-VLGLEPTkggrLDRKAARARIRELSerygldVDPD-AKVED-----LSVGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 621 RKLSlgI--AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGmlKCVGS 696
Cdd:COG3845 148 QRVE--IlkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIiFITHKLREVMAIADRVTVLRRG--KVVGT 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1289-1517 |
1.19e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 93.96 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDKKDFllsrkvKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSET 1366
Cdd:PRK13637 2 SIKIENLTHIYMEGTPF------EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvDITDKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDDDSLKCMGYCPQinplWPDTTLqehFE-------IYGAVK-GMSASDMKEVISRITHA--LDLKEHLQKTVKKLPAG 1436
Cdd:PRK13637 76 VKLSDIRKKVGLVFQ----YPEYQL---FEetiekdiAFGPINlGLSEEEIENRVKRAMNIvgLDYEDYKDKSPFELSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1437 IKRKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK13637 149 QKRRVAIAgvVAM--EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
...
gi 27262626 1515 GTV 1517
Cdd:PRK13637 227 GTP 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
497-680 |
1.27e-20 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.77 E-value: 1.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEIDEmfEARKmIGICPQLDIHFDVLTV 573
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPA--EQRR-IGILFQDDLLFPHLSV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSiLASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC----S 649
Cdd:COG4136 94 GENLA-FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAlraqF 172
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 650 RHIVWNLLkyRKANRVTVFSTHfmDEADILA 680
Cdd:COG4136 173 REFVFEQI--RQRGIPALLVTH--DEEDAPA 199
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
499-689 |
1.41e-20 |
|
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: 91.79 E-value: 1.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQLDIHFDVLTVEEN 576
Cdd:cd03298 14 PMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 LSiLASIKGIPANNIIQE-VQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:cd03298 91 VG-LGLSPGLKLTAEDRQaIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 656 L-LKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03298 170 LvLDLHAETKMTVlMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
493-689 |
1.47e-20 |
|
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: 92.68 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQldihfDvlT 572
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT-LDSLRRAIGVVPQ-----D--T 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSILASIK-GIP-ANNI-IQEVQKV--LLDLDMQ------TIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:cd03253 85 VLFNDTIGYNIRyGRPdATDEeVIEAAKAaqIHDKIMRfpdgydTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 27262626 642 TAGMD-PCSRHIVWNLLKYRKaNRVTVFSTHFMDEAdILADRKAVISQG 689
Cdd:cd03253 165 TSALDtHTEREIQAALRDVSK-GRTTIVIAHRLSTI-VNADKIIVLKDG 211
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
483-696 |
1.51e-20 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 92.65 E-value: 1.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 483 IQKTYrkKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICP 562
Cdd:PRK10895 9 LAKAY--KGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QLDIHFDVLTVEENL-SILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK10895 85 QEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 642 TAGMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1289-1518 |
1.68e-20 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 94.83 E-value: 1.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDkkdFLLSRKVkkvatkyiSFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD---YSSE 1365
Cdd:COG1118 2 SIEVRNISKRFGS---FTLLDDV--------SLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGrdlFTNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1366 TSEDDDslkcMGYCPQiNP-LWPDTTLQEHfeI-YGA-VKGMSASDMKEVISRITHALDLkEHLQktvKKLPAgikrklc 1442
Cdd:COG1118 71 PPRERR----VGFVFQ-HYaLFPHMTVAEN--IaFGLrVRPPSKAEIRARVEELLELVQL-EGLA---DRYPS------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1443 fALS-----------ML-GNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:COG1118 133 -QLSggqrqrvalarALaVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGR 211
|
....*...
gi 27262626 1511 LRCIGTVQ 1518
Cdd:COG1118 212 IEQVGTPD 219
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
497-689 |
2.23e-20 |
|
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: 91.76 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEM--FEARKMigicpqldihFDVLT 572
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgPDRMvvFQNYSL----------LPWLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSiLASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:TIGR01184 71 VRENIA-LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRpgqLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 650 R-HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR01184 150 RgNLQEELMQIWEEHRVTvLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
448-671 |
2.33e-20 |
|
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: 97.05 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 448 EELSEGNVNGNISFSEIIEPVSSEFVGKEAIRISgiqktYRKKGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNIL 527
Cdd:TIGR02868 308 VEVLDAAGPVAEGSAPAAGAVGLGKPTLELRDLS-----AGYPGAP-PVLDGVSLDLPPGERVAILGPSGSGKSTLLATL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 528 CGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQlDIH-FDVlTVEENLSILAsikgipANNIIQEVQKVL------- 599
Cdd:TIGR02868 382 AGLLDPLQGEVTLDGVPVSSLDQD-EVRRRVSVCAQ-DAHlFDT-TVRENLRLAR------PDATDEELWAALervglad 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 600 ----LDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR02868 453 wlraLPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITH 528
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
480-658 |
3.42e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 97.10 E-value: 3.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 480 ISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA---RK 556
Cdd:PRK10535 7 LKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ---LDIHfdvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK10535 87 HFGFIFQryhLLSH---LTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180
....*....|....*....|....*
gi 27262626 634 KILLLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILH 188
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
491-671 |
3.48e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 90.70 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 491 GENVEALR-------NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRvSEIDEMFEARKMIGicpq 563
Cdd:PRK13539 5 GEDLACVRggrvlfsGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEACHYLG---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 ldiHFD----VLTVEENLSILASIKGIPANNIIQevqkVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:PRK13539 80 ---HRNamkpALTVAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 640 EPTAGMDPCSRHIVWNLLKYR-KANRVTVFSTH 671
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHlAQGGIVIAATH 185
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
478-710 |
4.32e-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: 91.06 E-value: 4.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKM 557
Cdd:cd03249 1 IEFKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN-LRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVlTVEENLS----------ILASIKGIPANNIIQEvqkvlLDLDMQTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRygkpdatdeeVEEAAKKANIHDFIMS-----LPDGYDTLVGERGSQLSGGQKQRIAIAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 628 AVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMdeADIL-ADRKAVISQGMLKCVGSSMFLKSKWGI 706
Cdd:cd03249 153 ALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRnADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
....
gi 27262626 707 GYRL 710
Cdd:cd03249 231 YAKL 234
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
478-689 |
4.96e-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: 89.29 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARKM 557
Cdd:cd03247 1 LSINNVSFSY--PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK--ALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVltveenlsilasikgipanniiqevqkvlldldmqTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03247 77 ISVLNQRPYLFDT-----------------------------------TLRNNLGRRFSGGERQRLALARILLQDAPIVL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH------FMDEAdILADRKAVISQG 689
Cdd:cd03247 122 LDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHhltgieHMDKI-LFLENGKIIMQG 178
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
496-712 |
6.25e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 92.01 E-value: 6.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyGHRV--SEIDE--MFEARKMIGICPQLDIH--FD 569
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVitAGKKNkkLKPLRKKVGIVFQFPEHqlFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 570 VlTVEENLSILASIKGIPANNIIQEVQKV--LLDLDmQTIKDNQAKKLSGGQKRKLSlgIA-VLG-NPKILLLDEPTAGM 645
Cdd:PRK13634 101 E-TVEKDICFGPMNFGVSEEDAKQKAREMieLVGLP-EELLARSPFELSGGQMRRVA--IAgVLAmEPEVLVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 646 DPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS--SMFLKSKWGIGYRLSM 712
Cdd:PRK13634 177 DPKGRKEMMEMFYklHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTprEIFADPDELEAIGLDL 247
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1285-1520 |
6.50e-20 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 95.36 E-value: 6.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1285 EEKPSIMVSNLHKEYDdkkdflLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DY 1362
Cdd:COG1123 256 AAEPLLEVRNLSKRYP------VRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkDL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1363 SSETSEDDDSL-KCMGYCPQ-----INPLWP-DTTLQEHFEIYGavkGMSASDMKEvisRITHALDL----KEHLQKTVK 1431
Cdd:COG1123 330 TKLSRRSLRELrRRVQMVFQdpyssLNPRMTvGDIIAEPLRLHG---LLSRAERRE---RVAELLERvglpPDLADRYPH 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1432 KLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG1123 404 ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
....*....
gi 27262626 1512 RCIGTVQHL 1520
Cdd:COG1123 484 VEDGPTEEV 492
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1295-1516 |
7.25e-20 |
|
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: 91.55 E-value: 7.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1295 LHKEYDDKKDfLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSL- 1373
Cdd:cd03294 20 LLAKGKSKEE-ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRe 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1374 ---KCMGYCPQINPLWPDTTLQEHFEiYG-AVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:cd03294 99 lrrKKISMVFQSFALLPHRTVLENVA-FGlEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAV 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03294 178 DPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGT 244
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1290-1520 |
7.26e-20 |
|
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: 90.32 E-value: 7.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINIL-----VGDIEPTSGQVFL-GDYS 1363
Cdd:cd03260 1 IELRDLNVYYGDKH-----------ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndLIPGAPDEGEVLLdGKDI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1364 SETSEDDDSLKC-MGYCPQI-NPLwpDTTLQEHFEiYGA-VKGMsaSDMKEVISRITHALDlKEHLQKTVK------KLP 1434
Cdd:cd03260 70 YDLDVDVLELRRrVGMVFQKpNPF--PGSIYDNVA-YGLrLHGI--KLKEELDERVEEALR-KAALWDEVKdrlhalGLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1435 AGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfkNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:cd03260 144 GGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAEL--KKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEF 221
|
....*.
gi 27262626 1515 GTVQHL 1520
Cdd:cd03260 222 GPTEQI 227
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1319-1511 |
8.57e-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: 8.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVG--DIEPTSGQVFLGDYSSetseDDDSLKC-MGYCPQINPLWPDTTLQEhf 1395
Cdd:cd03213 28 VSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPL----DKRSFRKiIGYVPQDDILHPTLTVRE-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 eiygavkgmsasdmkevisrithALDLKEHLqktvKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAI 1475
Cdd:cd03213 102 -----------------------TLMFAAKL----RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLL 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 27262626 1476 RtAFKNRKRAAILTTHYM-EEAEAVCDRVAIMVSGQL 1511
Cdd:cd03213 155 R-RLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
478-696 |
9.58e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 93.09 E-value: 9.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEARkm 557
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA--ENR-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 igicpqlDIH--------FDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK09452 87 -------HVNtvfqsyalFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 630 LGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK09452 160 VNKPKVLLLDESLSALDYKLRKQMQNELKAlqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
477-647 |
1.37e-19 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDE--M 551
Cdd:PRK11124 2 SIQLNGINCFY---GAH-QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDkaI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 FEARKMIGICPQ---LDIHfdvLTVEENLsILASIK--GIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLG 626
Cdd:PRK11124 78 RELRRNVGMVFQqynLWPH---LTVQQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIA 153
|
170 180
....*....|....*....|.
gi 27262626 627 IAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDP 174
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1289-1516 |
1.43e-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: 89.71 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDkkdFllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSET 1366
Cdd:cd03296 2 SIEVRNVSKRFGD---F--------VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGgeDATDVP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDddslKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPA----GIKRKLC 1442
Cdd:cd03296 71 VQE----RNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAqlsgGQRQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1443 FALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03296 147 LARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1286-1515 |
1.68e-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: 94.10 E-value: 1.68e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1286 EKPSIMVSNLHKEYddkkdFLLSRKVKKvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF--LGDYS 1363
Cdd:TIGR03269 276 GEPIIKVRNVSKRY-----ISVDRGVVK-AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEW 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1364 SETSEDDDSLK-----CMGYCPQINPLWPDTTLQEHF-EIYGAVKGMSASDMKEVISRITHALD---LKEHLQKTVKKLP 1434
Cdd:TIGR03269 350 VDMTKPGPDGRgrakrYIGILHQEYDLYPHRTVLDNLtEAIGLELPDELARMKAVITLKMVGFDeekAEEILDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1435 AGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKI 509
|
.
gi 27262626 1515 G 1515
Cdd:TIGR03269 510 G 510
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1314-1525 |
1.85e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.19 E-value: 1.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GdySSETSEDDDSLKCMGYCPQINPLWPDTTLQ 1392
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfG--QPVDAGDIATRRRVGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:NF033858 358 QNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1473 RAI----RtafknRKRAAI-LTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:NF033858 438 RLLielsR-----EDGVTIfISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG 489
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
478-696 |
1.92e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 90.43 E-value: 1.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKM 557
Cdd:PRK13644 2 IRLENVSYSYP---DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQ-LDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK13644 79 VGIVFQnPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 637 LLDEPTAGMDPCS-RHIVWNLLKYRKANRVTVFSTHFMDEADIlADRKAVISQGMLKCVGS 696
Cdd:PRK13644 159 IFDEVTSMLDPDSgIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
484-689 |
2.08e-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: 88.74 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 484 QKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhRVSEIDEMfearkMIGICPQ 563
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL-----GGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 ldihfdvLTVEENLSILASIKGIPANNIIQEVQKVL--------LDLDMqtikdnqaKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:cd03220 99 -------LTGRENIYLNGRLLGLSRKEIDEKIDEIIefselgdfIDLPV--------KTYSSGMKARLAFAIATALEPDI 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQG 689
Cdd:cd03220 164 LLIDEVLAVGDAAFQEKCQRRLRELLKQGKTViLVSHDPSSIKRLCDRALVLEKG 218
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
490-658 |
2.88e-19 |
|
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: 87.30 E-value: 2.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 490 KGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcppsdgfASIYGHRVSEI-------DEMFeaRKMIGICP 562
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--------RKTAGVITGEIlingrplDKNF--QRSTGYVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QLDIHFDVLTVEENLSILASIKGipanniiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:cd03232 86 QQDVHSPNLTVREALRFSALLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPT 136
|
170
....*....|....*.
gi 27262626 643 AGMDPCSRHIVWNLLK 658
Cdd:cd03232 137 SGLDSQAAYNIVRFLK 152
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1290-1520 |
3.77e-19 |
|
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: 88.41 E-value: 3.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDkkdfllsRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSED 1369
Cdd:cd03258 2 IELKNVSKVFGD-------TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLV-DGTDLTLLS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSL----KCMGYCPQ-INPLWPDTTLQE---HFEIYGavkgmsaSDMKEVISRITHAL---DLKEHLQKTVKKLPAGIK 1438
Cdd:cd03258 74 GKELrkarRRIGMIFQhFNLLSSRTVFENvalPLEIAG-------VPKAEIEERVLELLelvGLEDKADAYPAQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1439 RKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:cd03258 147 QRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVE 226
|
..
gi 27262626 1519 HL 1520
Cdd:cd03258 227 EV 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
478-691 |
4.01e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 88.01 E-value: 4.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKkgeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR 555
Cdd:PRK10908 2 IRFEHVSKAYLG---GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKnrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KMIGICPQlDIHFDV-LTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK10908 79 RQIGMIFQ-DHHLLMdRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 635 ILLLDEPTAGMDPCSRHIVWNLlkYRKANRVTV---FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRL--FEEFNRVGVtvlMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
494-689 |
5.55e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 88.01 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQLDIHFDVLTV 573
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSIlasiKGIPAN--NIIQEVQKVL-LDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:PRK11614 98 EENLAM----GGFFAErdQFQERIKWVYeLFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIII 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 651 HIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQG 689
Cdd:PRK11614 174 QQIFDTIEQLREQGMTIFLVeQNANQALKLADRGYVLENG 213
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1319-1506 |
6.64e-19 |
|
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: 92.35 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQiNPLWPDTTLQEhfEIY 1398
Cdd:TIGR02857 341 VSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQ-HPFLFAGTIAE--NIR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKEVISRiTHALDLkehlqktVKKLPAGI---------------KRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:TIGR02857 418 LARPDASDAEIREALER-AGLDEF-------VAALPQGLdtpigeggaglsggqAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1464 DPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAvCDRVAIM 1506
Cdd:TIGR02857 490 DAETEAEVLEALRALAQG--RTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
495-689 |
8.03e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.75 E-value: 8.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE-MFEARKMIGICPQ-LDIHFDVLT 572
Cdd:PRK13636 20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKgLMKLRESVGMVFQdPDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 27262626 653 VWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13636 180 IMKLLVemQKELGLTIIIATHDIDIVPLYCDNVFVMKEG 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1287-1512 |
8.29e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1287 KPSIMVSNLHKEYDDKKdfLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGdysset 1366
Cdd:COG0488 313 KKVLELEGLSKSYGDKT--LLDD---------LSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG------ 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 seddDSLKcMGYCPQIN-PLWPDTTLQEHFEIYgavkgmsASDMKEvisriTHALDL-------KEHLQKTVKKLPAGIK 1438
Cdd:COG0488 376 ----ETVK-IGYFDQHQeELDPDKTVLDELRDG-------APGGTE-----QEVRGYlgrflfsGDDAFKPVGVLSGGEK 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1439 RKLCFALSMLGNPQITLLDEPSTGMDPKAKQhmwrAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:COG0488 439 ARLALAKLLLSPPNVLLLDEPTNHLDIETLE----ALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
495-691 |
8.64e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 88.68 E-value: 8.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---HRVSEIDEMFEARKMIGIC---PQLDIHF 568
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitiTHKTKDKYIRPVRKRIGMVfqfPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DvlTVEENLSILASIKGIPANNIIQEVQKVLLDLDM-QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13646 101 D--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 648 CSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13646 179 QSKRQVMRLLKslQTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
476-696 |
8.69e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 8.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 476 EAIRISGIQKTYR------------------KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF 537
Cdd:COG1134 3 SMIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 538 ASIYGhRVSEIDEMfearkMIGICPQldihfdvLTVEENLSILASIKGIPAnniiQEVQKVL------------LDLDMQ 605
Cdd:COG1134 83 VEVNG-RVSALLEL-----GAGFHPE-------LTGRENIYLNGRLLGLSR----KEIDEKFdeivefaelgdfIDQPVK 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 606 TikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-----CSRHIvwnlLKYRKANRVTVFSTHFMDEADILA 680
Cdd:COG1134 146 T--------YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkkCLARI----RELRESGRTVIFVSHSMGAVRRLC 213
|
250
....*....|....*.
gi 27262626 681 DRKAVISQGMLKCVGS 696
Cdd:COG1134 214 DRAIWLEKGRLVMDGD 229
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
473-695 |
9.06e-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: 91.79 E-value: 9.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 473 VGKEAIRISGIQKTYRKKGENV-EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIyghRVSE---- 547
Cdd:TIGR03269 275 VGEPIIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNV---RVGDewvd 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 548 -----IDEMFEARKMIGICPQ---LDIHFDVLtveENLSILASIKgIPANniiQEVQKVLLDLDMQTIKDNQAK------ 613
Cdd:TIGR03269 352 mtkpgPDGRGRAKRYIGILHQeydLYPHRTVL---DNLTEAIGLE-LPDE---LARMKAVITLKMVGFDEEKAEeildky 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 614 --KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKA-NRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR03269 425 pdELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*.
gi 27262626 690 MLKCVG 695
Cdd:TIGR03269 505 KIVKIG 510
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
486-691 |
9.76e-19 |
|
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: 87.14 E-value: 9.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARK--MIGICPQ 563
Cdd:cd03248 20 AYPTR-PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKvsLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 L-------DIHFDVLTVEENlSILASIKGIPANNIIQEVQKvlldlDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03248 99 LfarslqdNIAYGLQSCSFE-CVKEAAQKAHAHSFISELAS-----GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:cd03248 173 ILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
441-642 |
1.07e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.66 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 441 SKSKRN------YEEL-------SEGNVNgnISFSEiiepvsSEFVGKEAIRISGIQKTYrkkgENVEALRNLSFDIYEG 507
Cdd:COG0488 274 RKAKQAqsrikaLEKLereepprRDKTVE--IRFPP------PERLGKKVLELEGLSKSY----GDKTLLDDLSLRIDRG 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 508 QITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSeidemfearkmIGICPQldiHFDVLtvEENLSILASIKGI 586
Cdd:COG0488 342 DRIGLIGPNGAGKSTLLKLLAGELEPDSG--TVkLGETVK-----------IGYFDQ---HQEEL--DPDKTVLDELRDG 403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 587 PANNIIQEVQKVLLDL----DMQtikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG0488 404 APGGTEQEVRGYLGRFlfsgDDA---FKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPT 460
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1308-1520 |
1.35e-18 |
|
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: 86.97 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1308 SRKVKKVATKYISFCVKKGEILGLLGPNGAGKST---IINILvgdIEPTSGQVFLGDysSETSEDDDS--LKCMGYCPQI 1382
Cdd:cd03295 9 RYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTtmkMINRL---IEPTSGEIFIDG--EDIREQDPVelRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1383 NPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDL--KEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPS 1460
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPF 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1461 TGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:cd03295 164 GALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1319-1511 |
2.15e-18 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 84.19 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTtlqehfeiy 1398
Cdd:cd03246 21 VSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDDELFSGS--------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 gavkgmsasdMKEVIsrithaldlkehlqktvkkLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRtA 1478
Cdd:cd03246 92 ----------IAENI-------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIA-A 141
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 1479 FKNRKRAAILTTHYMEEAEAvCDRVAIMVSGQL 1511
Cdd:cd03246 142 LKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
486-703 |
2.48e-18 |
|
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: 90.48 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFEarKMIGICPQl 564
Cdd:TIGR01842 323 TIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDrETFG--KHIGYLPQ- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHFDVLTVEENLS----ILASIKGIPANNIIQeVQKVLLDLDM--QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:TIGR01842 400 DVELFPGTVAENIArfgeNADPEKIIEAAKLAG-VHELILRLPDgyDTVIGPGGATLSGGQRQRIALARALYGDPKLVVL 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHfMDEADILADRKAVISQGMLKCVGSSMFLKSK 703
Cdd:TIGR01842 479 DEPNSNLDEEGEQALANAIKALKARGITVvVITH-RPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
478-689 |
2.51e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.50 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKM 557
Cdd:PRK15439 12 LCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 -IGICPQLDIHFDVLTVEENlsILAsikGIPAN--------NIIQEVQkVLLDLDMQT----IKDNQAKKLSGGQKRkls 624
Cdd:PRK15439 87 gIYLVPQEPLLFPNLSVKEN--ILF---GLPKRqasmqkmkQLLAALG-CQLDLDSSAgsleVADRQIVEILRGLMR--- 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 625 lgiavlgNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRV-TVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK15439 158 -------DSRILILDEPTASLTPAETERLFSRIRELLAQGVgIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1290-1510 |
2.52e-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: 86.08 E-value: 2.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLlsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSED 1369
Cdd:cd03256 1 IEVENLSKTYPNGKKAL----------KDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDI-NKLK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKcmGYCPQINPLWPDTTLQEHFEIYGAV-----------KGMSASDMKEVISRITHALD---LKEHLQKTVKKLPA 1435
Cdd:cd03256 70 GKALR--QLRRQIGMIFQQFNLIERLSVLENVlsgrlgrrstwRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1436 GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:cd03256 148 GQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
478-696 |
2.65e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 2.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGE-NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG---FASIYGHRVSEIDEMFE 553
Cdd:PRK13643 2 IKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtVGDIVVSSTSKQKEIKP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 ARKMIGICPQLDihfDVLTVEEnlSILASIKGIPANNII--QEVQKVLLD-LDMQTIKDNQAKK----LSGGQKRKLSLG 626
Cdd:PRK13643 82 VRKKVGVVFQFP---ESQLFEE--TVLKDVAFGPQNFGIpkEKAEKIAAEkLEMVGLADEFWEKspfeLSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFEsIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
496-691 |
3.05e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 86.72 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEMFEARKMIGICPQLDihfDVLT 572
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstSKNKDIKQIRKKVGLVFQFP---ESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEEnlSILASIKGIPANNIIQEVQKVLL---DLDMQTIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PRK13649 99 FEE--TVLKDVAFGPQNFGVSQEEAEALareKLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27262626 646 DPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTiVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
500-696 |
3.42e-18 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 88.25 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhRVseideMFEARKMIgicpQLDIH------------ 567
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RT-----LFDSRKGI----FLPPEkrrigyvfqear 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 -FDVLTVEENLSILASIKGIPANNIIQEvqKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR02142 86 lFPHLSVRGNLRYGMKRARPSERRISFE--RVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 647 -PCSRHIVWNLLKYRKANRV-TVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:TIGR02142 164 dPRKYEILPYLERLHAEFGIpILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
483-646 |
4.46e-18 |
|
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: 84.24 E-value: 4.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 483 IQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLcppSDGFASIYGHrVS----EIDEMFE-ARKM 557
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGD-IHyngiPYKEFAEkYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGipaNNIIqevqkvlldldmqtikdnqaKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG---NEFV--------------------RGISGGERKRVSIAEALVSRASVLC 141
|
....*....
gi 27262626 638 LDEPTAGMD 646
Cdd:cd03233 142 WDNSTRGLD 150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
496-696 |
4.55e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 88.55 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEAR-KMIGICPQLDIHFDVLT 572
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaELREVRrKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHI 652
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 653 VWN-LLKYR-KANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK10070 203 MQDeLVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1314-1517 |
5.56e-18 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 89.32 E-value: 5.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYCPQinplwpdttlq 1392
Cdd:COG3845 19 VANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALgIGMVHQ----------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 eHF---------E--IYGAVKGMSAS-DMKEVISRITHALD---LKEHLQKTVKKLPAGIKRKL----CfalsMLGNPQI 1453
Cdd:COG3845 88 -HFmlvpnltvaEniVLGLEPTKGGRlDRKAARARIRELSErygLDVDPDAKVEDLSVGEQQRVeilkA----LYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1454 TLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLrcIGTV 1517
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILR-RLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGTV 223
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
501-696 |
6.23e-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: 87.46 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMFEARKmIGICPQLDIHFDVLTVEEN 576
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdSARGIFLPPHRRR-IGYVFQEARLFPHLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 LsiLASIKGIPANNIIQEVQKV--------LLDLDMQTikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPC 648
Cdd:COG4148 98 L--LYGRKRAPRAERRISFDEVvellgighLLDRRPAT--------LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 649 SRHivwNLLKY-----RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:COG4148 168 RKA---EILPYlerlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1312-1511 |
8.95e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 83.79 E-value: 8.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQinplwpDTTL 1391
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQ------DVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 qehfeIYGAVK-----GMSASDMKEVI--SRITHALDLkehlqktVKKLPAGIKRKLC---FALS------------MLG 1449
Cdd:cd03245 90 -----FYGTLRdnitlGAPLADDERILraAELAGVTDF-------VNKHPNGLDLQIGergRGLSggqrqavalaraLLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAFknRKRAAILTTHYMeEAEAVCDRVAIMVSGQL 1511
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLL--GDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| 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 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMFEA--------RKMIGICPQLd 565
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAgiayvpedRKREGLVLDL- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 ihfdvlTVEENLSILASikgipanniiqevqkvlldldmqtikdnqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03215 94 ------SVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 646 DPCSRHIVWNLL-KYRKANR-VTVFSTHfMDEADILADRKAVISQG 689
Cdd:cd03215 136 DVGAKAEIYRLIrELADAGKaVLLISSE-LDELLGLCDRILVMYEG 180
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1319-1516 |
1.05e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 88.54 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysSETSEDD--DSLKcMG----YcpQ-INpLWPDTTL 1391
Cdd:COG1129 23 VSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDG--EPVRFRSprDAQA-AGiaiiH--QeLN-LVPNLSV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QE----HFEI--YGAVkgmsasDMKEVISRITHALD---LKEHLQKTVKKLPAGiKRKL---CFALSMlgNPQITLLDEP 1459
Cdd:COG1129 97 AEniflGREPrrGGLI------DWRAMRRRARELLArlgLDIDPDTPVGDLSVA-QQQLveiARALSR--DARVLILDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1460 STGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLrcIGT 1516
Cdd:COG1129 168 TASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1392-1619 |
1.10e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 86.71 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:NF000106 104 RENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1472 WRAIRTAFKNrKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGkGYFLEIKLKdwiENLEVDRLQREI- 1550
Cdd:NF000106 184 WDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPA---HAAELDRMVGAIa 258
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1551 QYIFPNASRQESFSSILAYKIPKEDVQSLSQSFFKLEEakHAFAIEEYSFSQATLEQVFVELTKEQEEE 1619
Cdd:NF000106 259 QAGLDGIAGATADHEDGVVNVPIVSDEQLSAVVGMLGE--RGFTISGHQHPSAQL*EVFLAITGQKTSE 325
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1290-1527 |
1.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.17 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDfllsrkvkKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSE 1368
Cdd:PRK13650 5 IEVKNLTFKYKEDQE--------KYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdGDLLTEENV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKcMGYCPQiNP--LWPDTTLQEHFEIYGAVKGMSASDMKEvisRITHALDL---KEHLQKTVKKLPAGIKRKLCF 1443
Cdd:PRK13650 77 WDIRHK-IGMVFQ-NPdnQFVGATVEDDVAFGLENKGIPHEEMKE---RVNEALELvgmQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1444 ALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQHLksk 1523
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPREL--- 227
|
....
gi 27262626 1524 FGKG 1527
Cdd:PRK13650 228 FSRG 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1288-1515 |
1.29e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 86.81 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSET 1366
Cdd:PRK11607 18 PLLEIRNLTKSFDGQH-----------AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLdGVDLSHV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDDDSLKCMGycpQINPLWPDTTLQEHFEiYGAVKGMSASDmkEVISRITHALDLKeHLQKTVKKLP----AGIKRKLC 1442
Cdd:PRK11607 87 PPYQRPINMMF---QSYALFPHMTVEQNIA-FGLKQDKLPKA--EIASRVNEMLGLV-HMQEFAKRKPhqlsGGQRQRVA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1443 FALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK11607 160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIG 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1319-1516 |
1.29e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 84.17 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetseDDDSL--------KCMGYCPQinplwpDTT 1390
Cdd:PRK10895 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLlplhararRGIGYLPQ------EAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 LQEHFEIYGAVkgMSASDMKEVIS---RITHALDLKE-----HLQKTV-KKLPAGIKRKLCFALSMLGNPQITLLDEPST 1461
Cdd:PRK10895 89 IFRRLSVYDNL--MAVLQIRDDLSaeqREDRANELMEefhieHLRDSMgQSLSGGERRRVEIARALAANPKFILLDEPFA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1462 GMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK10895 167 GVDPISVIDIKRIIE-HLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1290-1511 |
1.32e-17 |
|
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: 82.36 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysSETSED 1369
Cdd:cd03247 1 LSINNVSFSYPEQE---------QQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDG--VPVSDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSL-KCMGYCPQiNPLWPDTTLQEHFEiygavkgmsasdmkevisrithaldlkehlqktvKKLPAGIKRKLCFALSML 1448
Cdd:cd03247 70 EKALsSLISVLNQ-RPYLFDTTLRNNLG----------------------------------RRFSGGERQRLALARILL 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1449 GNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAVcDRVAIMVSGQL 1511
Cdd:cd03247 115 QDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD--KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
477-677 |
1.43e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.03 E-value: 1.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKkgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidEMFEARK 556
Cdd:NF033858 1 VARLEGVSHRYGK----TVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGG------DMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQldIHF----------DVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLG 626
Cdd:NF033858 71 RRAVCPR--IAYmpqglgknlyPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLC 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANR----VTVfSTHFMDEAD 677
Cdd:NF033858 149 CALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmsVLV-ATAYMEEAE 202
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1290-1482 |
1.74e-17 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 83.43 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLlsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSED 1369
Cdd:cd03254 3 IEFENVNFSYDEKKPVL----------KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLqEHFEIygavkGMSASDMKEVI--SRITHALDLKEHLQK---TV-----KKLPAGIKR 1439
Cdd:cd03254 73 KSLRSMIGVVLQDTFLFSGTIM-ENIRL-----GRPNATDEEVIeaAKEAGAHDFIMKLPNgydTVlgengGNLSQGERQ 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1440 KLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNR 1482
Cdd:cd03254 147 LLAIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR 189
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1310-1523 |
1.77e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 84.27 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1310 KVKKVATKY----------ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYC 1379
Cdd:PRK13632 9 KVENVSFSYpnsennalknVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1380 PQiNPlwpD-----TTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQIT 1454
Cdd:PRK13632 89 FQ-NP---DnqfigATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1455 LLDEpSTGM-DPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQH-LKSK 1523
Cdd:PRK13632 165 IFDE-STSMlDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNNK 233
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
477-691 |
1.81e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 83.93 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:COG1117 11 KIEVRNLNVYYGDK----QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIPGArvegeilldgEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 547 EIdemfEARKMIGICPQLDIHFdVLTVEENLSILASIKGIPANNIIQE-VQKVLLDLDM-QTIKDN---QAKKLSGGQKR 621
Cdd:COG1117 87 VV----ELRRRVGMVFQKPNPF-PKSIYDNVAYGLRLHGIKSKSELDEiVEESLRKAALwDEVKDRlkkSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 622 KLSL--GIAVlgNPKILLLDEPTAGMDPCSRHIVWNL---LKyrkaNRVT-VFSTHFMDEADILADRKAVISQGML 691
Cdd:COG1117 162 RLCIarALAV--EPEVLLMDEPTSALDPISTAKIEELileLK----KDYTiVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
495-647 |
2.01e-17 |
|
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: 82.41 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI-DEMFEARKMIGICPQLDihfDVLTV 573
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHENILYLGHLPGLK---PELSA 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 574 EENLSILASIKGIPANNIIQEVQKVLLDldmqTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:TIGR01189 91 LENLHFWAAIHGGAQRTIEDALAAVGLT----GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
462-689 |
2.59e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.57 E-value: 2.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 462 SEIIE-PVSSEFVGKE-------AIRISGIQKTYRKKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP 533
Cdd:PRK11160 315 NEITEqKPEVTFPTTStaaadqvSLTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 534 SDGFASIYGHRVSEIDEMfEARKMIGICPQlDIHFDVLTVEENLSILASikgiPANN--IIQEVQKVLLDLDMQTIKDNQ 611
Cdd:PRK11160 393 QQGEILLNGQPIADYSEA-ALRQAISVVSQ-RVHLFSATLRDNLLLAAP----NASDeaLIEVLQQVGLEKLLEDDKGLN 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 612 A------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CSRHIVWNLLKYRKaNRVTVFSTH---FMDEAD--IL 679
Cdd:PRK11160 467 AwlgeggRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAeTERQILELLAEHAQ-NKTVLMITHrltGLEQFDriCV 545
|
250
....*....|
gi 27262626 680 ADRKAVISQG 689
Cdd:PRK11160 546 MDNGQIIEQG 555
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1290-1568 |
3.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLLSrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYS-----S 1364
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFK------ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAipanlK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1365 ETSEDDDSLKCMGYCPQinplWPDTTL-QEHFE---IYGAVKgmSASDMKEVISRITHALDL----KEHLQKTVKKLPAG 1436
Cdd:PRK13645 81 KIKEVKRLRKEIGLVFQ----FPEYQLfQETIEkdiAFGPVN--LGENKQEAYKKVPELLKLvqlpEDYVKRSPFELSGG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1437 IKRKLCFA--LSMLGNPQItlLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK13645 155 QKRRVALAgiIAMDGNTLV--LDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1515 GTV------QHLKSKFG----KGYFLEIKLKdwieNLEVDRLQREIQYIfpnasrqESFSSILA 1568
Cdd:PRK13645 233 GSPfeifsnQELLTKIEidppKLYQLMYKLK----NKGIDLLNKNIRTI-------EEFAKELA 285
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1315-1523 |
3.45e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 83.74 E-value: 3.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG----DYSSETSEDDDSLKCMGYCPQINPLWPDTT 1390
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgkpiDYSRKGLMKLRESVGMVFQDPDNQLFSASV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 LQEhfEIYGAVKGMSASDmkEVISRITHALDLK--EHLQ-KTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKA 1467
Cdd:PRK13636 101 YQD--VSFGAVNLKLPED--EVRKRVDNALKRTgiEHLKdKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMG 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1468 KQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:PRK13636 177 VSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
478-685 |
3.94e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 84.33 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHRVSEID--EMF 552
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 553 EAR-KMIGICPQldihfD-------VLTVEENLS-ILASIKGIPANNIIQEVQKVL----LDLDMQTIKD--NQakkLSG 617
Cdd:COG0444 82 KIRgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLervgLPDPERRLDRypHE---LSG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 618 GQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHfmdeaDI-----LADRKAV 685
Cdd:COG0444 154 GMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLaiLFITH-----DLgvvaeIADRVAV 223
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
493-697 |
4.40e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 82.65 E-value: 4.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC-----PPSDGFASIYGHRVSEIDeMFEARKMIGICPQLDIH 567
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMD-VIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLSI------LASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK14247 94 IPNLSIFENVALglklnrLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 642 TAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
478-691 |
5.91e-17 |
|
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: 86.31 E-value: 5.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKM 557
Cdd:TIGR02203 331 VEFRNVTFRYP--GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADY-TLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQlDIH-FDVlTVEENLSIlasikGIPANNIIQEVQKVLLDLDMQTIKDN-----------QAKKLSGGQKRKLSL 625
Cdd:TIGR02203 408 VALVSQ-DVVlFND-TIANNIAY-----GRTEQADRAEIERALAAAYAQDFVDKlplgldtpigeNGVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADiLADRKAVISQGML 691
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1292-1516 |
8.27e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 84.70 E-value: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDD-------------KKDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF 1358
Cdd:PRK10070 7 IKNLYKIFGEhpqrafkyieqglSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1359 LGDYS----SETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLP 1434
Cdd:PRK10070 87 IDGVDiakiSDAELREVRRKKIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1435 AGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK10070 167 GGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQV 246
|
..
gi 27262626 1515 GT 1516
Cdd:PRK10070 247 GT 248
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
486-689 |
1.07e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEiDEMFEARKMIGICPQ-L 564
Cdd:PRK13652 10 CYSYSG-SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFVGLVFQnP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PRK13652 88 DDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAG 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 645 MDPCSRHivwNLLKYRKANRVT-----VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13652 168 LDPQGVK---ELIDFLNDLPETygmtvIFSTHQLDLVPEMADYIYVMDKG 214
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1319-1464 |
1.15e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 81.70 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgdyssetsEDDDSLKcMGYCPQinPLWPDTTLQEHFEIY 1398
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI----------KRNGKLR-IGYVPQ--KLYLDTTLPLTVNRF 89
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1399 GAVK-GMSASDMKEVISRITHAldlkeHL-QKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK09544 90 LRLRpGTKKEDILPALKRVQAG-----HLiDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
478-695 |
1.15e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 83.93 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM 557
Cdd:PRK11000 4 VTLRNVTKAY----GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP---AERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:PRK11000 77 VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 638 LDEPTAGMDPCSR---HIVWNLLkYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK11000 157 LDEPLSNLDAALRvqmRIEISRL-HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1290-1524 |
1.17e-16 |
|
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: 85.24 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVG--DIEPTSGQVFLG------- 1360
Cdd:TIGR03269 1 IEVKNLTKKFDGKE-----------VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHvalcekc 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1361 DYSSETSEDDDSLKCMG--YCPQINPLW-PDTT------------LQEHFEIYG-------AVKGMSASDM--KEVISRi 1416
Cdd:TIGR03269 70 GYVERPSKVGEPCPVCGgtLEPEEVDFWnLSDKlrrrirkriaimLQRTFALYGddtvldnVLEALEEIGYegKEAVGR- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1417 thALDLKEHLQ------KTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTT 1490
Cdd:TIGR03269 149 --AVDLIEMVQlshritHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTS 226
|
250 260 270
....*....|....*....|....*....|....
gi 27262626 1491 HYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:TIGR03269 227 HWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
478-696 |
1.26e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 82.36 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGE-NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfASIYGH-----RVSEIDEM 551
Cdd:PRK13645 7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETG-QTIVGDyaipaNLKKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 FEARKMIGIC---PQLDIHFDvlTVEENLSILASIKGIPANNIIQEVQKVLldlDMQTIKDNQAKK----LSGGQKRKLS 624
Cdd:PRK13645 86 KRLRKEIGLVfqfPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELL---KLVQLPEDYVKRspfeLSGGQKRRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 625 LGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL---LKYRKANRVtVFSTHFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13645 161 LAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRI-IMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1286-1520 |
1.54e-16 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 81.99 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1286 EKPSIMVSNLHKEYDDKKDFllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYssE 1365
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATY---------ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM--V 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1366 TSEDD--DSLKCMGYCPQiNplwPD-----TTLQEHFEIYGAVKGMSASDMkevISRITHALDL---KEHLQKTVKKLPA 1435
Cdd:PRK13635 71 LSEETvwDVRRQVGMVFQ-N---PDnqfvgATVQDDVAFGLENIGVPREEM---VERVDQALRQvgmEDFLNREPHRLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1436 GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILT-THYMEEAeAVCDRVAIMVSGQLRCI 1514
Cdd:PRK13635 144 GQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQ-LKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEE 221
|
....*.
gi 27262626 1515 GTVQHL 1520
Cdd:PRK13635 222 GTPEEI 227
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1289-1520 |
1.83e-16 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 82.81 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSET 1366
Cdd:COG3839 3 SLELENVSKSYGGV-----------EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrDVTDLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDDDslkcMGYCPQiNP-LWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAG--------- 1436
Cdd:COG3839 72 PKDRN----IAMVFQ-SYaLYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqrqrvalgr 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1437 -IKRklcfalsmlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:COG3839 147 aLVR----------EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
....*
gi 27262626 1516 TVQHL 1520
Cdd:COG3839 217 TPEEL 221
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
501-695 |
1.85e-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: 79.91 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKMIGICPQLDIHFDVLTVEENLSiL 580
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAP---YQRPVSMLFQENNLFAHLTVRQNIG-L 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 581 ASIKGIPANNIIQE-VQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY 659
Cdd:TIGR01277 94 GLHPGLKLNAEQQEkVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQ 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 27262626 660 --RKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:TIGR01277 174 lcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1319-1491 |
2.61e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKEVISRIthALDLKEHLQktVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTa 1478
Cdd:PRK13539 98 AAFLGGEELDIAAALEAV--GLAPLAHLP--FGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRA- 172
|
170
....*....|....*
gi 27262626 1479 fkNRKR--AAILTTH 1491
Cdd:PRK13539 173 --HLAQggIVIAATH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
479-689 |
2.78e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 83.81 E-value: 2.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 479 RISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIDEMFEARk 556
Cdd:PRK11288 6 SFDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqeMRFASTTAALAAG- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 mIGICPQlDIHFdV--LTVEENLSI--LASIKG-IPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLG 631
Cdd:PRK11288 81 -VAIIYQ-ELHL-VpeMTVAENLYLgqLPHKGGiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 632 NPKILLLDEPTAGMDpcSRHIVwNLLK----YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11288 158 NARVIAFDEPTSSLS--AREIE-QLFRvireLRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
496-684 |
2.90e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.60 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPP--SDGFASIYGHRV--SEIDEMfEARKMIGICPQLDIHF 568
Cdd:PRK14243 25 AVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLyaPDVDPV-EVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVlTVEENLSILASIKGIPANniIQEV------QKVLLDLDMQTIKDNqAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYKGD--MDELverslrQAALWDEVKDKLKQS-GLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
477-682 |
3.25e-16 |
|
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: 79.79 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR- 555
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDE--DARa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 ----KMIGICPQldiHF---DVLTVEENlsilasikgipanniiqevqkVLLDLDMQTIKDNQA---------------- 612
Cdd:COG4181 86 rlraRHVGFVFQ---SFqllPTLTALEN---------------------VMLPLELAGRRDARArarallervglghrld 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 613 ---KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVT-VFSTHfmDEAdiLADR 682
Cdd:COG4181 142 hypAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLfELNRERGTTlVLVTH--DPA--LAAR 212
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1301-1520 |
3.54e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 82.07 E-value: 3.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1301 DKKDFLLSRKVKK-----VATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSEDDDSLk 1374
Cdd:PRK11432 2 TQKNFVVLKNITKrfgsnTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdGEDVTHRSIQQRDI- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1375 CMGYcpQINPLWPDTTLQEHFEiYG-AVKGMSASDMKEvisRITHAL---DLKEHLQKTVKKLPAGIKRKLCFALSMLGN 1450
Cdd:PRK11432 81 CMVF--QSYALFPHMSLGENVG-YGlKMLGVPKEERKQ---RVKEALelvDLAGFEDRYVDQISGGQQQRVALARALILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1451 PQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK11432 155 PKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1315-1518 |
3.66e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.68 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYCPQINPLWPDTTLQE 1393
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFEI----YGAVKGMSASD---MKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPK 1466
Cdd:PRK09700 100 NLYIgrhlTKKVCGVNIIDwreMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1467 AKQHMWrAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK09700 180 EVDYLF-LIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVS 230
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
477-698 |
4.42e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 81.81 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARK 556
Cdd:PRK11650 3 GLKLQAVRKSY---DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP---ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ---LDIHfdvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK11650 77 DIAMVFQnyaLYPH---MSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 634 KILLLDEPTAGMDPcsrhivwnllKYRKANRV------------TVFSTHFMDEADILADRKAVISQGMLKCVGSSM 698
Cdd:PRK11650 154 AVFLFDEPLSNLDA----------KLRVQMRLeiqrlhrrlkttSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPV 220
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
496-682 |
4.78e-16 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 4.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV-------SEIDEMFearkmigicPqldihf 568
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARvayvpqrSEVPDSL---------P------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 dvLTVEENLSI----LASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:NF040873 72 --LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 27262626 645 MDPCSRHIVWNLLKYRKANRVTVF-STHFMDEAdILADR 682
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVvVTHDLELV-RRADP 187
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
485-692 |
7.73e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 78.70 E-value: 7.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 485 KTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR---KMIGIC 561
Cdd:PRK11629 13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnQKLGFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 562 PQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK11629 93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 642 TAGMDPCSRHIVWNLLKYRKANRVTVF--STHFMDEADILaDRKAVISQGMLK 692
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFlvVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1290-1525 |
7.93e-16 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 78.81 E-value: 7.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLlsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSED 1369
Cdd:cd03253 1 IEFENVTFAYDPGRPVL----------KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILI-DGQDIREVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSL-KCMGYCPQINPLWPDTTLqehFEI-YGAVkgmSASDmKEVI--SRITHALDLKEHLQK---TV-----KKLPAGI 1437
Cdd:cd03253 70 LDSLrRAIGVVPQDTVLFNDTIG---YNIrYGRP---DATD-EEVIeaAKAAQIHDKIMRFPDgydTIvgergLKLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1438 KRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAeAVCDRVAIMVSGQLRCIGTV 1517
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG--RTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTH 219
|
....*...
gi 27262626 1518 QHLKSKFG 1525
Cdd:cd03253 220 EELLAKGG 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1285-1491 |
8.27e-16 |
|
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: 82.41 E-value: 8.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1285 EEKPSIMVSNLHKEYDDKKDFLlsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSS 1364
Cdd:TIGR02868 330 LGKPTLELRDLSAGYPGAPPVL----------DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1365 ETSEDDDSLKCMGYCPQiNPLWPDTTLQEHFEIygAVKGMSASDMKEVISRI---THALDLKEHLQKTV----KKLPAGI 1437
Cdd:TIGR02868 400 SSLDQDEVRRRVSVCAQ-DAHLFDTTVRENLRL--ARPDATDEELWAALERVglaDWLRALPDGLDTVLgeggARLSGGE 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1438 KRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfkNRKRAAILTTH 1491
Cdd:TIGR02868 477 RQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAA--LSGRTVVLITH 528
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1319-1511 |
9.41e-16 |
|
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: 77.09 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYCPqinplwpdttlQEHFEi 1397
Cdd:cd03215 19 VSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVP-----------EDRKR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 YGAVKGMSasdmkeVISRIThaldLKEHL-----QktvkklpagikrKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:cd03215 87 EGLVLDLS------VAENIA----LSSLLsggnqQ------------KVVLARWLARDPRVLILDEPTRGVDVGAKAEIY 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 27262626 1473 RAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03215 145 RLIR-ELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1319-1516 |
9.54e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 79.78 E-value: 9.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDY----SSETSEDDDSLKCMGYCPQI--NPLWPDTTLQ 1392
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvssTSKQKEIKPVRKKVGVVFQFpeSQLFEETVLK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EhfEIYGAVK-GMSASDMKEVISRITHALDL-KEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:PRK13643 105 D--VAFGPQNfGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 1471 MWRAIRTAFKNrKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK13643 183 MMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
478-691 |
9.73e-16 |
|
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: 79.08 E-value: 9.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGEN-----VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmf 552
Cdd:TIGR02769 3 LEVRDVTHTYRTGGLFgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 553 EARKMIGICPQLDIHFDVLTVEENLSILASIkGIPANNII-----QEVQKVLLDLDMQTIKDNQAKK----LSGGQKRKL 623
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDSPSAVNPRMTVRQII-GEPLRHLTsldesEQKARIAELLDMVGLRSEDADKlprqLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 624 SLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTHFMDEADILADRKAVISQGML 691
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTayLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
476-682 |
1.20e-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: 77.86 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 476 EAIRISGIQKTYR---KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSI-YGHRVSEID-- 549
Cdd:COG4778 3 TLLEVENLSKTFTlhlQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSG--SIlVRHDGGWVDla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 550 -----EMFEARK-MIGICPQ----------LDIhfdvltVEENLsiLAsiKGIPANNIIQEVQKVLLDLdmqtikdNQAK 613
Cdd:COG4778 81 qasprEILALRRrTIGYVSQflrviprvsaLDV------VAEPL--LE--RGVDREEARARARELLARL-------NLPE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 614 KL--------SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSThFMDEA--DILADR 682
Cdd:COG4778 144 RLwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADR 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
507-646 |
1.34e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.90 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 507 GQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEAR-----KMIGICPQLDIHFDVLTVEENLSILA 581
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDE--EARaklraKHVGFVFQSFMLIPTLNALENVELPA 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 582 SIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10584 114 LLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1323-1511 |
1.40e-15 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 77.53 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYcpQINPLWPDTTLQEHFEIyGAVK 1402
Cdd:cd03298 21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLF--QENNLFAHLTVEQNVGL-GLSP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1403 G--MSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFK 1480
Cdd:cd03298 98 GlkLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 1481 NRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1317-1516 |
1.46e-15 |
|
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: 77.53 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTT------ 1390
Cdd:cd03244 21 KNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSGTIrsnldp 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 LQEH--FEIYGAVKGMSasdMKEVISRITHALDLKEHLQKtvKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAK 1468
Cdd:cd03244 101 FGEYsdEELWQALERVG---LKEFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1469 QHMWRAIRTAFKNRkraAILT-THYMeeaEAV--CDRVAIMVSGQLRCIGT 1516
Cdd:cd03244 176 ALIQKTIREAFKDC---TVLTiAHRL---DTIidSDRILVLDKGRVVEFDS 220
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1319-1511 |
1.66e-15 |
|
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: 77.70 E-value: 1.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEP---TSGQVFlgdYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHF 1395
Cdd:cd03234 26 VSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQIL---FNGQPRKPDQFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIY----------GAVKGMSASD--MKEV-ISRITHALdlkehlqktVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:cd03234 103 TYTailrlprkssDAIRKKRVEDvlLRDLaLTRIGGNL---------VKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1463 MDPkakqhmwraiRTAFK---------NRKRAAILTTHY-MEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03234 174 LDS----------FTALNlvstlsqlaRRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1312-1570 |
1.83e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSL----KCMGYCPQInplwP 1387
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrKRIGMVFQF----P 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1388 DTTLQE---HFEIYGAVK--GMSASDMKEVISRITHALDL-KEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPST 1461
Cdd:PRK13646 95 ESQLFEdtvEREIIFGPKnfKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1462 GMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLkskFGKGYfleiKLKDW-IEN 1540
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL---FKDKK----KLADWhIGL 247
|
250 260 270
....*....|....*....|....*....|....*
gi 27262626 1541 LEVDRLQREI----QYIFPN-ASRQESFSSIlaYK 1570
Cdd:PRK13646 248 PEIVQLQYDFeqkyQTKLKDiALTEEEFVSL--YK 280
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1292-1459 |
1.83e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 81.26 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSsetsedd 1370
Cdd:COG0488 1 LENLSKSFGGRP--LLDD---------VSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIpKGLR------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1371 dslkcMGYCPQINPLWPDTTLQE-----HFEIYGAVK---------GMSASDMKEV------------------ISRITH 1418
Cdd:COG0488 63 -----IGYLPQEPPLDDDLTVLDtvldgDAELRALEAeleeleaklAEPDEDLERLaelqeefealggweaearAEEILS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 1419 ALDLKEH-LQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEP 1459
Cdd:COG0488 138 GLGFPEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
490-658 |
2.00e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 82.46 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 490 KGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP---SDGFASIYGHrvsEIDEMFEARkmIGICPQLDI 566
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGR---PLDSSFQRS--IGYVQQQDL 846
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 HFDVLTVEENLSILASIKgIPANNIIQE----VQKVLLDLDMQTIKDN----QAKKLSGGQKRKLSLGIAVLGNPKILL- 637
Cdd:TIGR00956 847 HLPTSTVRESLRFSAYLR-QPKSVSKSEkmeyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKPKLLLf 925
|
170 180
....*....|....*....|.
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLK 658
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMR 946
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
491-695 |
2.18e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 77.96 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 491 GENvEALRNLSFDIYEGQITALLGHSGTGKSTLM---NILCGLCPPS--DGFASIYGHRVSEID-EMFEARKMIGICPQL 564
Cdd:PRK14267 15 GSN-HVIKGVDLKIPQNGVFALMGPSGCGKSTLLrtfNRLLELNEEArvEGEVRLFGRNIYSPDvDPIEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHFDVLTVEENLSILASIKGI--PANNIIQEVQKVLLDLDM-QTIKD---NQAKKLSGGQKRKLSLGIAVLGNPKILLL 638
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwDEVKDrlnDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 639 DEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVG 695
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
487-689 |
2.32e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.13 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 487 YRKKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKMIGICPQLDI 566
Cdd:PRK13638 9 FRYQDEPV--LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-----YSKRGLLALRQQVAT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 HFD-----VLTVEENLSILASIK--GIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:PRK13638 82 VFQdpeqqIFYTDIDSDIAFSLRnlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 640 EPTAGMDPCSRHIVWNLLK--YRKANRVtVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13638 162 EPTAGLDPAGRTQMIAIIRriVAQGNHV-IISSHDIDLIYEISDAVYVLRQG 212
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
483-689 |
3.04e-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: 81.32 E-value: 3.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 483 IQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICP 562
Cdd:TIGR01193 476 INDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINYLP 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QLDIHFDVlTVEENLsILASIKGIPANNIIQEVQKVLLDLDM-------QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:TIGR01193 555 QEPYIFSG-SILENL-LLGAKENVSQDEIWAACEIAEIKDDIenmplgyQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 636 LLLDEPTAGMDPCSRH-IVWNLLKYRK------ANRVTVFSthfMDEADILADRKAVISQG 689
Cdd:TIGR01193 633 LILDESTSNLDTITEKkIVNNLLNLQDktiifvAHRLSVAK---QSDKIIVLDHGKIIEQG 690
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
475-671 |
3.16e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.62 E-value: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIQKTYRKkGENveALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfea 554
Cdd:PRK15056 4 QAGIVVNDVTVTWRN-GHT--ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQ---LDIHFDVLTveENLSILA-----SIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLG 626
Cdd:PRK15056 77 KNLVAYVPQseeVDWSFPVLV--EDVVMMGryghmGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 627 IAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFSTH 671
Cdd:PRK15056 155 RAIAQQGQVILLDEPFTGVDVKTEARIISLLReLRDEGKTMLVSTH 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1310-1520 |
3.44e-15 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 76.72 E-value: 3.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1310 KVKKVATKY------ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSsetsedddslkcmgyCPQIN 1383
Cdd:COG3840 3 RLDDLTYRYgdfplrFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD---------------LTALP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1384 P-------LWPDTTLQEHFEIYGAVK-GMSaSDMK---EVISRITHALD---LKEHLQktvkKLPA----GIKRKLCFAL 1445
Cdd:COG3840 68 PaerpvsmLFQENNLFPHLTVAQNIGlGLR-PGLKltaEQRAQVEQALErvgLAGLLD----RLPGqlsgGQRQRVALAR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1446 SMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
474-697 |
3.60e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 77.39 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 474 GKEAIRISGIQKTYRKKGENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP------PSDGFASIYGHRVSE 547
Cdd:PRK14246 4 GKSAEDVFNISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 548 IDEMfEARKMIGICPQLDIHFDVLTVEENLSILASIKGIPANNIIQEV-----QKVLLDLDMQTIKDNQAKKLSGGQKRK 622
Cdd:PRK14246 83 IDAI-KLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIveeclRKVGLWKEVYDRLNSPASQLSGGQQQR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK14246 162 LTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
496-689 |
3.67e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 77.05 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS----EIDEMFEARkmiGICPQLDihfdvl 571
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgaERGVVFQNE---GLLPWRN------ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 tVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK11248 87 -VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 652 IVWNLL--KYRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11248 166 QMQTLLlkLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1516 |
4.00e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 77.43 E-value: 4.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGdySSETSED 1369
Cdd:PRK13639 2 LETRDLKYSYPDGT----------EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIK--GEPIKYD 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSL----KCMGYCPQiNP---LWPDTTLQEhfEIYGAVK-GMSasdMKEVISRITHAL---DLKEHLQKTVKKLPAGIK 1438
Cdd:PRK13639 70 KKSLlevrKTVGIVFQ-NPddqLFAPTVEED--VAFGPLNlGLS---KEEVEKRVKEALkavGMEGFENKPPHHLSGGQK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1439 RKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAfkNRKRAAI-LTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK13639 144 KRVAIAgiLAM--KPEIIVLDEPTSGLDPMGASQIMKLLYDL--NKEGITIiISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
.
gi 27262626 1516 T 1516
Cdd:PRK13639 220 T 220
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1290-1516 |
4.10e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.44 E-value: 4.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDfllsrKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSED 1369
Cdd:PRK13633 5 IKCKNVSYKYESNEE-----STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 ddslkcmgycpqinpLW------------PD----TTLQEHFEIYGAVK-GMSASDMKEVISRITHALDLKEHLQKTVKK 1432
Cdd:PRK13633 80 ---------------LWdirnkagmvfqnPDnqivATIVEEDVAFGPENlGIPPEEIRERVDESLKKVGMYEYRRHAPHL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1433 LPAGIKRKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAeAVCDRVAIMVSGQ 1510
Cdd:PRK13633 145 LSGGQKQRVAIAgiLAM--RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGK 221
|
....*.
gi 27262626 1511 LRCIGT 1516
Cdd:PRK13633 222 VVMEGT 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1290-1503 |
4.25e-15 |
|
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: 74.02 E-value: 4.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSetsed 1369
Cdd:cd03221 1 IELENLSKTYGGKL--LLKD---------ISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 ddslkcMGYCPQinplwpdttlqehfeiygavkgmsasdmkevisrithaldlkehlqktvkkLPAGIKRKLCFALSMLG 1449
Cdd:cd03221 65 ------IGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLE 87
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQhmwrAIRTAFKNRKRAAILTTHYMEEAEAVCDRV 1503
Cdd:cd03221 88 NPNLLLLDEPTNHLDLESIE----ALEEALKEYPGTVILVSHDRYFLDQVATKI 137
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1313-1551 |
6.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 77.37 E-value: 6.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1313 KVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCM----GYCPQI--NPLW 1386
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKLKPLrkkvGIVFQFpeHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1387 PDTTLQEhfeI-YGAVK-GMSASDMKEVISRITHALDLKEH-LQKTVKKLPAGIKRKLCFA--LSMlgNPQITLLDEPST 1461
Cdd:PRK13634 100 EETVEKD---IcFGPMNfGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAgvLAM--EPEVLVLDEPTA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1462 GMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKfgkgyfleiklKDWIENL 1541
Cdd:PRK13634 175 GLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD-----------PDELEAI 243
|
250
....*....|....*
gi 27262626 1542 EVD-----RLQREIQ 1551
Cdd:PRK13634 244 GLDlpetvKFKRALE 258
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1289-1524 |
9.35e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 76.39 E-value: 9.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEY-------DDKKDFLLSRKVKKV--ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVfl 1359
Cdd:PRK13546 4 SVNIKNVTKEYriyrtnkERMKDALIPKHKNKTffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1360 gdyssetsEDDDSLKCMGYCPQINplwPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKR 1439
Cdd:PRK13546 82 --------DRNGEVSVIAISAGLS---GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1440 KLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:PRK13546 151 KLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIY-EFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDD 229
|
....*
gi 27262626 1520 LKSKF 1524
Cdd:PRK13546 230 VLPKY 234
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1276-1516 |
9.51e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 78.07 E-value: 9.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1276 KELMGCQCCEEKPSIMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSG 1355
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKE-----------VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1356 QVFLGDyssetsedddslKCMGYCP----QINPLWPDTTLQEHFEIYGAVK---GMSASDMKEVISRITHAL---DLKEH 1425
Cdd:PRK09452 70 RIMLDG------------QDITHVPaenrHVNTVFQSYALFPHMTVFENVAfglRMQKTPAAEITPRVMEALrmvQLEEF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1426 LQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMwraiRTAFKNRKRAA----ILTTHYMEEAEAVCD 1501
Cdd:PRK09452 138 AQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQM----QNELKALQRKLgitfVFVTHDQEEALTMSD 213
|
250
....*....|....*
gi 27262626 1502 RVAIMVSGQLRCIGT 1516
Cdd:PRK09452 214 RIVVMRDGRIEQDGT 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1323-1507 |
9.80e-15 |
|
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: 79.44 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgdyssetsedDDSLKcMGYCPQ-INPLWpDTTLQEHfeIYGAV 1401
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV------------DEDLK-ISYKPQyISPDY-DGTVEEF--LRSAN 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1402 KGMSASDMKEviSRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKN 1481
Cdd:COG1245 427 TDDFGSSYYK--TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAEN 504
|
170 180
....*....|....*....|....*...
gi 27262626 1482 RKRAAILTTH--YMeeAEAVCDRvaIMV 1507
Cdd:COG1245 505 RGKTAMVVDHdiYL--IDYISDR--LMV 528
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1319-1516 |
1.03e-14 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 79.44 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG-----DYssetseDDDSL-KCMGYCPQinplwpDTTLq 1392
Cdd:COG1132 359 ISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDgvdirDL------TLESLrRQIGVVPQ------DTFL- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 ehFE------I-YGAvkgMSASDmKEVIS--RITHALDLkehlqktVKKLPAGI---------------KRKLCFALSML 1448
Cdd:COG1132 426 --FSgtirenIrYGR---PDATD-EEVEEaaKAAQAHEF-------IEALPDGYdtvvgergvnlsggqRQRIAIARALL 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1449 GNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAvCDRVAIMVSGQLRCIGT 1516
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKG--RTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1319-1511 |
1.10e-14 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 75.09 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLK---CMGYCPQINPLWPDTTLQEHF 1395
Cdd:COG2884 21 VSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYlrrRIGVVFQDFRLLPDRTVYENV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYGAVKGMSASDMKEvisRITHALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:COG2884 101 ALPLRVTGKSRKEIRR---RVREVLDlvgLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDPETSWEIM 177
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 1473 RAIRTAfkNRKRAAIL-TTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG2884 178 ELLEEI--NRRGTTVLiATHDLELVDRMPKRVLELEDGRL 215
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
486-695 |
1.10e-14 |
|
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: 79.02 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMfEARKMIGICPQlD 565
Cdd:COG4618 337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDRE-ELGRHIGYLPQ-D 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IH-FDVlTVEENLSILASIkgiPANNIIQEVQKVLLDlDM--------QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:COG4618 415 VElFDG-TIAENIARFGDA---DPEKVVAAAKLAGVH-EMilrlpdgyDTRIGEGGARLSGGQRQRIGLARALYGDPRLV 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLLKYRKANRVTVF-STHfmdEADIL--ADRKAVISQGMLKCVG 695
Cdd:COG4618 490 VLDEPNSNLDDEGEAALAAAIRALKARGATVVvITH---RPSLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
498-643 |
1.21e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 74.46 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 498 RNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARKM--IGICPQLDihfDVLTVEE 575
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEY-HQDLlyLGHQPGIK---TELTALE 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 576 NLSILASIKGIPANNIIQEV-QKVLL----DLdmqtikdnQAKKLSGGQKRKLSLGIAVLGNPKILLLDEP-TA 643
Cdd:PRK13538 94 NLRFYQRLHGPGDDEALWEAlAQVGLagfeDV--------PVRQLSAGQQRRVALARLWLTRAPLWILDEPfTA 159
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1319-1550 |
1.42e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.05 E-value: 1.42e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSEDDdslKCMGYCpqinplwpdttlqehFEI 1397
Cdd:PRK10851 21 ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIrFHGTDVSRLHARD---RKVGFV---------------FQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 YGAVKGMSASD----------------MKEVISRITHALDLK--EHL-QKTVKKLPAGIKRKLCFALSMLGNPQITLLDE 1458
Cdd:PRK10851 83 YALFRHMTVFDniafgltvlprrerpnAAAIKAKVTQLLEMVqlAHLaDRYPAQLSGGQKQRVALARALAVEPQILLLDE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1459 PSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYFLEIKlkdwi 1538
Cdd:PRK10851 163 PFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM----- 237
|
250
....*....|..
gi 27262626 1539 enLEVDRLQREI 1550
Cdd:PRK10851 238 --GEVNRLQGTI 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
497-696 |
1.45e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 1.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMfeARkMIGICPQldiHFDV---L 571
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSpaEL--AR-RRAVLPQ---HSSLsfpF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 TVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLgiA-VL-------GNPKILLLDEPTA 643
Cdd:PRK13548 92 TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQL--ArVLaqlwepdGPPRWLLLDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 644 GMDPCSRHIVWNLLKYR-KANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK13548 170 ALDLAHQHHVLRLARQLaHERGLAVIVVlHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1323-1510 |
1.46e-14 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 75.14 E-value: 1.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgdyssETSEDDDSLKcmgycPQ-INPLWPDTTLQEHFEIygaV 1401
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI-------EIELDTVSYK-----PQyIKADYEGTVRDLLSSI---T 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1402 KGMSASDmkEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKN 1481
Cdd:cd03237 87 KDFYTHP--YFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAEN 164
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 1482 RKRAAILTTH--YMeeAEAVCDRVaIMVSGQ 1510
Cdd:cd03237 165 NEKTAFVVEHdiIM--IDYLADRL-IVFEGE 192
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1319-1518 |
1.54e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.58 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:PRK13548 21 VSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSFPFTVEEVVAMG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFA--LSML----GNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:PRK13548 101 RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArvLAQLwepdGPPRWLLLDEPTSALDLAHQHHVL 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1473 RAIRTAFKNRKRAAI-------LTTHYmeeaeavCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK13548 181 RLARQLAHERGLAVIvvlhdlnLAARY-------ADRIVLLHQGRLVADGTPA 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
497-696 |
1.61e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 75.44 E-value: 1.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeideMFEARKM---IGICPQldihfdVLTV 573
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPIS----MLSSRQLarrLALLPQ------HHLT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSI--LASIKGIPANNII--------QEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:PRK11231 88 PEGITVreLVAYGRSPWLSLWgrlsaednARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 644 GMDPCSRHIVWNLLKYRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGS 696
Cdd:PRK11231 168 YLDINHQVELMRLMRELNTQGKTVVTVlHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1292-1528 |
1.69e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 73.72 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVG--DIEPTSGQVFLGDYS-SETSE 1368
Cdd:cd03217 3 IKDLHVSVGGKE--IL---------KGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDiTDLPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKCMGYCPQINPlwpdttlqehfEIYGaVKgmsasdmkevisrithaldLKEHLQKTVKKLPAGIKRKLCFALSML 1448
Cdd:cd03217 72 EERARLGIFLAFQYPP-----------EIPG-VK-------------------NADFLRYVNEGFSGGEKKRNEILQLLL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1449 GNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAV-CDRVAIMVSGQLRCIGTVQHLKSKFGKG 1527
Cdd:cd03217 121 LEPDLAILDEPDSGLDIDALRLVAEVINK-LREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKG 199
|
.
gi 27262626 1528 Y 1528
Cdd:cd03217 200 Y 200
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1289-1516 |
1.99e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 76.43 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDKKDFLLsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSE 1368
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENEL------VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKCMGYCPQIN------------------PLWPDTTlqEHFEIYGAVK-GMSASDMKEVISRITHALDLKE-HLQK 1428
Cdd:PRK13631 95 NNHELITNPYSKKIKnfkelrrrvsmvfqfpeyQLFKDTI--EKDIMFGPVAlGVKKSEAKKLAKFYLNKMGLDDsYLER 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1429 TVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfKNRKRAAILTTHYMEEAEAVCDRVAIMVS 1508
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDA-KANNKTVFVITHTMEHVLEVADEVIVMDK 251
|
....*...
gi 27262626 1509 GQLRCIGT 1516
Cdd:PRK13631 252 GKILKTGT 259
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
478-697 |
2.19e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 75.05 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---PPSDGFASIYGHRVSE----IDE 550
Cdd:PRK09984 5 IRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQRegrlARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 551 MFEARKMIG-ICPQLDIhFDVLTVEENLsILASIKGIP---------ANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQK 620
Cdd:PRK09984 81 IRKSRANTGyIFQQFNL-VNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 621 RKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK-YRKANRVTVFST-HFMDEADILADRKAVISQGMLKCVGSS 697
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRdINQNDGITVVVTlHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1290-1511 |
2.57e-14 |
|
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: 73.72 E-value: 2.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSeTSED 1369
Cdd:cd03262 1 IEIKNLHKSFGDFH-----------VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKL-TDDK 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKC---MGYCPQINPLWPDTTLQEHfeIYGA---VKGMSAsdmKEVISRITHALD---LKEHLQKTVKKLPAGIKRK 1440
Cdd:cd03262 69 KNINELrqkVGMVFQQFNLFPHLTVLEN--ITLApikVKGMSK---AEAEERALELLEkvgLADKADAYPAQLSGGQQQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1441 LCFALSMLGNPQITLLDEPSTGMDPK------------AKQHMwrairtafknrkrAAILTTHYMEEAEAVCDRVAIMVS 1508
Cdd:cd03262 144 VAIARALAMNPKVMLFDEPTSALDPElvgevldvmkdlAEEGM-------------TMVVVTHEMGFAREVADRVIFMDD 210
|
...
gi 27262626 1509 GQL 1511
Cdd:cd03262 211 GRI 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1312-1525 |
3.45e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 3.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQ--VFLGDYSSETSEDDdslkcmgYCPQI------- 1382
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRveVLGGDMADARHRRA-------VCPRIaympqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1383 --NpLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRK--LCFALsmLGNPQITLLDE 1458
Cdd:NF033858 86 gkN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKlgLCCAL--IHDPDLLILDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1459 PSTGMDPKAKQHMWRAIrtafkNRKRAA------ILTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:NF033858 163 PTTGVDPLSRRQFWELI-----DRIRAErpgmsvLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1319-1511 |
3.61e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 74.87 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCM----GYCPQI--NPLWPDTTLQ 1392
Cdd:PRK13641 26 ISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvSLVFQFpeAQLFENTVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EhfEIYGAVK-GMSASDMKEVISRITHALDLKEHL-QKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:PRK13641 106 D--VEFGPKNfGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 1471 MWRairtAFKNRKRAA---ILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK13641 184 MMQ----LFKDYQKAGhtvILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
500-646 |
3.67e-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: 72.91 E-value: 3.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEI-DEMFEARKMIGICPQLDihfDVLTVEENLS 578
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQrDSIARGLLYLGHAPGIK---TTLSVLENLR 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 579 ILASIKGIPAnniiqeVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03231 96 FWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1323-1506 |
5.40e-14 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 72.27 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD-----YSSETSEDDDSLKC-------MGycpqinpLWPDTt 1390
Cdd:NF040873 15 IPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvaYVPQRSEVPDSLPLtvrdlvaMG-------RWARR- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 lqehfeiyGAVKGMSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:NF040873 87 --------GLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRER 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 1471 MWRAIRtAFKNRKRAAILTTHYMEEAEAVcDRVAIM 1506
Cdd:NF040873 158 IIALLA-EEHARGATVVVVTHDLELVRRA-DPCVLL 191
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
497-646 |
5.56e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.61 E-value: 5.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARKMIGICPQlDIHFDV---LTV 573
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKR--NGKLRIGYVPQ-KLYLDTtlpLTV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 574 EENLSILASIKG---IPANNIIQEVQkvLLDLDMQtikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK09544 87 NRFLRLRPGTKKediLPALKRVQAGH--LIDAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
492-689 |
5.81e-14 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 73.25 E-value: 5.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 492 ENVEALRN---LSFD--IYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvSEIDEMFEARKMIGICPQLDI 566
Cdd:COG3840 5 DDLTYRYGdfpLRFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG---QDLTALPPAERPVSMLFQENN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 HFDVLTVEENLSIlasikGIPAN---------NIIQEVQKVLLDlDMQTIKDNQakkLSGGQKRKLSLGIAVLGNPKILL 637
Cdd:COG3840 82 LFPHLTVAQNIGL-----GLRPGlkltaeqraQVEQALERVGLA-GLLDRLPGQ---LSGGQRQRVALARCLVRKRPILL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:COG3840 153 LDEPFSALDPALRQEMLDLVDelCRERGLTVLMVTHDPEDAARIADRVLLVADG 206
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
489-697 |
6.04e-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: 76.76 E-value: 6.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 489 KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGL--CPPSDGfASIY------------------------G 542
Cdd:TIGR03269 8 KKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSG-RIIYhvalcekcgyverpskvgepcpvcG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 543 HRVSEIDEMF---------EARKMIGICPQLDIH-FDVLTVEENlsILASIK--GIPANNIIQEVQKVLLDLDMQTIKDN 610
Cdd:TIGR03269 87 GTLEPEEVDFwnlsdklrrRIRKRIAIMLQRTFAlYGDDTVLDN--VLEALEeiGYEGKEAVGRAVDLIEMVQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 611 QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVT-VFSTHFMDEADILADRKAVISQ 688
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISmVLTSHWPEVIEDLSDKAIWLEN 244
|
....*....
gi 27262626 689 GMLKCVGSS 697
Cdd:TIGR03269 245 GEIKEEGTP 253
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1319-1491 |
6.41e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.57 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEdddSLKCMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYLGHLPGLKADLSTLENLHFL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKeviSRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIrTA 1478
Cdd:PRK13543 107 CGLHGRRAKQMP---GSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMI-SA 182
|
170
....*....|...
gi 27262626 1479 FKNRKRAAILTTH 1491
Cdd:PRK13543 183 HLRGGGAALVTTH 195
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
474-705 |
7.70e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.77 E-value: 7.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 474 GKEAIRISGIQKTYrkkGEnVEALRNLSFDIYEGQITALLGHSGTG--KSTLMNILCGlcpPSDG-----FASIYGHRVS 546
Cdd:NF000106 10 ARNAVEVRGLVKHF---GE-VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGrrpwrF*TWCANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 547 eidemfeARKMIGIC-PQLDIHFDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSL 625
Cdd:NF000106 83 -------LRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 626 GIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGMLKCVGSSMFLKSKW 704
Cdd:NF000106 156 AASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVlLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKV 235
|
.
gi 27262626 705 G 705
Cdd:NF000106 236 G 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
477-689 |
8.21e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 73.25 E-value: 8.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIyghRVS--EIDEMFEA 554
Cdd:PRK11264 3 AIEVKNLVKKF--HGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAG--TI---RVGdiTIDTARSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGICPQLDIH----------FDVLTVEENlsILAS---IKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKR 621
Cdd:PRK11264 74 SQQKGLIRQLRQHvgfvfqnfnlFPHRTVLEN--IIEGpviVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 622 KLSLGIAVLGNPKILLLDEPTAGMDPcsrHIVWNLLKYRKA----NRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11264 152 RVAIARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1303-1520 |
8.50e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1303 KDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQi 1382
Cdd:PRK13652 7 RDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1383 NP---LWPDTTLQEhfEIYGAVK-GMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDE 1458
Cdd:PRK13652 86 NPddqIFSPTVEQD--IAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDE 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1459 PSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK13652 164 PTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
480-642 |
8.74e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.26 E-value: 8.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 480 ISGIQKTYRKKgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemFEARKMIG 559
Cdd:COG0488 1 LENLSKSFGGR----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVS-----IPKGLRIG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 560 ICPQLDIHFDVLTVEENlsILASIKGIPAnnIIQEVQKVLLDLDMQTIK-------------------DNQAKK------ 614
Cdd:COG0488 65 YLPQEPPLDDDLTVLDT--VLDGDAELRA--LEAELEELEAKLAEPDEDlerlaelqeefealggweaEARAEEilsglg 140
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 615 ------------LSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG0488 141 fpeedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1298-1526 |
1.86e-13 |
|
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: 71.88 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1298 EYDDKKDFLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMG 1377
Cdd:cd03251 9 RYPGDGPPVL---------RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1378 YCPQiNPLWPDTTLQEHFEiYGAvkgmSASDMKEVIS--RITHALDLKEHLQK---TV-----KKLPAGIKRKLCFALSM 1447
Cdd:cd03251 80 LVSQ-DVFLFNDTVAENIA-YGR----PGATREEVEEaaRAANAHEFIMELPEgydTVigergVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1448 LGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAI---LTThyMEEAeavcDRVAIMVSGQLRCIGTVQHLKSKF 1524
Cdd:cd03251 154 LKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIahrLST--IENA----DRIVVLEDGKIVERGTHEELLAQG 227
|
..
gi 27262626 1525 GK 1526
Cdd:cd03251 228 GV 229
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
480-689 |
2.27e-13 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 72.02 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 480 ISGIQKTYrkkGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE----MF-EA 554
Cdd:PRK11247 15 LNAVSKRY---GER-TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREdtrlMFqDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RkmigICPQldihfdvLTVEENLSIlaSIKGIPANNIIQEVQKVLLdldmqtikDNQAKK----LSGGQKRKLSLGIAVL 630
Cdd:PRK11247 91 R----LLPW-------KKVIDNVGL--GLKGQWRDAALQALAAVGL--------ADRANEwpaaLSGGQKQRVALARALI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 631 GNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11247 150 HRPGLLLLDEPLGALDALTRIEMQDLIEslWQQHGFTVLLVTHDVSEAVAMADRVLLIEEG 210
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1319-1511 |
2.65e-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: 70.90 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysSETSEDDDSL-----KCMGYCPQINPLWPDTTLQE 1393
Cdd:cd03292 20 INISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNG--QDVSDLRGRAipylrRKIGVVFQDFRLLPDRNVYE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPkakQHMWR 1473
Cdd:cd03292 98 NVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDP---DTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 1474 AIRTAFKNRKRAA--ILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:cd03292 175 IMNLLKKINKAGTtvVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
489-677 |
2.70e-13 |
|
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: 70.58 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 489 KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQLD-IH 567
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS--------------IAYVSQEPwIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDvlTVEENlsILAsikGIPANNiiQEVQKVL----LDLDMQTIKD-----------NqakkLSGGQKRKLSLGIAVLGN 632
Cdd:cd03250 79 NG--TIREN--ILF---GKPFDE--ERYEKVIkacaLEPDLEILPDgdlteigekgiN----LSGGQKQRISLARAVYSD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 633 PKILLLDEPTAGMDP-CSRHIVWN-LLKYRKANRVTVFSTH---FMDEAD 677
Cdd:cd03250 146 ADIYLLDDPLSAVDAhVGRHIFENcILGLLLNNKTRILVTHqlqLLPHAD 195
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1290-1511 |
2.83e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 71.70 E-value: 2.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTI---INILVgdiEPTSGQVFLGDYSSET 1366
Cdd:PRK11264 4 IEVKNLVKKFHGQ-----------TVLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLE---QPEAGTIRVGDITIDT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDDDSLKCM--------GYCPQINPLWPDTTLQEHFeIYGA--VKGMSASDM----KEVISRIthALDLKEhlQKTVKK 1432
Cdd:PRK11264 70 ARSLSQQKGLirqlrqhvGFVFQNFNLFPHRTVLENI-IEGPviVKGEPKEEAtaraRELLAKV--GLAGKE--TSYPRR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1433 LPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11264 145 LSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIR-QLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
491-702 |
3.51e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 72.83 E-value: 3.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 491 GENVeALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeiDEMFEARKmIGICPQLDIHFDV 570
Cdd:PRK11432 17 GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT--HRSIQQRD-ICMVFQSYALFPH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 571 LTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPcsr 650
Cdd:PRK11432 93 MSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDA--- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 651 hivwNLlkyRKANR------------VTVFSTHFMDEADILADRKAVISQGMLKCVGS---------SMFLKS 702
Cdd:PRK11432 170 ----NL---RRSMRekirelqqqfniTSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMAS 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
478-689 |
3.74e-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: 74.09 E-value: 3.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGH----RVSEIDEMfe 553
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYWSgsplKASNIRDT-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 554 ARKMIGIcpqldIHFDvLTVEENLSILASI--------KG--IPANNIIQEVQKVLLDLDMQTIKDNQA-KKLSGGQKRK 622
Cdd:TIGR02633 76 ERAGIVI-----IHQE-LTLVPELSVAENIflgneitlPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 623 LSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDG 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1306-1514 |
4.64e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 73.67 E-value: 4.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1306 LLSRKVKKVatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSEDDDSLKCMGYCPQI-- 1382
Cdd:PRK09700 271 VTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLnGKDISPRSPLDAVKKGMAYITESrr 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1383 -NPLWPDTTLQEHFEIY---------GAVKGMSASDMKEVISRITHALDLKEH-LQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:PRK09700 349 dNGFFPNFSIAQNMAISrslkdggykGAMGLFHEVDEQRTAENQRELLALKCHsVNQNITELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQ-LADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1319-1511 |
5.04e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 5.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssETSEDDDSLKCMG----YCP---QINPLWPDTTL 1391
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNG---KEINALSTAQRLArglvYLPedrQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 qehfeiYGAVKGMSASDM---------KEVISRITHALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPST 1461
Cdd:PRK15439 359 ------AWNVCALTHNRRgfwikpareNAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 1462 GMDPKAKQHMWRAIRTAFKnRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK15439 433 GVDVSARNDIYQLIRSIAA-QNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
473-689 |
5.40e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.41 E-value: 5.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 473 VGKEAIRISGIQKtyrkkgenvEALRN-LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeIDEM 551
Cdd:PRK11288 253 LGEVRLRLDGLKG---------PGLREpISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID-IRSP 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 FEA-RKMIGICPQlDIHFD----VLTVEENLSILASIKGIPANNIIQE------VQKVLLDLDMQTIKDNQA-KKLSGG- 618
Cdd:PRK11288 323 RDAiRAGIMLCPE-DRKAEgiipVHSVADNINISARRHHLRAGCLINNrweaenADRFIRSLNIKTPSREQLiMNLSGGn 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 619 -QK----RKLSLGIavlgnpKILLLDEPTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK11288 402 qQKailgRWLSEDM------KVILLDEPTRGIDVGAKHEIYNVI-YELAAQgvaVLFVSSDLP-EVLGVADRIVVMREG 472
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1319-1511 |
5.82e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 73.51 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYCP---QINPLWPDTTLQE- 1393
Cdd:COG1129 271 VSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAgIAYVPedrKGEGLVLDLSIREn 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 ----HFEIYGAVKGMSASDMKEVISRITHALDLK-EHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAK 1468
Cdd:COG1129 351 itlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAK 430
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1469 QHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG1129 431 AEIYRLIR-ELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
493-710 |
6.94e-13 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 73.60 E-value: 6.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQLDIHFDVlT 572
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLS----------ILASIKGIPANNIIQEVQKvlldlDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:TIGR00958 571 VRENIAygltdtpdeeIMAAAKAANAHDFIMEFPN-----GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 643 AGMDPCSRHIVWNLLKyrKANRVTVFSTHFMDEADiLADRKAVISQGMLKCVGSSMFLKSKWGIGYRL 710
Cdd:TIGR00958 646 SALDAECEQLLQESRS--RASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMEDQGCYKHL 710
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
477-684 |
7.71e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 70.45 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGF----------ASIYGHRVS 546
Cdd:PRK14258 7 AIKVNNLSFYY----DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVrvegrveffnQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 547 eIDEMFEARKMIGICPQLdihFDvLTVEENLSILASIKGI-PANNIIQEVQKVLLDLDM-QTIKDN---QAKKLSGGQKR 621
Cdd:PRK14258 83 -LNRLRRQVSMVHPKPNL---FP-MSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLwDEIKHKihkSALDLSGGQQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYR--KANRVTVFSTHFMDEADILADRKA 684
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
494-689 |
8.96e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 72.65 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY---------GHRVSEidemfeaRKMIGIcpql 564
Cdd:PRK13549 18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqasNIRDTE-------RAGIAI---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 dIHFDvLTVEENLSILASI-------KG--IPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK13549 87 -IHQE-LALVKELSVLENIflgneitPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIAcIYISHKLNEVKAISDTICVIRDG 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1319-1525 |
9.99e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 72.18 E-value: 9.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQinplwpDTTLQEHFEIY 1398
Cdd:PRK09536 22 VDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQ------DTSLSFEFDVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVK-----------GMSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDpka 1467
Cdd:PRK09536 96 QVVEmgrtphrsrfdTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1468 kqhMWRAIRTAFKNRK-----RAAILTTHYMEEAEAVCDRVAIMVSGQLRCIG------TVQHLKSKFG 1525
Cdd:PRK09536 172 ---INHQVRTLELVRRlvddgKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAFD 237
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1319-1522 |
1.02e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 69.66 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINIL-VGDIePTSGQVFLG----DYSSETSEDDDSL--KCMGYCPQINPLWPD-TT 1390
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLnLLET-PDSGQLNIAghqfDFSQKPSEKAIRLlrQKVGMVFQQYNLWPHlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 LQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:COG4161 100 MENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1471 MWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:COG4161 180 VVEIIRE-LSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQ 230
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1310-1516 |
1.05e-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: 68.98 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1310 KVKKVATKY----------ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYC 1379
Cdd:cd03369 8 EVENLSVRYapdlppvlknVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1380 PQiNPLWPDTTLQEHFEIYGavkgmSASDMKevisrITHALDLKEhlqkTVKKLPAGIKRKLCFALSMLGNPQITLLDEP 1459
Cdd:cd03369 88 PQ-DPTLFSGTIRSNLDPFD-----EYSDEE-----IYGALRVSE----GGLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1460 STGMDPKAKQHMWRAIRTAFKNrkrAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:cd03369 153 TASIDYATDALIQKTIREEFTN---STILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1296-1528 |
1.18e-12 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 72.62 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1296 HKEYDDKKDFLLSRK--VKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgdyssetsEDDDSL 1373
Cdd:PRK13545 18 NKPFDKLKDLFFRSKdgEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI--------KGSAAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1374 KCMGycpqiNPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQI 1453
Cdd:PRK13545 90 IAIS-----SGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1454 TLLDEP-STGMDPKAKQHMWRAirTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFG---KGY 1528
Cdd:PRK13545 165 LVIDEAlSVGDQTFTKKCLDKM--NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDeflKKY 241
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
499-675 |
1.19e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 72.57 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIDEMfEARKMI---GICPQLdIHfdvLTVEE 575
Cdd:PRK11174 368 PLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP-YQGSLKINGIELRELDPE-SWRKHLswvGQNPQL-PH---GTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NLSiLASIKgipANNiiQEVQKVL-------------LDLDMQtIKDnQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK11174 442 NVL-LGNPD---ASD--EQLQQALenawvseflpllpQGLDTP-IGD-QAAGLSVGQAQRLALARALLQPCQLLLLDEPT 513
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 643 AGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDE 675
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMVTHQLED 546
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1323-1493 |
1.31e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.53 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgdyssetsedDDSLKcMGYCPQInpLWPDTTLQEHFEIYGAVK 1402
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV------------DPELK-ISYKPQY--IKPDYDGTVEDLLRSITD 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1403 GMSASDMKeviSRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNR 1482
Cdd:PRK13409 427 DLGSSYYK---SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER 503
|
170
....*....|...
gi 27262626 1483 KRAAILTTH--YM 1493
Cdd:PRK13409 504 EATALVVDHdiYM 516
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
478-676 |
1.70e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 70.11 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGE-NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIYGHRVSEIDEM 551
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewiFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 F------------------EARKMIGICPQLDIH--FDVlTVEENLSILASIKGIPANNIIQEVQKV--LLDLDMQTIKD 609
Cdd:PRK13651 83 VleklviqktrfkkikkikEIRRRVGVVFQFAEYqlFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYieLVGLDESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 610 NQAKkLSGGQKRKLSL-GIAVLgNPKILLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEA 676
Cdd:PRK13651 162 SPFE-LSGGQKRRVALaGILAM-EPDFLVFDEPTAGLDPQGVKEILEIFdNLNKQGKTIILVTHDLDNV 228
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1319-1516 |
2.12e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEiY 1398
Cdd:PRK11231 21 LSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTPEGITVRELVA-Y 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 G-----AVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:PRK11231 100 GrspwlSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMR 179
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 1474 AIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK11231 180 LMRE-LNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
509-705 |
2.13e-12 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 70.67 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 509 ITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMF----EARKmIGICPQ---LDIHFdvlTVEENLSIla 581
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppEKRR-IGYVFQdarLFPHY---KVRGNLRY-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 582 sikGIPANNIIQEVQKVLLdLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD-PCSRHivwnLLKY- 659
Cdd:PRK11144 100 ---GMAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE----LLPYl 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 660 -RKANRVT---VFSTHFMDEADILADRKAVISQGMLKCVGSsmfLKSKWG 705
Cdd:PRK11144 172 eRLAREINipiLYVSHSLDEILRLADRVVVLEQGKVKAFGP---LEEVWA 218
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1286-1529 |
2.27e-12 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 71.78 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1286 EKPSIMVSNLHKEYDDKKDFLLSRkvkkvatkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYS-S 1364
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDQPQPVLKG---------LSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPiA 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1365 ETSEDDdsLK-CMGYCPQINPLWPDtTLQEHFEIYGAvkgmSASD--MKEVISRIthalDLKEHLQkTVKKLPA------ 1435
Cdd:PRK11160 406 DYSEAA--LRqAISVVSQRVHLFSA-TLRDNLLLAAP----NASDeaLIEVLQQV----GLEKLLE-DDKGLNAwlgegg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1436 -----GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMEEAEAVcDRVAIMVSGQ 1510
Cdd:PRK11160 474 rqlsgGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQN--KTVLMITHRLTGLEQF-DRICVMDNGQ 550
|
250
....*....|....*....
gi 27262626 1511 LRCIGTVQHLKSKFGkGYF 1529
Cdd:PRK11160 551 IIEQGTHQELLAQQG-RYY 568
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
474-691 |
2.37e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 2.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 474 GKEAIRISGIqkTYRKKGeNVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE--IDEM 551
Cdd:COG3845 254 GEVVLEVENL--SVRDDR-GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGlsPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 552 FEA--------RKMIGICPQldihfdvLTVEENLsILASIKGIPANN--------IIQEVQKVLLDLDmqtIK----DNQ 611
Cdd:COG3845 331 RRLgvayipedRLGRGLVPD-------MSVAENL-ILGRYRRPPFSRggfldrkaIRAFAEELIEEFD---VRtpgpDTP 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 612 AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANR-VTVFSTHfMDEADILADRKAVISQG 689
Cdd:COG3845 400 ARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAaVLLISED-LDEILALSDRIAVMYEG 478
|
..
gi 27262626 690 ML 691
Cdd:COG3845 479 RI 480
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
497-675 |
2.42e-12 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.20 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID-EMFeaRKMIGICPQLDIHFDVlTVEE 575
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpEIY--RQQVSYCAQTPTLFGD-TVYD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NLSILASIKgipanNIIQEVQKVLLDLDM----QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:PRK10247 100 NLIFPWQIR-----NQQPDPAIFLDDLERfalpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 27262626 652 IVWNLL-KYRKANRVTV-FSTHFMDE 675
Cdd:PRK10247 175 NVNEIIhRYVREQNIAVlWVTHDKDE 200
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
478-689 |
2.60e-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: 65.93 E-value: 2.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFaSIYGHRVSeidemfearkm 557
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 IGICPQLdihfdvltveenlsilasikgipanniiqevqkvlldldmqtikdnqakklSGGQKRKLSLGIAVLGNPKILL 637
Cdd:cd03221 65 IGYFEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLL 93
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 638 LDEPTAGMDPCSRHIVWNLLKYRKANRVTVfsTH---FMDEadiLADRKAVISQG 689
Cdd:cd03221 94 LDEPTNHLDLESIEALEEALKEYPGTVILV--SHdryFLDQ---VATKIIELEDG 143
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1323-1520 |
2.72e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 68.79 E-value: 2.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIE-----PTSGQVFLGD---YSSETSEDDDSLKCMGYCPqiNPLwPDTTLQEH 1394
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGqdiFKMDVIELRRRVQMVFQIP--NPI-PNLSIFEN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 FEIyGAVKGMSASDMKEVISRITHALD-------LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPK- 1466
Cdd:PRK14247 103 VAL-GLKLNRLVKSKKELQERVRWALEkaqlwdeVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPEn 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1467 -AKqhmwraIRTAFKNRKR--AAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK14247 182 tAK------IESLFLELKKdmTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREV 232
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
480-671 |
2.73e-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: 72.25 E-value: 2.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 480 ISGIQKTYRKKGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEIdEMFEARKMIG 559
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSV-TLQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 560 ICPQlDIHFDVLTVEENLSILASIKGipanniiQEVQKVLLDLDMQTIKDNQAKK-----------LSGGQKRKLSLGIA 628
Cdd:TIGR01271 1296 VIPQ-KVFIFSGTFRKNLDPYEQWSD-------EEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARS 1367
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:TIGR01271 1368 ILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEH 1410
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1324-1476 |
3.41e-12 |
|
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: 71.35 E-value: 3.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1324 KKGEILGLLGPNGAGKSTIINILVGDIEPTsgqvfLGDYSSETSEDDDSLKCMGycpqinplwpdTTLQEHFE------- 1396
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPN-----LGDYDEEPSWDEVLKRFRG-----------TELQDYFKklangei 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 -----------IYGAVKG-----MSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPS 1460
Cdd:COG1245 161 kvahkpqyvdlIPKVFKGtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
170
....*....|....*.
gi 27262626 1461 TGMDPKAKQHMWRAIR 1476
Cdd:COG1245 241 SYLDIYQRLNVARLIR 256
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
492-671 |
3.42e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 71.98 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 492 ENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY-GHRVSEIDEMFeARKMIGICPQLDIHF-- 568
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINdSHNLKDINLKW-WRSKIGVVSQDPLLFsn 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 -------------------------DVLTVEENLSILASIKGIPA---NNIIQEVQKV-LLDL--DMQTIKDNQ------ 611
Cdd:PTZ00265 475 siknnikyslyslkdlealsnyyneDGNDSQENKNKRNSCRAKCAgdlNDMSNTTDSNeLIEMrkNYQTIKDSEvvdvsk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 612 ----------------------AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKA--NRVTV 667
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGneNRITI 634
|
....
gi 27262626 668 FSTH 671
Cdd:PTZ00265 635 IIAH 638
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1319-1518 |
3.82e-12 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 68.22 E-value: 3.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQinplwpDTTLQEHF--- 1395
Cdd:COG4559 20 VSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQ------HSSLAFPFtve 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYG---AVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFA--LSML-----GNPQITLLDEPSTGMDP 1465
Cdd:COG4559 94 EVVAlgrAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLArvLAQLwepvdGGPRWLFLDEPTSALDL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1466 KAKQHMWRAIRTaFKNRKRAAI-------LTTHYmeeaeavCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG4559 174 AHQHAVLRLARQ-LARRGGGVVavlhdlnLAAQY-------ADRILLLHQGRLVAQGTPE 225
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1509 |
4.36e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 68.61 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSE 1368
Cdd:PRK13647 5 IEVEDLHFRYKDGTK----------ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 D-------------DDSLKCMgycpqinPLWPDTTlqehfeiYGAVK-GMSASDMKEVISRITHALDLKEHLQKTVKKLP 1434
Cdd:PRK13647 75 KwvrskvglvfqdpDDQVFSS-------TVWDDVA-------FGPVNmGLDKDEVERRVEEALKAVRMWDFRDKPPYHLS 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1435 AGIKRKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMwRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK13647 141 YGQKKRVAIAgvLAM--DPDVIVLDEPMAYLDPRGQETL-MEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
509-691 |
4.43e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 4.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 509 ITALLGHSGTGKSTLMNILCGLCPPSDGF-----ASIYGHRVSEIDEMFEARKMIGICPQLDIHFDVLTVEENLSILASI 583
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 584 KGIPANNIIQEVQKVLLDLDM-QTIKDNQAK---KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKy 659
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTEVGLwDAVKDRLSDspfRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIR- 207
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 660 RKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK14271 208 SLADRLTViIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1287-1511 |
5.51e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 67.88 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1287 KPSIMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINIL--VGDIEP---TSGQV-FLG 1360
Cdd:PRK14239 3 EPILQVSDLSVYYNKKK-----------ALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIvYNG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1361 -DYSSETSEDDDSLKCMGYC-PQINPlWPdttlqehFEIY-GAVKGMSASDMKEViSRITHALD-----------LKEHL 1426
Cdd:PRK14239 72 hNIYSPRTDTVDLRKEIGMVfQQPNP-FP-------MSIYeNVVYGLRLKGIKDK-QVLDEAVEkslkgasiwdeVKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1427 QKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQhmwRAIRTAFKNRKRAAILT-THYMEEAEAVCDRVAI 1505
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAG---KIEETLLGLKDDYTMLLvTRSMQQASRISDRTGF 219
|
....*.
gi 27262626 1506 MVSGQL 1511
Cdd:PRK14239 220 FLDGDL 225
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1323-1491 |
5.79e-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: 67.78 E-value: 5.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTsgqvfLGDYSSETSEDDdslkcmgycpqINPLWPDTTLQEHFE------ 1396
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAGKLKPN-----LGKFDDPPDWDE-----------ILDEFRGSELQNYFTkllegd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 ------------IYGAVKG-----MSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEP 1459
Cdd:cd03236 87 vkvivkpqyvdlIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|..
gi 27262626 1460 STGMDPKAKQHMWRAIRTAFKNrKRAAILTTH 1491
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAED-DNYVLVVEH 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
497-692 |
5.84e-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: 5.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpSDGFASIYGHRVSEIdEMFEARKMIGICPQLDIHFDVlTVEEN 576
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSV-PLQKWRKAFGVIPQKVFIFSG-TFRKN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 LSILASIKGipanniiQEVQKVLLDLDMQTIKDNQAKKL-----------SGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03289 97 LDPYGKWSD-------EEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27262626 646 DPCSRHIVWNLLKYRKANRVTVFSTHFMdEADILADRKAVISQGMLK 692
Cdd:cd03289 170 DPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVR 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1319-1516 |
6.42e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 67.71 E-value: 6.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSE-TSEDDDSLKCMGYCPQINPLWPDTTLQEHFEI 1397
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEgLPGHQIARMGVVRTFQHVRLFREMTVIENLLV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 -------YGAVKGMSASDM-----KEVISRITHALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:PRK11300 104 aqhqqlkTGLFSGLLKTPAfrraeSEALDRAATWLErvgLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1463 MDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGT 1516
Cdd:PRK11300 184 LNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
478-657 |
7.16e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.51 E-value: 7.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKG-----ENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMF 552
Cdd:PRK15112 5 LEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 553 EARK--MI------GICPQLDIH--FDV-LTVEENLSILASIKgipanNIIQEVQKVLLDLDMQTIKDNQakkLSGGQKR 621
Cdd:PRK15112 85 RSQRirMIfqdpstSLNPRQRISqiLDFpLRLNTDLEPEQREK-----QIIETLRQVGLLPDHASYYPHM---LAPGQKQ 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 622 KLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLL 657
Cdd:PRK15112 157 RLGLARALILRPKVIIADEALASLDMSMRSQLINLM 192
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1286-1464 |
7.77e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 66.76 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1286 EKPSIMVSNLHKEYDDKKdflLSRKVkkvaTKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYS-- 1363
Cdd:PRK11629 2 NKILLQCDNLCKRYQEGS---VQTDV----LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPms 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1364 --SETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKL 1441
Cdd:PRK11629 75 klSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRV 154
|
170 180
....*....|....*....|...
gi 27262626 1442 CFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK11629 155 AIARALVNNPRLVLADEPTGNLD 177
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1319-1511 |
8.45e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 8.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCmG----YcpQINPLWPDTTLQEH 1394
Cdd:PRK11288 23 ISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA-GvaiiY--QELHLVPEMTVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 feIY--------GAVkgmsasDMKEVISRITHALD-LKEHL--QKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:PRK11288 100 --LYlgqlphkgGIV------NRRLLNYEAREQLEhLGVDIdpDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 1464 DPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK11288 172 SAREIEQLFRVIR-ELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1319-1519 |
8.56e-12 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.96 E-value: 8.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG----DYSSETSEDDDSL--KCMGYCPQINPLWPDTTLQ 1392
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfDFSKTPSDKAIRElrRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHF-EIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:PRK11124 101 QNLiEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 1472 WRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQH 1519
Cdd:PRK11124 181 VSIIR-ELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC 227
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
496-690 |
1.19e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 66.94 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 496 ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKMIGICPQLDIHFDVLTVEE 575
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NL----------SILASIKGIPA---------NNIIQEVQKV-LLDLdmqtiKDNQAKKLSGGQKRKLSLGIAVLGNPKI 635
Cdd:PRK11300 100 NLlvaqhqqlktGLFSGLLKTPAfrraesealDRAATWLERVgLLEH-----ANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 636 LLLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFST-HFMDEADILADRKAVISQGM 690
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIaELRNEHNVTVLLIeHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
503-709 |
1.19e-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: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemfearkmigICPQ-LDIHFDVlTVEENLSILA 581
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQyIKADYEG-TVRDLLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 582 SIKGIPA---NNIIQEVQkvlldldMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK 658
Cdd:cd03237 87 KDFYTHPyfkTEIAKPLQ-------IEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 659 -YRKANRVTVFST-HFMDEADILADRKAVIS------------QGMLKcvGSSMFLKSkWGIGYR 709
Cdd:cd03237 160 rFAENNEKTAFVVeHDIIMIDYLADRLIVFEgepsvngvanppQSLRS--GMNRFLKN-LDITFR 221
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1323-1512 |
1.21e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.34 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSEDDDSL---KCMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvGQPLHQMDEEARAKlraKHVGFVFQSFMLIPTLNALENVELP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQhmwRAIRTA 1478
Cdd:PRK10584 113 ALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD---KIADLL 189
|
170 180 190
....*....|....*....|....*....|....*..
gi 27262626 1479 FK-NRKRAA--ILTTHYMEEAeAVCDRVAIMVSGQLR 1512
Cdd:PRK10584 190 FSlNREHGTtlILVTHDLQLA-ARCDRRLRLVNGQLQ 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
487-692 |
1.26e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 66.92 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 487 YRKKGENvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE------MFEARKMIGI 560
Cdd:PRK10619 12 HKRYGEH-EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDkdgqlkVADKNQLRLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 561 CPQLDI---HFDV---LTVEEN-----LSILASIKGIPANNIIQEVQKVLLDldmQTIKDNQAKKLSGGQKRKLSLGIAV 629
Cdd:PRK10619 91 RTRLTMvfqHFNLwshMTVLENvmeapIQVLGLSKQEARERAVKYLAKVGID---ERAQGKYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 630 LGNPKILLLDEPTAGMDPcsrHIVWNLL----KYRKANRVTVFSTHFMDEADILADRKAVISQGMLK 692
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDP---ELVGEVLrimqQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1323-1482 |
1.30e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.45 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTsgqvfLGDYSSETSEDDDSLKCMGycpqinplwpdTTLQEHFE------ 1396
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPN-----LGDYEEEPSWDEVLKRFRG-----------TELQNYFKklynge 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 ------------IYGAVKGmSASD----------MKEVISRithaLDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQIT 1454
Cdd:PRK13409 160 ikvvhkpqyvdlIPKVFKG-KVREllkkvdergkLDEVVER----LGLENILDRDISELSGGELQRVAIAAALLRDADFY 234
|
170 180
....*....|....*....|....*...
gi 27262626 1455 LLDEPSTGMDPKAKQHMWRAIRTAFKNR 1482
Cdd:PRK13409 235 FFDEPTSYLDIRQRLNVARLIRELAEGK 262
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1290-1511 |
1.50e-11 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 67.80 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsRKVkkVATKYISFCVKKGEILGLLGPNGAGKST---IINILvgdiE-PTSGQVFLgdysse 1365
Cdd:COG1135 2 IELENLSKTFPTKG-----GPV--TALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLL----ErPTSGSVLV------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1366 tseDDDSLkcmgycpqinplwpdTTLQE---------------HFE------IYGAV------KGMSASDMKEvisRITH 1418
Cdd:COG1135 65 ---DGVDL---------------TALSErelraarrkigmifqHFNllssrtVAENValpleiAGVPKAEIRK---RVAE 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1419 ALDL-----KEHlqktvkKLPA----------GIKRklcfALSMlgNPQITLLDEPSTGMDPKAKQhmwrAIRTAFK--N 1481
Cdd:COG1135 124 LLELvglsdKAD------AYPSqlsggqkqrvGIAR----ALAN--NPKVLLCDEATSALDPETTR----SILDLLKdiN 187
|
250 260 270
....*....|....*....|....*....|..
gi 27262626 1482 RKRAA--ILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG1135 188 RELGLtiVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
497-653 |
1.70e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 69.49 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcPPSDGFasIYGH-RVSEIDEMFEARKMI-GICPQLDIHFDVLTVE 574
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGY--IEGDiRISGFPKKQETFARIsGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 575 ENLsILASIKGIPANNIIQE----VQKVLLDLDMQTIKDN-----QAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:PLN03140 972 ESL-IYSAFLRLPKEVSKEEkmmfVDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
....*...
gi 27262626 646 DPCSRHIV 653
Cdd:PLN03140 1051 DARAAAIV 1058
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
499-689 |
1.89e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 66.33 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEID--EMFEARKMIGICPQLDIHFDVLTVEEN 576
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 LSI-LASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN 655
Cdd:PRK11831 105 VAYpLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 27262626 656 LL-KYRKANRVT-VFSTH-------FMDEADILADRKaVISQG 689
Cdd:PRK11831 185 LIsELNSALGVTcVVVSHdvpevlsIADHAYIVADKK-IVAHG 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
495-646 |
2.03e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.51 E-value: 2.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS--EIDEMFEA--------RKMIGICPQL 564
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirSPRDAIRAgiayvpedRKGEGLVLDL 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIhfdvltvEENLSiLASIKGIPANNII------QEVQKVLLDLDmqtIK----DNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:COG1129 346 SI-------RENIT-LASLDRLSRGGLLdrrrerALAEEYIKRLR---IKtpspEQPVGNLSGGNQQKVVLAKWLATDPK 414
|
170
....*....|..
gi 27262626 635 ILLLDEPTAGMD 646
Cdd:COG1129 415 VLILDEPTRGID 426
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1290-1517 |
2.14e-11 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 67.13 E-value: 2.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsRKVkkVATKYISFCVKKGEILGLLGPNGAGKST---IINILVgdiEPTSGQVFLGDysset 1366
Cdd:PRK11153 2 IELKNISKVFPQGG-----RTI--HALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLE---RPTSGRVLVDG----- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 sEDDDSLKcmgycpqinplwpDTTLQE----------HFE------IYGAV------KGMSASDMKeviSRITHALDLKE 1424
Cdd:PRK11153 67 -QDLTALS-------------EKELRKarrqigmifqHFNllssrtVFDNValplelAGTPKAEIK---ARVTELLELVG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1425 hLQKTVKKLPA----------GIKRklcfALSMlgNPQITLLDEPSTGMDPKAKqhmwRAIRTAFK--NRKR--AAILTT 1490
Cdd:PRK11153 130 -LSDKADRYPAqlsggqkqrvAIAR----ALAS--NPKVLLCDEATSALDPATT----RSILELLKdiNRELglTIVLIT 198
|
250 260
....*....|....*....|....*..
gi 27262626 1491 HYMEEAEAVCDRVAIMVSGQLRCIGTV 1517
Cdd:PRK11153 199 HEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1315-1564 |
2.35e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 66.16 E-value: 2.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSEDDDSLKCMGYCPQiNP--LWPDTTL 1391
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsGIDTGDFSKLQGIRKLVGIVFQ-NPetQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1472 WRAIRTaFKNRKRAAILTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGKGYfLEIKLKDWIENLEvdRLQR-EI 1550
Cdd:PRK13644 176 LERIKK-LHEKGKTIVYITHNLEELHDA-DRIIVMDRGKIVLEGEPENVLSDVSLQT-LGLTPPSLIELAE--NLKMhGV 250
|
250
....*....|....
gi 27262626 1551 QYIFPNASRQESFS 1564
Cdd:PRK13644 251 VIPWENTSSPSSFA 264
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1319-1528 |
2.98e-11 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 65.49 E-value: 2.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDdslkcMGYCPQINPLWPDTTLQEHFEIY 1398
Cdd:PRK11248 20 INLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE-----RGVVFQNEGLLPWRNVQDNVAFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTA 1478
Cdd:PRK11248 95 LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQTLLLKL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 1479 FKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRcigTVQHLKSKFGKGY 1528
Cdd:PRK11248 175 WQETGKQVLLITHDIEEAVFMATELVLLSPGPGR---VVERLPLNFARRF 221
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
501-689 |
3.16e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 64.99 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG--HRVSEIdemfeARKMIGICPQLDIHFDVLTVEENLS 578
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGqdHTTTPP-----SRRPVSMLFQENNLFSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 579 IlasikGIPANNIIQEVQKVLLdldmQTIKDNQA---------KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCS 649
Cdd:PRK10771 94 L-----GLNPGLKLNAAQREKL----HAIARQMGiedllarlpGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPAL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 650 RHIVWNLLKYRKANR-VTVFS-THFMDEADILADRKAVISQG 689
Cdd:PRK10771 165 RQEMLTLVSQVCQERqLTLLMvSHSLEDAARIAPRSLVVADG 206
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
495-691 |
3.22e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE----------MFEARKMIGICPQL 564
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvyLPEDRQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHFDVLTVEENLSILAsIKGIPANNIIQEVQKVLldldmqTIK----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK15439 357 PLAWNVCALTHNRRGFW-IKPARENAVLERYRRAL------NIKfnhaEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 641 PTAGMDPCSRHIVWNLLKYRKANRVTV-FSTHFMDEADILADRKAVISQGML 691
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQNVAVlFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
467-691 |
3.45e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 67.69 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 467 PVSSEFVGKEAIRISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVS 546
Cdd:PRK10522 312 PRPQAFPDWQTLELRNVTFAY---QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 547 EiDEMFEARKMIGICPQlDIH-FDVLTVEEnlsilasikGIPANNiiQEVQKVLLDLDMQ---TIKDNQAK--KLSGGQK 620
Cdd:PRK10522 389 A-EQPEDYRKLFSAVFT-DFHlFDQLLGPE---------GKPANP--ALVEKWLERLKMAhklELEDGRISnlKLSKGQK 455
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 621 RKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10522 456 KRLALLLALAEERDILLLDEWAADQDPHFRREFYQvLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQL 527
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1292-1464 |
4.00e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 67.61 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKDFllsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgdYSSETSEddd 1371
Cdd:PRK15064 322 VENLTKGFDNGPLF-----------KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----KWSENAN--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1372 slkcMGYCPQINPLW--PDTTLQEHFEIYG-------AVKGM------SASDMKevisrithaldlkehlqKTVKKLPAG 1436
Cdd:PRK15064 384 ----IGYYAQDHAYDfeNDLTLFDWMSQWRqegddeqAVRGTlgrllfSQDDIK-----------------KSVKVLSGG 442
|
170 180
....*....|....*....|....*...
gi 27262626 1437 IKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK15064 443 EKGRMLFGKLMMQKPNVLVMDEPTNHMD 470
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
453-646 |
4.14e-11 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 67.68 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 453 GNVNGNISFseiiEPVSSEFVGKEairisgiqktyrkkgenvEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP 532
Cdd:PRK13657 329 GRVKGAVEF----DDVSFSYDNSR------------------QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFD 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 533 PSDGFASIYGHRVSEIDeMFEARKMIGICPQLDIHFDvLTVEENLSI----------LASIKGIPANNIIQevqKVLLDL 602
Cdd:PRK13657 387 PQSGRILIDGTDIRTVT-RASLRRNIAVVFQDAGLFN-RSIEDNIRVgrpdatdeemRAAAERAQAHDFIE---RKPDGY 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 603 DmqTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK13657 462 D--TVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALD 503
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1326-1520 |
5.16e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.19 E-value: 5.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1326 GEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFEI-----YGA 1400
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwHGA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1401 VKGMSASDMKEVISRIThALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFK 1480
Cdd:PRK10575 117 LGRFGAADREKVEEAIS-LVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQ 195
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 1481 NRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK10575 196 ERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1309-1529 |
5.35e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 67.38 E-value: 5.35e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1309 RKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEP---TSGQVFLGDYSSEtsedddsLKCM----GYCPQ 1381
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID-------AKEMraisAYVQQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1382 INPLWPDTTLQEHFEIYGAVK---GMSASDMKEVISRITHALDLKEhLQKT-------VKKLPAGIKRKLCFALSMLGNP 1451
Cdd:TIGR00955 107 DDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRK-CANTrigvpgrVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHyMEEAEAVC--DRVAIMVSGQLRCIGTVQHLKSKFGKGYF 1529
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLK-GLAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLGSPDQAVPFFSDLGH 263
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
499-692 |
6.13e-11 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 66.77 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-DGFASIYGHRV----------SEIDEMFEARKMIGICPQLDIH 567
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdirnpaqairAGIAMVPEDRKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVltveeNLSILASIKGIPANNIIQEVQKVLLDLDMQTIK----DNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTA 643
Cdd:TIGR02633 358 KNI-----TLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKtaspFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 27262626 644 GMDPCSRHIVWNLLKY--RKANRVTVFSTHfMDEADILADRKAVISQGMLK 692
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQlaQEGVAIIVVSSE-LAEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1319-1518 |
6.52e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 64.77 E-value: 6.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQiNP--LWPDTTLQehFE 1396
Cdd:PRK13648 28 VSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQ-NPdnQFVGSIVK--YD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 IYGAVKGMSAS--DMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRA 1474
Cdd:PRK13648 105 VAFGLENHAVPydEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDL 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 27262626 1475 IRTAFKNRKRAAILTTHYMEEAeAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:PRK13648 185 VRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPT 227
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
488-640 |
6.80e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 66.84 E-value: 6.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 488 RKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGhrvseidemfeARKMIGICPQLDih 567
Cdd:PRK13545 31 SKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLN-- 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 568 fDVLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK13545 98 -GQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE 169
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1320-1511 |
7.55e-11 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 63.83 E-value: 7.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-GDYSSETSEDDDSLKcMGYcpQINPLWPDTTLQEHFEIy 1398
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLnGQDHTTTPPSRRPVS-MLF--QENNLFSHLTVAQNIGL- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMS-ASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRT 1477
Cdd:PRK10771 95 GLNPGLKlNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190
....*....|....*....|....*....|....
gi 27262626 1478 AFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10771 175 VCQERQLTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1319-1530 |
9.34e-11 |
|
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: 63.66 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWpDTTLQEHFEIy 1398
Cdd:cd03252 21 ISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLF-NRSIRDNIAL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 gavkGMSASDMKEVI--SRITHA----LDLKEHLQKTVKK----LPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAK 1468
Cdd:cd03252 99 ----ADPGMSMERVIeaAKLAGAhdfiSELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDYESE 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1469 QHMWRAIRTAFKNrkRAAILTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSKFGKGYFL 1530
Cdd:cd03252 175 HAIMRNMHDICAG--RTVIIIAHRLSTVKNA-DRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
459-695 |
9.37e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 64.45 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 459 ISFSEIIEPVSSEF----VGKEAIRISGIQKtyrKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS 534
Cdd:PRK13546 1 MNVSVNIKNVTKEYriyrTNKERMKDALIPK---HKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 535 DGFASIYGHrVSeidemfearkMIGICPQLDIHfdvLTVEENLSILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKK 614
Cdd:PRK13546 78 VGKVDRNGE-VS----------VIAISAGLSGQ---LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 615 LSGGQKRKLSLGIAVLGNPKILLLDEP-TAGMDPCSRHIVWNLLKYRKANRVTVFSTHFMDEADILADRKAVISQGMLKC 693
Cdd:PRK13546 144 YSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
..
gi 27262626 694 VG 695
Cdd:PRK13546 224 YG 225
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
467-689 |
9.52e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.42 E-value: 9.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 467 PVSSEFVGKEAIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYG---- 542
Cdd:PRK10261 2 PHSDELDARDVLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 543 ---HRVSEIDEMFEAR---------KMIGICPQLDIHfDVLTVEENlsILASIK---GIPANNIIQEVQKvLLDL----D 603
Cdd:PRK10261 82 rrsRQVIELSEQSAAQmrhvrgadmAMIFQEPMTSLN-PVFTVGEQ--IAESIRlhqGASREEAMVEAKR-MLDQvripE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 604 MQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKY--RKANRVTVFSTHFMDEADILAD 681
Cdd:PRK10261 158 AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVlqKEMSMGVIFITHDMGVVAEIAD 237
|
....*...
gi 27262626 682 RKAVISQG 689
Cdd:PRK10261 238 RVLVMYQG 245
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1320-1509 |
9.81e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 64.52 E-value: 9.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSEDDdslkCMGYCPQINPL-WPDTTLQEHFEI 1397
Cdd:PRK15056 27 SFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKIsILGQPTRQALQKN----LVAYVPQSEEVdWSFPVLVEDVVM 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 YGAVKGM------SASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:PRK15056 103 MGRYGHMgwlrraKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARI 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 27262626 1472 WRAIRtAFKNRKRAAILTTHYMEEAEAVCDrVAIMVSG 1509
Cdd:PRK15056 182 ISLLR-ELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
497-646 |
1.29e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.80 E-value: 1.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE----------IDEMFEARKMIGIcpqldi 566
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTrspqdglangIVYISEDRKRDGL------ 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 hfdVL--TVEENLSILA----SIKGIPANNIiQEVQKVLLDLDMQTIK----DNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK10762 342 ---VLgmSVKENMSLTAlryfSRAGGSLKHA-DEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170
....*....|
gi 27262626 637 LLDEPTAGMD 646
Cdd:PRK10762 418 ILDEPTRGVD 427
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
477-646 |
1.68e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 65.89 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYRKkGENVeaLRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFeARK 556
Cdd:PRK10790 340 RIDIDNVSFAYRD-DNLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV-LRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICPQ-----LDIHFDVLTVEENLSILASIKgipannIIQEVQKVLLDLDM----QTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK10790 416 GVAMVQQdpvvlADTFLANVTLGRDISEEQVWQ------ALETVQLAELARSLpdglYTPLGEQGNNLSVGQKQLLALAR 489
|
170
....*....|....*....
gi 27262626 628 AVLGNPKILLLDEPTAGMD 646
Cdd:PRK10790 490 VLVQTPQILILDEATANID 508
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1319-1529 |
1.71e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTT------LQ 1392
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVrfnidpFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEIyGAVKGMSASDMKEVISRITHALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:PLN03232 1335 EHNDA-DLWEALERAHIKDVIDRNPFGLDAE--VSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQ 1411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1473 RAIRTAFKNrkrAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSKFGKGYF 1529
Cdd:PLN03232 1412 RTIREEFKS---CTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFF 1465
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
495-646 |
1.94e-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: 62.04 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 495 EALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQLDIHFDVlTVE 574
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP-LEDLRSSLTIIPQDPTLFSG-TIR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 575 ENLSILasikgipanNIIQEVQkVLLDLDMQTIKDNqakkLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03369 100 SNLDPF---------DEYSDEE-IYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1319-1511 |
2.24e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.57 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSEDDDSLK-CMGYCPQiNP--LWPDTTLQEHF 1395
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-DGELLTAENVWNLRrKIGMVFQ-NPdnQFVGATVEDDV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAI 1475
Cdd:PRK13642 104 AFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190
....*....|....*....|....*....|....*..
gi 27262626 1476 RtAFKNRKRAAILT-THYMEEAeAVCDRVAIMVSGQL 1511
Cdd:PRK13642 184 H-EIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEI 218
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
1292-1509 |
2.36e-10 |
|
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: 62.66 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGD--IEPTSGQV-FLGDYSSETSE 1368
Cdd:TIGR01978 3 IKDLHVSVEDKE--IL---------KGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsYEVTSGTIlFKGQDLLELEP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKCMGYCPQINPLWPDTTLQEhFeIYGAVKGMSASDMKEVISrithALDLKEHLQKTVKKL---PAGIKRKL---- 1441
Cdd:TIGR01978 72 DERARAGLFLAFQYPEEIPGVSNLE-F-LRSALNARRSARGEEPLD----LLDFEKLLKEKLALLdmdEEFLNRSVnegf 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1442 ---------CFALSMLgNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVC-DRVAIMVSG 1509
Cdd:TIGR01978 146 sggekkrneILQMALL-EPKLAILDEIDSGLDIDALKIVAEGIN-RLREPDRSFLIITHYQRLLNYIKpDYVHVLLDG 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
497-646 |
2.37e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEARKmIGICPQLDIHFDVLTVEEn 576
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTVRE- 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 577 lsiLASIKGIPANNII--------QEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK10575 105 ---LVAIGRYPWHGALgrfgaadrEKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
500-647 |
3.30e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 61.79 E-value: 3.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 500 LSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfeARKM--IGICPQLDIHFDVLtveENL 577
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR---SRFMayLGHLPGLKADLSTL---ENL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 578 SILASIKGIPANniiQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13543 104 HFLCGLHGRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
498-691 |
3.45e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 64.42 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 498 RNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV---SEIDEM-------FEARKMIGICPQLDIh 567
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIsprSPLDAVkkgmayiTESRRDNGFFPNFSI- 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 fdvltvEENLSILASIK--------GIPANNI---IQEVQKVLLDLDMQTIKDNqAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:PRK09700 359 ------AQNMAISRSLKdggykgamGLFHEVDeqrTAENQRELLALKCHSVNQN-ITELSGGNQQKVLISKWLCCCPEVI 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 637 LLDEPTAGMDPCSRHIVWNLL-KYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK09700 432 IFDEPTRGIDVGAKAEIYKVMrQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
1292-1516 |
3.56e-10 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 62.01 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKdfLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVG--DIEPTSGQVFL-GDYSSETSE 1368
Cdd:COG0396 3 IKNLHVSVEGKE--IL---------KGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLdGEDILELSP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKCMGYCPQiNPLwpdttlqehfeiygAVKGMSASD-MKEVISRIT----HALDLKEHLQKTVKKLpaGIKRKLC- 1442
Cdd:COG0396 72 DERARAGIFLAFQ-YPV--------------EIPGVSVSNfLRTALNARRgeelSAREFLKLLKEKMKEL--GLDEDFLd 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1443 -----------------FALSMLgNPQITLLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHY---MEEAEAvcDR 1502
Cdd:COG0396 135 ryvnegfsggekkrneiLQMLLL-EPKLAILDETDSGLDIDALRIVAEGVN-KLRSPDRGILIITHYqriLDYIKP--DF 210
|
250
....*....|....
gi 27262626 1503 VAIMVSGQLRCIGT 1516
Cdd:COG0396 211 VHVLVDGRIVKSGG 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1319-1491 |
3.92e-10 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 61.36 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDD--DSLKCMGYCPQINplwPDTTLQEHFE 1396
Cdd:PRK13538 20 LSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhQDLLYLGHQPGIK---TELTALENLR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 IYGAVKGMSASDmkevisRITHALD---LK--EHLqkTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKA---- 1467
Cdd:PRK13538 97 FYQRLHGPGDDE------ALWEALAqvgLAgfEDV--PVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGvarl 168
|
170 180
....*....|....*....|....
gi 27262626 1468 KQHMWRAIRtafknRKRAAILTTH 1491
Cdd:PRK13538 169 EALLAQHAE-----QGGMVILTTH 187
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
507-671 |
4.17e-10 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 4.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 507 GQITALLGHSGTGKSTLMNILCGLCPPSD--GFASIYGHRVSEidemfEARKMIGICPQLDIHFDVLTVEENL------- 577
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-----QILKRTGFVTQDDILYPHLTVRETLvfcsllr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 578 ---SILASIKGIPANNIIQEVQkvLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH-IV 653
Cdd:PLN03211 169 lpkSLTKQEKILVAESVISELG--LTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYrLV 246
|
170
....*....|....*...
gi 27262626 654 WNLLKYRKANRVTVFSTH 671
Cdd:PLN03211 247 LTLGSLAQKGKTIVTSMH 264
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1319-1476 |
4.23e-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: 4.23e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINIL-----VGDIEptsGQVFLGDYSSetseDDDSLKCMGYCPQINPLWPDTTLQE 1393
Cdd:cd03232 26 ISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRPL----DKNFQRSTGYVEQQDVHSPNLTVRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFEIYGAVKGMSASDmkevisrithaldlkehlqktvkklpagiKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:cd03232 99 ALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVR 149
|
...
gi 27262626 1474 AIR 1476
Cdd:cd03232 150 FLK 152
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1289-1550 |
4.48e-10 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 63.51 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1289 SIMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDysSETSE 1368
Cdd:PRK11000 3 SVTLRNVTKAYGDV-----------VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE--KRMND 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1369 DDDSLKCMGYCPQINPLWPDTTLQEHFEIygavkGM--SASDMKEVISRITHA---LDLKEHLQKTVKKLPAGIKRKLCF 1443
Cdd:PRK11000 70 VPPAERGVGMVFQSYALYPHLSVAENMSF-----GLklAGAKKEEINQRVNQVaevLQLAHLLDRKPKALSGGQRQRVAI 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1444 ALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL--- 1520
Cdd:PRK11000 145 GRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhy 224
|
250 260 270
....*....|....*....|....*....|....*...
gi 27262626 1521 -KSKFGKGY-------FLEIKlkdwIENLEVDRLQREI 1550
Cdd:PRK11000 225 pANRFVAGFigspkmnFLPVK----VTATAIEQVQVEL 258
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
1323-1510 |
4.50e-10 |
|
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: 60.28 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTsgqvflgdyssetsEDDDSlkcmgycpqinplWPDTTLqehfeiygAVK 1402
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPN--------------GDNDE-------------WDGITP--------VYK 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1403 GmsasdmkevisrithaldlkehlQKTvkKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNR 1482
Cdd:cd03222 67 P-----------------------QYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEG 121
|
170 180
....*....|....*....|....*...
gi 27262626 1483 KRAAILTTHYMEEAEAVCDRVaIMVSGQ 1510
Cdd:cd03222 122 KKTALVVEHDLAVLDYLSDRI-HVFEGE 148
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1319-1510 |
4.56e-10 |
|
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: 60.95 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGdyssetsedddslKCMGYCPQiNPLWPDTTLQEHFeIY 1398
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP-------------GSIAYVSQ-EPWIQNGTIRENI-LF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVkgMSASDMKEVIsritHALdlkeHLQKTVKKLPAGI---------------KRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:cd03250 89 GKP--FDEERYEKVI----KAC----ALEPDLEILPDGDlteigekginlsggqKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 1464 DPKAKQHMW-RAIRTAFKNrKRAAILTTHYMEEAEAvCDRVAIMVSGQ 1510
Cdd:cd03250 159 DAHVGRHIFeNCILGLLLN-NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
497-646 |
4.81e-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: 64.46 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmfEA-RKMIGICPQldihfDvlTVEE 575
Cdd:COG5265 374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ--ASlRAAIGIVPQ-----D--TVLF 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NLSIlasikgipANNII--------QEVQKV-----LLDLDMQTIKDNQAK------KLSGGQKRKLslGIA--VLGNPK 634
Cdd:COG5265 445 NDTI--------AYNIAygrpdaseEEVEAAaraaqIHDFIESLPDGYDTRvgerglKLSGGEKQRV--AIArtLLKNPP 514
|
170
....*....|..
gi 27262626 635 ILLLDEPTAGMD 646
Cdd:COG5265 515 ILIFDEATSALD 526
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1319-1491 |
4.84e-10 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 60.97 E-value: 4.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL--GDYSSETSEDDDSLKCMGYCPQINPLwpdTTLQEHFE 1396
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLngGPLDFQRDSIARGLLYLGHAPGIKTT---LSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 IYGAVKGMSAsdMKEVISRIthALDLKEHLqkTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIR 1476
Cdd:cd03231 96 FWHADHSDEQ--VEEALARV--GLNGFEDR--PVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169
|
170
....*....|....*
gi 27262626 1477 tAFKNRKRAAILTTH 1491
Cdd:cd03231 170 -GHCARGGMVVLTTH 183
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1319-1503 |
4.89e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 61.27 E-value: 4.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDT---TLQEHF 1395
Cdd:PRK10247 26 ISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTvydNLIFPW 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYGavkgmSASDMKEVISRITHaLDLKEH-LQKTVKKLPAGIKRKlcfaLSMLGN----PQITLLDEPSTGMDPKAKQH 1470
Cdd:PRK10247 106 QIRN-----QQPDPAIFLDDLER-FALPDTiLTKNIAELSGGEKQR----ISLIRNlqfmPKVLLLDEITSALDESNKHN 175
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 1471 MWRAIRTAFKNRKRAAILTTHYMEEAEAvCDRV 1503
Cdd:PRK10247 176 VNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1313-1526 |
6.19e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 61.64 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1313 KVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLK---------------CMG 1377
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG------KDVTKLPeykrakyigrvfqdpMMG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1378 YCpqinplwPDTTLQEHFEI-------YGAVKGMSASDMKEVISRITH-ALDLKEHLQKTVKKLPAGiKRKlcfALSML- 1448
Cdd:COG1101 93 TA-------PSMTIEENLALayrrgkrRGLRRGLTKKRRELFRELLATlGLGLENRLDTKVGLLSGG-QRQ---ALSLLm 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1449 ---GNPQITLLDEPSTGMDPK-AKQHMwRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVaIM---------VSGQLRCIG 1515
Cdd:COG1101 162 atlTKPKLLLLDEHTAALDPKtAALVL-ELTEKIVEENNLTTLMVTHNMEQALDYGNRL-IMmhegriildVSGEEKKKL 239
|
250
....*....|.
gi 27262626 1516 TVQHLKSKFGK 1526
Cdd:COG1101 240 TVEDLLELFEE 250
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
486-671 |
7.40e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 486 TYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQlD 565
Cdd:PRK11176 348 TFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY-TLASLRNQVALVSQ-N 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDVLTVEENL-----------SILASIKGIPANNIIQEVQKVLldldmQTIKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK11176 426 VHLFNDTIANNIayarteqysreQIEEAARMAYAMDFINKMDNGL-----DTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190
....*....|....*....|....*....|....*..
gi 27262626 635 ILLLDEPTAGMDPCSRHIVWNLLKYRKANRVTVFSTH 671
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
455-696 |
7.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 64.23 E-value: 7.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 455 VNGNISFSEIIEPVSSE----------FVGKEAIRISGIQKTYRKKGENvEALRNLSFDIYEGQITALLGHSGTGKSTLM 524
Cdd:PLN03232 582 VNANVSLQRIEELLLSEerilaqnpplQPGAPAISIKNGYFSWDSKTSK-PTLSDINLEIPVGSLVAIVGGTGEGKTSLI 660
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 525 NILCGLCPPSDgfasiyghrvseiDEMFEARKMIGICPQLDIHFDVlTVEENLSILASIKGIPANNIIqEVQKVLLDLDM 604
Cdd:PLN03232 661 SAMLGELSHAE-------------TSSVVIRGSVAYVPQVSWIFNA-TVRENILFGSDFESERYWRAI-DVTALQHDLDL 725
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 605 QTIKD-----NQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWN-LLKYRKANRVTVFST---HFMDe 675
Cdd:PLN03232 726 LPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDsCMKDELKGKTRVLVTnqlHFLP- 804
|
250 260
....*....|....*....|.
gi 27262626 676 adiLADRKAVISQGMLKCVGS 696
Cdd:PLN03232 805 ---LMDRIILVSEGMIKEEGT 822
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1290-1523 |
8.12e-10 |
|
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: 61.79 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKDFLLsrkvkkvatKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEpTSGQVFLGDYSSETSED 1369
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVL---------ENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWpDTTLQEHFEIYGA------VKGMSASDMKEVISRITHALDLKehLQKTVKKLPAGIKRKLCF 1443
Cdd:cd03289 73 QKWRKAFGVIPQKVFIF-SGTFRKNLDPYGKwsdeeiWKVAEEVGLKSVIEQFPGQLDFV--LVDGGCVLSHGHKQLMCL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1444 ALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNrkRAAILTTHYMeEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:cd03289 150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNE 226
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
492-696 |
9.74e-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: 59.85 E-value: 9.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 492 ENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlCP---PSDGfaSIY--GHRVSEIdEMFE-ARKMIGICPQLD 565
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEG--EILfkGEDITDL-PPEErARLGIFLAFQYP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDVLTVEEnlsilasikgipanniiqevqkVLLDLDMqtikdnqakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGM 645
Cdd:cd03217 87 PEIPGVKNAD----------------------FLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 646 DPCSRHIVWNLL-KYRKANRVTVFSTHFMDEAD-ILADRKAVISQGMLKCVGS 696
Cdd:cd03217 136 DIDALRLVAEVInKLREEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1288-1558 |
1.11e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 61.21 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1288 PSIMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTII------NILVGDIEpTSGQV-FLG 1360
Cdd:PRK14258 6 PAIKVNNLSFYYDTQK-----------ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVR-VEGRVeFFN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1361 DYSSETSEDDDSLK---CMGYC-PQINPLWPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALD-LKEHLQKTVKKLPA 1435
Cdd:PRK14258 74 QNIYERRVNLNRLRrqvSMVHPkPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDeIKHKIHKSALDLSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1436 GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCig 1515
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENRI-- 231
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 27262626 1516 tvqhlkskfgkGYFLEIKLKDWIENLEVDRLQREiqYIFPNAS 1558
Cdd:PRK14258 232 -----------GQLVEFGLTKKIFNSPHDSRTRE--YVLSRLG 261
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1319-1491 |
1.15e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYS--SETSEDDDSLKCMGYCPQINplwPDTTLQEH-- 1394
Cdd:PRK13540 20 ISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSikKDLCTYQKQLCFVGHRSGIN---PYLTLRENcl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 FEIYGAVKGMSASDMKEVISrITHALDLKEHLqktvkkLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRA 1474
Cdd:PRK13540 97 YDIHFSPGAVGITELCRLFS-LEHLIDYPCGL------LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITK 169
|
170
....*....|....*..
gi 27262626 1475 IRtAFKNRKRAAILTTH 1491
Cdd:PRK13540 170 IQ-EHRAKGGAVLLTSH 185
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1319-1499 |
1.35e-09 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 59.80 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEP---TSGQVFLGDyssetsEDDDSL----KCMGYCPQINPLWPdttl 1391
Cdd:COG4136 20 LSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNG------RRLTALpaeqRRIGILFQDDLLFP---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 qeHFEI-----YGAVKGMSASDMKEvisRITHALD---LKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:COG4136 90 --HLSVgenlaFALPPTIGRAQRRA---RVEQALEeagLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKL 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 27262626 1464 DPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAV 1499
Cdd:COG4136 165 DAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAA 200
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1313-1525 |
1.35e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 62.94 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1313 KVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIePTSGQVFLGDYSSETSEDDDSLKCMGYCPQiNPLWPDTTLQ 1392
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQ-NPQLPHGTLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEiygavkgMSASDMKEviSRITHALDlKEHLQKTVKKLPAGIK---------------RKLCFALSMLGNPQITLLD 1457
Cdd:PRK11174 441 DNVL-------LGNPDASD--EQLQQALE-NAWVSEFLPLLPQGLDtpigdqaaglsvgqaQRLALARALLQPCQLLLLD 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1458 EPSTGMDPKAKQHMWRAIRTAfkNRKRAAILTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:PRK11174 511 EPTASLDAHSEQLVMQALNAA--SRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGG 575
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
478-683 |
1.53e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 60.86 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYR-----KKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEmf 552
Cdd:PRK10419 4 LNVSGLSHHYAhgglsGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNR-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 553 EARKMIgicpQLDIHfdvLTVEENLSILASIKGIPAnnIIQEVQKVLLDLDMQ-----------------TIKDNQAKKL 615
Cdd:PRK10419 82 AQRKAF----RRDIQ---MVFQDSISAVNPRKTVRE--IIREPLRHLLSLDKAerlarasemlravdlddSVLDKRPPQL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLKYRKANRVT--VFSTH-------------FMDEADILA 680
Cdd:PRK10419 153 SGGQLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHdlrlverfcqrvmVMDNGQIVE 232
|
...
gi 27262626 681 DRK 683
Cdd:PRK10419 233 TQP 235
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
467-653 |
1.81e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.94 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 467 PVSSEFVGKEAIRISGIQKTYRKKgenVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS---DGFASIYGH 543
Cdd:PLN03140 154 PNAARNIAESALGMLGINLAKKTK---LTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGY 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 544 RVSEidemFEARKMIGICPQLDIHFDVLTVEENLSILASIKGIPA----------------------------------- 588
Cdd:PLN03140 231 RLNE----FVPRKTSAYISQNDVHVGVMTVKETLDFSARCQGVGTrydllselarrekdagifpeaevdlfmkatamegv 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 589 -NNIIQEVQKVLLDLDM---QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP--------CSRHIV 653
Cdd:PLN03140 307 kSSLITDYTLKILGLDIckdTIVGDEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSsttyqivkCLQQIV 383
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1312-1511 |
1.82e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.58 E-value: 1.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTI---IN-ILVGDIEPTSGQVFLGDYSSETSEDDDSLKcMGYCPQiNP--L 1385
Cdd:PRK13640 19 KKPALNDISFSIPRGSWTALIGHNGSGKSTIsklINgLLLPDDNPNSKITVDGITLTAKTVWDIREK-VGIVFQ-NPdnQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1386 WPDTTLQEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDP 1465
Cdd:PRK13640 97 FVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDP 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 1466 KAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEaVCDRVAIMVSGQL 1511
Cdd:PRK13640 177 AGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKL 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1319-1506 |
2.09e-09 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 59.76 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFlgdYSSE-------TSEDDDSL----KCMGYCPQ------ 1381
Cdd:COG4778 30 VSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSIL---VRHDggwvdlaQASPREILalrrRTIGYVSQflrvip 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1382 --------INPLwpdttlqehfeiygAVKGMSASDMKEVISRITHALDLKEHLQKTVkklPA----GIKRKLCFALSMLG 1449
Cdd:COG4778 107 rvsaldvvAEPL--------------LERGVDREEARARARELLARLNLPERLWDLP---PAtfsgGEQQRVNIARGFIA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIRTAfKNRKRAAILTTHYMEEAEAVCDRVAIM 1506
Cdd:COG4778 170 DPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1319-1511 |
2.62e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYcpqinplwpdttLQEHFEI 1397
Cdd:PRK10762 271 VSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVY------------ISEDRKR 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 YGAVKGMSasdMKEVIS------------RITHAldlKEHL----------------QKTVKKLPAGIKRKLCFALSMLG 1449
Cdd:PRK10762 339 DGLVLGMS---VKENMSltalryfsraggSLKHA---DEQQavsdfirlfniktpsmEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1450 NPQITLLDEPSTGMDPKAKQHMWRAIrTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1285-1540 |
3.24e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 3.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1285 EEKPSIMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVG--DIEPTSGQVFLGDy 1362
Cdd:CHL00131 3 KNKPILEIKNLHASVNENE-----------ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKG- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1363 SSETSEDDDSLKCMG------YCPQInplwPDTTLQEHFEI-YGAV-KGMSASDMK-----EVISRITHALDLKEH-LQK 1428
Cdd:CHL00131 71 ESILDLEPEERAHLGiflafqYPIEI----PGVSNADFLRLaYNSKrKFQGLPELDpleflEIINEKLKLVGMDPSfLSR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1429 TVKKLPAGIKRKLCFALSM-LGNPQITLLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVC-DRVAIM 1506
Cdd:CHL00131 147 NVNEGFSGGEKKRNEILQMaLLDSELAILDETDSGLDIDALKIIAEGINK-LMTSENSIILITHYQRLLDYIKpDYVHVM 225
|
250 260 270
....*....|....*....|....*....|....
gi 27262626 1507 VSGQLRCIGTVQHLKSkfgkgyfLEIKLKDWIEN 1540
Cdd:CHL00131 226 QNGKIIKTGDAELAKE-------LEKKGYDWLKQ 252
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
488-646 |
3.51e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 488 RKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcpPSDGFA-------SIYGHRVSEIDEMFeaRKMIGI 560
Cdd:TIGR00956 68 FRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHigvegviTYDGITPEEIKKHY--RGDVVY 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 561 CPQLDIHFDVLTVEENLSILASIKGiPANNII----QEVQKVLLDLDMQT----------IKDNQAKKLSGGQKRKLSLG 626
Cdd:TIGR00956 143 NAETDVHFPHLTVGETLDFAARCKT-PQNRPDgvsrEEYAKHIADVYMATyglshtrntkVGNDFVRGVSGGERKRVSIA 221
|
170 180
....*....|....*....|
gi 27262626 627 IAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLD 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
497-646 |
4.24e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 4.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLC---------------------PPSDGFASIYGHrVSE-IDEMFEA 554
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVllddgriiyeqdlivarlqqdPPRNVEGTVYDF-VAEgIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGicpqlDIHFDVLT--VEENLSILASIKGIPAN-------NIIQEVQKvLLDLDmqtiKDNQAKKLSGGQKRKLSL 625
Cdd:PRK11147 98 LKRYH-----DISHLVETdpSEKNLNELAKLQEQLDHhnlwqleNRINEVLA-QLGLD----PDAALSSLSGGWLRKAAL 167
|
170 180
....*....|....*....|.
gi 27262626 626 GIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK11147 168 GRALVSNPDVLLLDEPTNHLD 188
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1328-1515 |
4.78e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.25 E-value: 4.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1328 ILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG----DYSSEtsedddslKCMGYCPQINPLWPDTTLQEHF-----EIY 1398
Cdd:PRK13638 29 VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkplDYSKR--------GLLALRQQVATVFQDPEQQIFYtdidsDIA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GAVKGMSASDmKEVISRITHAL---DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAI 1475
Cdd:PRK13638 101 FSLRNLGVPE-AEITRRVDEALtlvDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAII 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 1476 RTAFKNRKRaAILTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK13638 180 RRIVAQGNH-VIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1317-1511 |
5.55e-09 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 58.25 E-value: 5.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-----GDYSSETSEDDDSLkcMGYCPQINPlwpdTTL 1391
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdgkpiSQYEHKYLHSKVSL--VGQEPVLFA----RSL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEiYGaVKGMSASDMKEVISRiTHALDLKEHLQKTVK--------KLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:cd03248 105 QDNIA-YG-LQSCSFECVKEAAQK-AHAHSFISELASGYDtevgekgsQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 27262626 1464 DPKAKQHMWRAIRTAfkNRKRAAILTTHYMEEAEAVcDRVAIMVSGQL 1511
Cdd:cd03248 182 DAESEQQVQQALYDW--PERRTVLVIAHRLSTVERA-DQILVLDGGRI 226
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
497-681 |
5.71e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 58.05 E-value: 5.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG--LCPPSDGFASIyghrvseidemfearkmigicpqLDIHFDvltve 574
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDV-----------------------PDNQFG----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 575 ENLSIlasIKGIPANNIIQEVQKVlldLDMQTIKDNQA-----KKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-C 648
Cdd:COG2401 98 REASL---IDAIGRKGDFKDAVEL---LNAVGLSDAVLwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRqT 171
|
170 180 190
....*....|....*....|....*....|....
gi 27262626 649 SRHIVWNLLKY-RKANRVTVFSTHfmdEADILAD 681
Cdd:COG2401 172 AKRVARNLQKLaRRAGITLVVATH---HYDVIDD 202
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1319-1476 |
6.38e-09 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 58.35 E-value: 6.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQ-VFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFei 1397
Cdd:PRK11614 24 VSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRiVFDGKDITDWQTAKIMREAVAIVPEGRRVFSRMTVEENL-- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 ygAVKGMSAsDMKEVISRITHALDLKEHLQ----KTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:PRK11614 102 --AMGGFFA-ERDQFQERIKWVYELFPRLHerriQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD 178
|
...
gi 27262626 1474 AIR 1476
Cdd:PRK11614 179 TIE 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1308-1512 |
6.94e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.22 E-value: 6.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1308 SRKVKKVATkyISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPT-SGQVFLGDYSSETSEDDDSLK---CMgyCPQin 1383
Cdd:TIGR02633 270 NPHRKRVDD--VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRagiAM--VPE-- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1384 plwpDTTLQEHFEIYGAVKGMSASDMKEV--ISRITHALDLK---EHLQK----------TVKKLPAGIKRKLCFALSML 1448
Cdd:TIGR02633 344 ----DRKRHGIVPILGVGKNITLSVLKSFcfKMRIDAAAELQiigSAIQRlkvktaspflPIGRLSGGNQQKAVLAKMLL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1449 GNPQITLLDEPSTGMDPKAKQHMWRAIrTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:TIGR02633 420 TNPRVLILDEPTRGVDVGAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1328-1522 |
1.07e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.18 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1328 ILGLLGPNGAGKSTIINILVGDIEPTSG-----QVFLGDYSSETSEDD-DSLKCMGYCPQINPLWPDTTLQEHFEIYGAV 1401
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1402 KGMSASDMKEVI-SRITHA---LDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRT 1477
Cdd:PRK14271 129 KLVPRKEFRGVAqARLTEVglwDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRS 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 27262626 1478 AFKnrKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:PRK14271 209 LAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1319-1533 |
1.14e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 58.22 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYS-SETSEDDD---SLKCMGYCPQI--NPLWPDTTLQ 1392
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLiTSTSKNKDikqIRKKVGLVFQFpeSQLFEETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 ------EHFeiygavkGMSASDMKEVISRITHALDLKEHL-QKTVKKLPAGIKRKLCFA--LSMlgNPQITLLDEPSTGM 1463
Cdd:PRK13649 106 dvafgpQNF-------GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAgiLAM--EPKILVLDEPTAGL 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1464 DPKAKqhmwRAIRTAFKNRKRAA---ILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVqhlKSKFGKGYFLEIK 1533
Cdd:PRK13649 177 DPKGR----KELMTLFKKLHQSGmtiVLVTHLMDDVANYADFVYVLEKGKLVLSGKP---KDIFQDVDFLEEK 242
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
494-689 |
1.22e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 1.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRV--SEIDEMfEARKMIGICPQLDIHFDVL 571
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDER-LIRQEAGMVFQQFYLFPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 TVEENLSI-LASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSR 650
Cdd:PRK09493 93 TALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELR 172
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 651 HIVWNLLKYRKANRVT-VFSTHFMDEADILADRKAVISQG 689
Cdd:PRK09493 173 HEVLKVMQDLAEEGMTmVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1319-1511 |
1.44e-08 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 57.41 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTI---INILVgdiEPTSGQVFLGDYSSETSEDDDSL--KCMGYCPQINPLWPDTTLQE 1393
Cdd:PRK09493 20 IDLNIDQGEVVVIIGPSGSGKSTLlrcINKLE---EITSGDLIVDGLKVNDPKVDERLirQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFeIYGA--VKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:PRK09493 97 NV-MFGPlrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 1472 WRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK09493 176 LKVMQD-LAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1290-1464 |
1.51e-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: 59.18 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGdyssetsed 1369
Cdd:TIGR03719 323 IEAENLTKAFGDK-----------LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 dDSLKcMGYCPQI-NPLWPDTTLQEhfEIYGAVKGMSASDmKEVISR-ITHALDLK-EHLQKTVKKLPAGIKRKLCFALS 1446
Cdd:TIGR03719 383 -ETVK-LAYVDQSrDALDPNKTVWE--EISGGLDIIKLGK-REIPSRaYVGRFNFKgSDQQKKVGQLSGGERNRVHLAKT 457
|
170
....*....|....*...
gi 27262626 1447 MLGNPQITLLDEPSTGMD 1464
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLD 475
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
479-689 |
1.60e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 57.63 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 479 RISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASiYGHR---VSEIDEMFEA- 554
Cdd:PRK11701 8 SVRGLTKLY----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVH-YRMRdgqLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGicpQLDIHFdvltVEEN--------LSILASI----KGIPAN---NIIQE----VQKVLLDLDmqTIkDNQAKKL 615
Cdd:PRK11701 83 RRRLL---RTEWGF----VHQHprdglrmqVSAGGNIgerlMAVGARhygDIRATagdwLERVEIDAA--RI-DDLPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 616 SGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADILADRKAVISQG 689
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRglVRELGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1290-1511 |
1.84e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 57.29 E-value: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKKdfllsrkvkkvATKYISFCVKKGEILGLLGPNGAGKSTI---INILVgdiEPTSGQVFL-GDYSSE 1365
Cdd:PRK10619 6 LNVIDLHKRYGEHE-----------VLKGVSLQANAGDVISIIGSSGSGKSTFlrcINFLE---KPSEGSIVVnGQTINL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1366 TSEDDDSLKC------------MGYCPQINPLWPDTTLQEH-FEIYGAVKGMSASDMKEVISRITHALDLKEHLQ-KTVK 1431
Cdd:PRK10619 72 VRDKDGQLKVadknqlrllrtrLTMVFQHFNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1432 KLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRaIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK10619 152 HLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1319-1494 |
2.37e-08 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.15 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVgDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQ------------INPL- 1385
Cdd:TIGR01271 1238 LSFSVEGGQRVGLLGRTGSGKSTLLSALL-RLLSTEGEIQIDGVSWNSVTLQTWRKAFGVIPQkvfifsgtfrknLDPYe 1316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1386 -WPDTTLQEHFEIYGavkgmsasdMKEVISRITHALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:TIGR01271 1317 qWSDEEIWKVAEEVG---------LKSVIEQFPDKLDFV--LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLD 1385
|
170 180 190
....*....|....*....|....*....|
gi 27262626 1465 PKAKQHMWRAIRTAFKNrkRAAILTTHYME 1494
Cdd:TIGR01271 1386 PVTLQIIRKTLKQSFSN--CTVILSEHRVE 1413
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
441-646 |
2.46e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.79 E-value: 2.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 441 SKSK---RNYEELSEGNVNGNISFSEIIEPVSsEFVGKEAIRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSG 517
Cdd:TIGR03719 284 AKSKarlARYEELLSQEFQKRNETAEIYIPPG-PRLGDKVIEAENLTKAF---GDKL-LIDDLSFKLPPGGIVGVIGPNG 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 518 TGKSTLMNILCGLCPPSDGFASIyGHRV--SEIDEMFEArkmigicpqLDihfdvltveenlsilasikgiPANNIIQEV 595
Cdd:TIGR03719 359 AGKSTLFRMITGQEQPDSGTIEI-GETVklAYVDQSRDA---------LD---------------------PNKTVWEEI 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 596 QKVLLDLDMQTIKDN--------------QAKK---LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 408 SGGLDIIKLGKREIPsrayvgrfnfkgsdQQKKvgqLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
483-646 |
2.57e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.92 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 483 IQKTYRKKGENVE-------ALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR 555
Cdd:PRK10253 2 TESVARLRGEQLTlgygkytVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 556 KmIGICPQLDIHFDVLTVEEnlsiLASIKGIPANNII--------QEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGI 627
Cdd:PRK10253 82 R-IGLLAQNATTPGDITVQE----LVARGRYPHQPLFtrwrkedeEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAM 156
|
170
....*....|....*....
gi 27262626 628 AVLGNPKILLLDEPTAGMD 646
Cdd:PRK10253 157 VLAQETAIMLLDEPTTWLD 175
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1313-1511 |
3.47e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.59 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1313 KVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTTLQ 1392
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEIYGAV----KGMSASDMKEVISRITHAL-------DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPST 1461
Cdd:PRK14246 103 PHLSIYDNIayplKSHGIKEKREIKKIVEECLrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 1462 GMDPKAKQHMWRAIrTAFKNrKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK14246 183 MIDIVNSQAIEKLI-TELKN-EIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1326-1467 |
3.74e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 58.35 E-value: 3.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1326 GEILGLLGPNGAGKSTIINILVGDIEPTS--GQVFLGDYSSETSedddSLKCMGYCPQINPLWPDTTLQEHFeIYGAVKG 1403
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQ----ILKRTGFVTQDDILYPHLTVRETL-VFCSLLR 168
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1404 MSASDMKEVISRITHALDLKEHLQKT---------VKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKA 1467
Cdd:PLN03211 169 LPKSLTKQEKILVAESVISELGLTKCentiignsfIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATA 241
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1317-1509 |
3.98e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.75 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGY-CPQINPLWPDTTLQEHF 1395
Cdd:PRK15439 28 KGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYlVPQEPLLFPNLSVKENI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 eIYGAVKGM-SASDMKEVISRITHALDLkehlqktvkKLPAG-----------IKRKLcfalsmLGNPQITLLDEPSTGM 1463
Cdd:PRK15439 108 -LFGLPKRQaSMQKMKQLLAALGCQLDL---------DSSAGslevadrqiveILRGL------MRDSRILILDEPTASL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 1464 DPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSG 1509
Cdd:PRK15439 172 TPAETERLFSRIR-ELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
487-694 |
4.43e-08 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 57.79 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 487 YRKKGENVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILCGLCPPsdgfASIYghrvseidemfearkmigicPQLD 565
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSP----PVVY--------------------PSGD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHF---DVLTVEEnlsilASIKGIPANN---IIQE----------VQKVLLD--------------------LDMQTIKd 609
Cdd:PRK15134 71 IRFhgeSLLHASE-----QTLRGVRGNKiamIFQEpmvslnplhtLEKQLYEvlslhrgmrreaargeilncLDRVGIR- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 610 nQAKK--------LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNLLK--YRKANRVTVFSTHFMDEADIL 679
Cdd:PRK15134 145 -QAAKrltdyphqLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKL 223
|
250
....*....|....*
gi 27262626 680 ADRKAVISQGmlKCV 694
Cdd:PRK15134 224 ADRVAVMQNG--RCV 236
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1290-1511 |
4.66e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 56.63 E-value: 4.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdflLSRKVKkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgDYSSETSED 1369
Cdd:PRK13651 3 IKVKNIVKIFNKK----LPTELK--ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTI---EWIFKDEKN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKcmgycpQINPLWPDTTLQ--------------------------EHFE-------IYGAVK-GMSASDMKEVISR 1415
Cdd:PRK13651 74 KKKTK------EKEKVLEKLVIQktrfkkikkikeirrrvgvvfqfaeyQLFEqtiekdiIFGPVSmGVSKEEAKKRAAK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1416 ITHALDLKE-HLQKTVKKLPAGIKRKLCFA--LSMlgNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKrAAILTTHY 1492
Cdd:PRK13651 148 YIELVGLDEsYLQRSPFELSGGQKRRVALAgiLAM--EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHD 224
|
250
....*....|....*....
gi 27262626 1493 MEEAEAVCDRVAIMVSGQL 1511
Cdd:PRK13651 225 LDNVLEWTKRTIFFKDGKI 243
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
499-692 |
4.86e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.63 E-value: 4.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFDIYEGQITALLGHSGTGKSTLMNILCGLCP-PSDGFASIYGHRVS----------EIDEMFEARKMIGICPQLDih 567
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKirnpqqaiaqGIAMVPEDRKRDGIVPVMG-- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 fdvltVEENLSiLASIKGIPANNIIQE------VQKVLLDLDMQTIKDNQA-KKLSGGQKRKLSLGIAVLGNPKILLLDE 640
Cdd:PRK13549 358 -----VGKNIT-LAALDRFTGGSRIDDaaelktILESIQRLKVKTASPELAiARLSGGNQQKAVLAKCLLLNPKILILDE 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 641 PTAGMDPCSRHIVWNLLkYRKANR---VTVFSTHfMDEADILADRKAVISQGMLK 692
Cdd:PRK13549 432 PTRGIDVGAKYEIYKLI-NQLVQQgvaIIVISSE-LPEVLGLSDRVLVMHEGKLK 484
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
943-1224 |
5.55e-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: 56.63 E-value: 5.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 943 NDSDYVSVAPHSAALNVMHSEKDYVFAAVFNSTMVYSLPILVNIISNYYLYHLNVTETIQIWSTPFFQEITDIVFkielY 1022
Cdd:pfam12698 87 KGFSKDLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAY----Y 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1023 FQAALLGIIVTAMPPYFAMENAENHKIKAYTQLKLSGLLPSAYWIGQAVVDIPLFFIILILMLgsLLAFHYGLYFYTvkF 1102
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL--LLLFGIGIPFGN--L 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1103 LAVVFCLIGYVPSVILFTYIASFTFKKILNTKEFWSFIYSVAALACIAIteitfFMGYTIATILHYAFCiIIPIYPLlgc 1182
Cdd:pfam12698 239 GLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGL-----FPLEDPPSFLQWIFS-IIPFFSP--- 309
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 27262626 1183 LISFIKISwknvrknvdTYNPWDRLSVAVISPYLQCVLWIFL 1224
Cdd:pfam12698 310 IDGLLRLI---------YGDSLWEIAPSLIILLLFAVVLLLL 342
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
494-657 |
5.58e-08 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 56.51 E-value: 5.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEA--RKMIGICPQ-----LDI 566
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKllRQKIQIVFQnpygsLNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 567 HFDV-LTVEENLSILASIkgipanNIIQEVQKVLLDLDMQTIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLDEP 641
Cdd:PRK11308 108 RKKVgQILEEPLLINTSL------SAAERREKALAMMAKVGLRPEHYDRyphmFSGGQRQRIAIARALMLDPDVVVADEP 181
|
170
....*....|....*.
gi 27262626 642 TAGMDPCSRHIVWNLL 657
Cdd:PRK11308 182 VSALDVSVQAQVLNLM 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
480-646 |
5.80e-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: 57.64 E-value: 5.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 480 ISGIQKTYrkkGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKMIG 559
Cdd:TIGR03719 7 MNRVSKVV---PPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG----------------EARPQPG 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 560 IC-------PQLDihfDVLTVEENLSI-LASIKgipanNIIQEVQKVLL-----DLDMQTIKDNQAK------------- 613
Cdd:TIGR03719 68 IKvgylpqePQLD---PTKTVRENVEEgVAEIK-----DALDRFNEISAkyaepDADFDKLAAEQAElqeiidaadawdl 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 614 ---------------------KLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR03719 140 dsqleiamdalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1290-1361 |
6.59e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 6.59e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1290 IMVSNLHKEYDDKkdfLLsrkvkkvaTKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD 1361
Cdd:PRK11819 325 IEAENLSKSFGDR---LL--------IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1314-1504 |
6.60e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 55.56 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1314 VATKYISFCVKKGEILGLLGPNGAGKSTIINIL--VGDIEPT---SGQVFLGDYSSetsedddslkcmgYCPQINPLWPD 1388
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFnrLNDLIPGfrvEGKVTFHGKNL-------------YAPDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1389 TTLQEHFE-------------IYGA-VKGMSAsDMKEVISRITH--AL--DLKEHLQKTVKKLPAGIKRKLCFALSMLGN 1450
Cdd:PRK14243 91 RRIGMVFQkpnpfpksiydniAYGArINGYKG-DMDELVERSLRqaALwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQ 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1451 PQITLLDEPSTGMDPKAKqhmwRAIRTAFKNRKR--AAILTTHYMEEAEAVCDRVA 1504
Cdd:PRK14243 170 PEVILMDEPCSALDPIST----LRIEELMHELKEqyTIIIVTHNMQQAARVSDMTA 221
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1290-1518 |
6.88e-08 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.47 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1290 IMVSNLHKEYDDKkdfllsrkvkkVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSED 1369
Cdd:COG4604 2 IEIKNVSKRYGGK-----------VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1370 DDSLKCMGYCPQINPLWPDTTLQE--HFEIYGAVKG-MSASDmKEVISRITHALDLKEHLQKTVKKLPAGiKRKLCF-AL 1445
Cdd:COG4604 71 RELAKRLAILRQENHINSRLTVRElvAFGRFPYSKGrLTAED-REIIDEAIAYLDLEDLADRYLDELSGG-QRQRAFiAM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1446 SMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQ 1518
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPE 221
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
493-691 |
7.28e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 7.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSE------IDEMF----EARKMIGICP 562
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINHGFalvtEERRSTGIYA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 563 QLDIHFDvltveenlSILASIK------GIPANNIIQ-EVQKVLLDLDMQT-IKDNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK10982 340 YLDIGFN--------SLISNIRnyknkvGLLDNSRMKsDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 635 ILLLDEPTAGMDPCSRHIVWNL-LKYRKANRVTVFSTHFMDEADILADRKAVISQGML 691
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLiAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1315-1557 |
8.31e-08 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 55.40 E-value: 8.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTII----NILVGDIEPTSGQVFLGDY---SSETSED-DDSLKCMGYCPQINPLW 1386
Cdd:PRK09984 19 ALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSAGSHIELLGRTvqrEGRLARDiRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1387 PDTTLQEHFEIyGA----------VKGMSASDMKEVISRITHaLDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLL 1456
Cdd:PRK09984 99 NRLSVLENVLI-GAlgstpfwrtcFSWFTREQKQRALQALTR-VGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1457 DEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLkskfgkgyfleiklkd 1536
Cdd:PRK09984 177 DEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF---------------- 240
|
250 260
....*....|....*....|.
gi 27262626 1537 wiENLEVDRLQREIQYIFPNA 1557
Cdd:PRK09984 241 --DNERFDHLYRSINRVEENA 259
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
478-642 |
8.72e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 8.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSeidemFEARKM 557
Cdd:PRK10762 5 LQLKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVT-----FNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 558 -----IGIcpqldIHFDV-----LTVEENL----SILASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKL 623
Cdd:PRK10762 76 sqeagIGI-----IHQELnlipqLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMV 150
|
170
....*....|....*....
gi 27262626 624 SLGIAVLGNPKILLLDEPT 642
Cdd:PRK10762 151 EIAKVLSFESKVIIMDEPT 169
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1308-1508 |
9.28e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.58 E-value: 9.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1308 SRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIE--PTSGQVFLGDyssetsedddslkcmgycpqiNPL 1385
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPD---------------------NQF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1386 WPDTTLQEHFEIYGAVKgmsasDMKEVISRI---THALdlkehLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:COG2401 97 GREASLIDAIGRKGDFK-----DAVELLNAVglsDAVL-----WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 27262626 1463 MDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVS 1508
Cdd:COG2401 167 LDRQTAKRVARNLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1292-1526 |
9.64e-08 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 55.08 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYddKKDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF-----LGDYSSET 1366
Cdd:PRK10419 6 VSGLSHHY--AHGGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSwrgepLAKLNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1367 SEDDDSLKCMGYCPQINPLWPDTTLQEHF-EIYGAVKGMSASDMKEVISRITHALDLK-EHLQKTVKKLPAGIKRKLCFA 1444
Cdd:PRK10419 84 RKAFRRDIQMVFQDSISAVNPRKTVREIIrEPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1445 LSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL---RCIGTVQHLK 1521
Cdd:PRK10419 164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIvetQPVGDKLTFS 243
|
....*
gi 27262626 1522 SKFGK 1526
Cdd:PRK10419 244 SPAGR 248
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1324-1491 |
9.67e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 57.16 E-value: 9.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1324 KKGEILGLLGPNGAGKSTIINILVGdiEPTSGQVfLGDY--SSETSEDDDSLKCMGYCPQINPLWPDTTLQEHFeIYGAV 1401
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI-EGDIriSGFPKKQETFARISGYCEQNDIHSPQVTVRESL-IYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1402 ----KGMSASDMKEVISRITHALDLkEHLQKTVKKLPaGI-------KRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:PLN03140 980 lrlpKEVSKEEKMMFVDEVMELVEL-DNLKDAIVGLP-GVtglsteqRKRLTIAVELVANPSIIFMDEPTSGLDARAAAI 1057
|
170 180
....*....|....*....|.
gi 27262626 1471 MWRAIRTAFkNRKRAAILTTH 1491
Cdd:PLN03140 1058 VMRTVRNTV-DTGRTVVCTIH 1077
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1317-1525 |
1.03e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 57.04 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSEDDDSL-KCMGYCPQINPLWPDT------ 1389
Cdd:TIGR00958 498 KGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLL-DGVPLVQYDHHYLhRQVALVGQEPVLFSGSvrenia 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1390 ---TLQEHFEIYGAVKGMSASDMkevISRITHALD--LKEHLQktvkKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:TIGR00958 577 yglTDTPDEEIMAAAKAANAHDF---IMEFPNGYDteVGEKGS----QLSGGQKQRIAIARALVRKPRVLILDEATSALD 649
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1465 PKAKQhmwrAIRTAFKNRKRAAILTTHYMEEAEAvCDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:TIGR00958 650 AECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1320-1525 |
1.15e-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: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1320 SFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDyssetsEDDDSLKC------MGYCPQiNPLWPDTTLQE 1393
Cdd:cd03249 23 SLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG------VDIRDLNLrwlrsqIGLVSQ-EPVLFDGTIAE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1394 HFEiYGAVKGmsasDMKEVISRITHA------LDLKEHLQKTV----KKLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:cd03249 96 NIR-YGKPDA----TDEEVEEAAKKAnihdfiMSLPDGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1464 DPKAKQHMWRAIRTAFKNRKRAAI---LTThymeeaeaV--CDRVAIMVSGQLRCIGTVQHLKSKFG 1525
Cdd:cd03249 171 DAESEKLVQEALDRAMKGRTTIVIahrLST--------IrnADLIAVLQNGQVVEQGTHDELMAQKG 229
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
1319-1464 |
1.41e-07 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 54.46 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGdIEPTSGQVFL-----GDYSSEtsedddSLKCM-GYCPQINPLWPDTTLQ 1392
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLngrplSDWSAA------ELARHrAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1393 EHFEIYGAVKGMSASDmKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSML-----GNP--QITLLDEPSTGMD 1464
Cdd:COG4138 88 QYLALHQPAGASSEAV-EQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMNSLD 165
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
491-677 |
1.44e-07 |
|
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: 53.87 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 491 GENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIYGHRVSEIDEMFEA-----RKMIGICPQLD 565
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEG--KVHWSNKNESEPSFEAtrsrnRYSVAYAAQKP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDVlTVEENLSIlasikGIPANN----IIQEVQKVLLDLDM-----QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKIL 636
Cdd:cd03290 89 WLLNA-TVEENITF-----GSPFNKqrykAVTDACSLQPDIDLlpfgdQTEIGERGINLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27262626 637 LLDEPTAGMD-PCSRHIVW-NLLKY-RKANRVTVFSTH---FMDEAD 677
Cdd:cd03290 163 FLDDPFSALDiHLSDHLMQeGILKFlQDDKRTLVLVTHklqYLPHAD 209
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1319-1510 |
1.57e-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: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGdIEPTsgqvflGDYSSETSEDDDSLKCMGY----------CPQINPLWPD 1388
Cdd:TIGR02633 20 IDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPH------GTWDGEIYWSGSPLKASNIrdteragiviIHQELTLVPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1389 TTLQEHF----EIYGAVKGMSASDMKEVISRITHALDLKE-HLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGM 1463
Cdd:TIGR02633 93 LSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDAdNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 27262626 1464 DPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:TIGR02633 173 TEKETEILLDIIRD-LKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
497-696 |
2.48e-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: 56.11 E-value: 2.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQLD-IHFDvlTVEE 575
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS--------------VAYVPQQAwIQND--SLRE 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 576 NLSILASIKGiPANNIIQEVQKVLLDLDM-----QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP-CS 649
Cdd:TIGR00957 718 NILFGKALNE-KYYQQVLEACALLPDLEIlpsgdRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAhVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 650 RHIVWNLL--KYRKANRVTVFSTH---FMDEADILadrkAVISQGMLKCVGS 696
Cdd:TIGR00957 797 KHIFEHVIgpEGVLKNKTRILVTHgisYLPQVDVI----IVMSGGKISEMGS 844
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1329-1467 |
2.55e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 2.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1329 LGLLGPNGAGKSTIINILVGDIEPTSGQVF------LGDYSSETSED-DDSLKCMGYCPQINPLWPDTTLQEHFEIYGav 1401
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGTVFrsakvrMAVFSQHHVDGlDLSSNPLLYMMRCFPGVPEQKLRAHLGSFG-- 615
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1402 kgmsasdmkevisrITHALDLkehlqKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKA 1467
Cdd:PLN03073 616 --------------VTGNLAL-----QPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA 662
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1292-1363 |
2.77e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 54.03 E-value: 2.77e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1292 VSNLHKEYDDKKDFLLSRKVKkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFL-------GDYS 1363
Cdd:PRK15112 7 VRNLSKTFRYRTGWFRRQTVE--AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfGDYS 83
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1315-1464 |
2.90e-07 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 53.34 E-value: 2.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSEDDDSL-KCMGYCPQINPLWPDTTL 1391
Cdd:PRK10908 17 ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSghDITRLKNREVPFLrRQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 1392 QEHFEIYGAVKGMSASDMKEvisRITHALDlKEHLQKTVKKLP----AGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRR---RVSAALD-KVGLLDKAKNFPiqlsGGEQQRVGIARAVVNKPAVLLADEPTGNLD 169
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1319-1464 |
3.32e-07 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 53.40 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGdIEPTSGQVFLGDYSSETSEDDDSLKCMGY-CPQINPLWPDTTLQeHFEI 1397
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYlSQQQTPPFAMPVFQ-YLTL 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1398 YGAVKGMSASDMKeVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSML-----GNP--QITLLDEPSTGMD 1464
Cdd:PRK03695 93 HQPDKTRTEAVAS-ALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNSLD 165
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1323-1510 |
3.67e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 54.74 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1323 VKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLG---DYSS--ETSEDDDS-----LKCMGYCPQINPLWpdttL 1391
Cdd:PRK10982 21 VRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlFQGkeiDFKSskEALENGISmvhqeLNLVLQRSVMDNMW----L 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHfeiygAVKGM--SASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQ 1469
Cdd:PRK10982 97 GRY-----PTKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 27262626 1470 HMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQ 1510
Cdd:PRK10982 172 HLFTIIRK-LKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1317-1515 |
3.86e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 53.31 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIIN-----ILVGDIEPTSGQV--FLGDYSSETSEDDDSLKCMGYCPQINPLWPDT 1389
Cdd:PRK14267 21 KGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrlLELNEEARVEGEVrlFGRNIYSPDVDPIEVRREVGMVFQYPNPFPHL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1390 TLQEHFEIYGAVKGMSASDmKEVISRITHAL-------DLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:PRK14267 101 TIYDNVAIGVKLNGLVKSK-KELDERVEWALkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTAN 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1463 MDPKAKQHMWRAIrtaFKNRKRAAI-LTTHYMEEAEAVCDRVAIMVSGQLRCIG 1515
Cdd:PRK14267 180 IDPVGTAKIEELL---FELKKEYTIvLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1292-1360 |
4.11e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 4.11e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1292 VSNLHKEYDDK---KDFllsrkvkkvatkyiSFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG 1360
Cdd:PRK11147 322 MENVNYQIDGKqlvKDF--------------SAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG 379
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
488-646 |
4.17e-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: 54.69 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 488 RKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCpPSDGFASIYGHRVSEID--EMFEARKMIGICPQ-- 563
Cdd:COG4172 293 RRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSrrALRPLRRRMQVVFQdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 564 ---LDIHFDVL-TVEENLSILAsiKGIPANNIIQEVQKVL----LDLDMQtikDNQAKKLSGGQKRKLSlgIA---VLgN 632
Cdd:COG4172 372 fgsLSPRMTVGqIIAEGLRVHG--PGLSAAERRARVAEALeevgLDPAAR---HRYPHEFSGGQRQRIA--IAralIL-E 443
|
170
....*....|....
gi 27262626 633 PKILLLDEPTAGMD 646
Cdd:COG4172 444 PKLLVLDEPTSALD 457
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
497-697 |
4.37e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 55.17 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghRVSeidemfeARKMIGICPQLD----------- 565
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG-------RVW-------AERSIAYVPQQAwimnatvrgni 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 566 IHFDvltvEENLSILASikgipANNIIQ-EVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAG 644
Cdd:PTZ00243 742 LFFD----EEDAARLAD-----AVRVSQlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 645 MDP-CSRHIVWNLLKYRKANRVTVFSTHfmdEADIL--ADRKAVISQGMLKCVGSS 697
Cdd:PTZ00243 813 LDAhVGERVVEECFLGALAGKTRVLATH---QVHVVprADYVVALGDGRVEFSGSS 865
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1315-1520 |
4.44e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 54.86 E-value: 4.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1315 ATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF---------------LGDYSSETSED----DDSLKC 1375
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrrrsrqvieLSEQSAAQMRHvrgaDMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1376 MGYCPQINPLWP-DTTLQEHFEIY-GAVKGMSASDMKEVIS--RITHAldlKEHLQKTVKKLPAGIKRKLCFALSMLGNP 1451
Cdd:PRK10261 111 QEPMTSLNPVFTvGEQIAESIRLHqGASREEAMVEAKRMLDqvRIPEA---QTILSRYPHQLSGGMRQRVMIAMALSCRP 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1452 QITLLDEPSTGMDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1319-1512 |
5.92e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 54.16 E-value: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIE-PTSGQVFLGDYSSETSEDDDSLK---CMgycpqinplwpdttLQEH 1394
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAqgiAM--------------VPED 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 FEIYGAVKGM--------SASDMKEVISRITHALDLKEHLQ-------KT------VKKLPAGIKRKLCFALSMLGNPQI 1453
Cdd:PRK13549 347 RKRDGIVPVMgvgknitlAALDRFTGGSRIDDAAELKTILEsiqrlkvKTaspelaIARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1454 TLLDEPSTGMDPKAKQHMWRAIrTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLR 1512
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLI-NQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
497-667 |
6.72e-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: 51.00 E-value: 6.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFasiyghrvseidemfearkmIGICPQLDIHFdvltveen 576
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR--------------------IGMPEGEDLLF-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 lsilasikgIPanniiqevQKVLLDLDmqTIKDnQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRH 651
Cdd:cd03223 69 ---------LP--------QRPYLPLG--TLRE-QliypwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170
....*....|....*.
gi 27262626 652 IVWNLLKYRKANRVTV 667
Cdd:cd03223 129 RLYQLLKELGITVISV 144
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
490-658 |
6.92e-07 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 53.17 E-value: 6.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 490 KGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDE--MFEARKMIGICPQldih 567
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDdeWRAVRSDIQMIFQ---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 fdvltveenlSILASIKG-IPANNIIQEVQKVLL-DLDMQTIKD---NQAKKL--------------SGGQKRKLSLGIA 628
Cdd:PRK15079 106 ----------DPLASLNPrMTIGEIIAEPLRTYHpKLSRQEVKDrvkAMMLKVgllpnlinryphefSGGQCQRIGIARA 175
|
170 180 190
....*....|....*....|....*....|
gi 27262626 629 VLGNPKILLLDEPTAGMDPCSRHIVWNLLK 658
Cdd:PRK15079 176 LILEPKLIICDEPVSALDVSIQAQVVNLLQ 205
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
459-646 |
6.95e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 6.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 459 ISFSEiiEPVSSEFVGKEAIRISGIQKTYrkkGE---NVEAlrnlsFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSD 535
Cdd:PRK13409 324 IEFEE--RPPRDESERETLVEYPDLTKKL---GDfslEVEG-----GEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDE 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 536 GFASiyghrvSEIDemfearkmIGICPQ-LDIHFDVlTVEENLSilaSIKGIPANNIIQEvqKVLLDLDMQTIKDNQAKK 614
Cdd:PRK13409 394 GEVD------PELK--------ISYKPQyIKPDYDG-TVEDLLR---SITDDLGSSYYKS--EIIKPLQLERLLDKNVKD 453
|
170 180 190
....*....|....*....|....*....|..
gi 27262626 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PRK13409 454 LSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
478-642 |
8.22e-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: 53.53 E-value: 8.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 478 IRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKS-TLMNILcGLCPPSDGFASiyghrvSEIdeMFEARK 556
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDPAAHPS------GSI--LFDGQD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 MIGICP-QL------DIHF----------DVLTVEENLS-ILASIKGIPAnniiQEVQKVLLD-LDMQTIKDNQAK---- 613
Cdd:COG4172 78 LLGLSErELrrirgnRIAMifqepmtslnPLHTIGKQIAeVLRLHRGLSG----AAARARALElLERVGIPDPERRlday 153
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 614 --KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG4172 154 phQLSGGQRQRVMIAMALANEPDLLIADEPT 184
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
497-696 |
9.65e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.97 E-value: 9.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPP-SDGFASIYGH--RVSEIDEMFEArkmigicpqldihfdvlTV 573
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTvaYVPQVSWIFNA-----------------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 574 EENLSILASIKGIPANNIIqEVQKVLLDLDM-----QTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP- 647
Cdd:PLN03130 696 RDNILFGSPFDPERYERAI-DVTALQHDLDLlpggdLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAh 774
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 648 CSRHIVWNLLK--YRKANRVTVFST-HFMDEadilADRKAVISQGMLKCVGS 696
Cdd:PLN03130 775 VGRQVFDKCIKdeLRGKTRVLVTNQlHFLSQ----VDRIILVHEGMIKEEGT 822
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
485-689 |
1.19e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 485 KTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIdEMFEARKMIGICPQL 564
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL-QLDSWRSRLAVVSQT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 565 DIHF-DvlTVEENLSIlasikGIPA--NNIIQEVQKV------LLDLDM--QTIKDNQAKKLSGGQKRKLSLGIAVLGNP 633
Cdd:PRK10789 398 PFLFsD--TVANNIAL-----GRPDatQQEIEHVARLasvhddILRLPQgyDTEVGERGVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 634 KILLLDEPTAGMDPCSRH-IVWNLLKYRKaNRVTVFSTHFMdEADILADRKAVISQG 689
Cdd:PRK10789 471 EILILDDALSAVDGRTEHqILHNLRQWGE-GRTVIISAHRL-SALTEASEILVMQHG 525
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
1.55e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 50.72 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFEAR-----KMIGICPQLDI----H 567
Cdd:PRK13540 17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQlcfvgHRSGINPYLTLrencL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLsilasikgipanniiqEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK13540 97 YDIHFSPGAV----------------GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*
gi 27262626 648 CS-RHIVWNLLKYRKANRVTVFSTH 671
Cdd:PRK13540 161 LSlLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1319-1526 |
1.57e-06 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 53.04 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSEdddSL-KCMGYCPQINPLW--------- 1386
Cdd:PRK13657 354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtDIRTVTRA---SLrRNIAVVFQDAGLFnrsiednir 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1387 ---PDTTlqeHFEIYGAVKGMSASDMkevISRITHALDlkehlqkTV-----KKLPAGIKRKLCFALSMLGNPQITLLDE 1458
Cdd:PRK13657 431 vgrPDAT---DEEMRAAAERAQAHDF---IERKPDGYD-------TVvgergRQLSGGERQRLAIARALLKDPPILILDE 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 1459 PSTGMDPKAKQHMWRAIRTAFKNRKRAAI---LTThyMEEAeavcDRVAIMVSGQLRCIGTVQHLKSKFGK 1526
Cdd:PRK13657 498 ATSALDVETEAKVKAALDELMKGRTTFIIahrLST--VRNA----DRILVFDNGRVVESGSFDELVARGGR 562
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1319-1519 |
1.60e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 52.61 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKC-MGYCPQ------INPLwpdTTL 1391
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgIMLCPEdrkaegIIPV---HSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIygavkgmSA----SDMKEVISRITHALDLKEHLQKTVKKLPAGikRKLCFALSMlGNPQ-------------IT 1454
Cdd:PRK11288 349 ADNINI-------SArrhhLRAGCLINNRWEAENADRFIRSLNIKTPSR--EQLIMNLSG-GNQQkailgrwlsedmkVI 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1455 LLDEPSTGMDPKAKQHMWRAIRtAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRciGTVQH 1519
Cdd:PRK11288 419 LLDEPTRGIDVGAKHEIYNVIY-ELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAR 480
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
497-646 |
1.75e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDeMFEARKMIGICPQLDIHFDVlTVEEN 576
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG-LTDLRRVLSIIPQSPVLFSG-TVRFN 1329
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 577 LSILAS------IKGIPANNIIQEVQKVLLDLDMQTIKDNQakKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:PLN03232 1330 IDPFSEhndadlWEALERAHIKDVIDRNPFGLDAEVSEGGE--NFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1319-1522 |
1.81e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 51.30 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLGDYSSETSEDD--DSLKCMGYCPQINPLWPDTT----- 1390
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEIlFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDMNvfdnv 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 ---LQEHfeiygavkgmsaSDMKEVISRIT-----HALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:PRK11831 106 aypLREH------------TQLPAPLLHSTvmmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1463 MDPKAKQHMWRAIRTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:PRK11831 174 QDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
499-642 |
1.86e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 499 NLSFdiYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvseidemfEARKMIGIC-------PQLDIHFDVL 571
Cdd:PRK11819 27 SLSF--FPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG----------------EARPAPGIKvgylpqePQLDPEKTVR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 572 -TVEENLsilASIKgipanNIIQEVQKV-----LLDLDMQTIKDNQAK-------------------------------- 613
Cdd:PRK11819 89 eNVEEGV---AEVK-----AALDRFNEIyaayaEPDADFDALAAEQGElqeiidaadawdldsqleiamdalrcppwdak 160
|
170 180 190
....*....|....*....|....*....|.
gi 27262626 614 --KLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:PRK11819 161 vtKLSGGERRRVALCRLLLEKPDMLLLDEPT 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
475-653 |
2.24e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.72 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 475 KEAIRISGIQKTYRKKgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIY-----GHRVSEID 549
Cdd:PTZ00265 1163 KGKIEIMDVNFRYISR-PNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFknehtNDMTNEQD 1241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 550 EMFEARKMIG----------------------------------IC----PQLDIHFDVLTVEE---NLSILASIKGIPA 588
Cdd:PTZ00265 1242 YQGDEEQNVGmknvnefsltkeggsgedstvfknsgkilldgvdICdynlKDLRNLFSIVSQEPmlfNMSIYENIKFGKE 1321
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 589 NNIIQEVQKV----LLDLDMQTIKDNQ-------AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIV 653
Cdd:PTZ00265 1322 DATREDVKRAckfaAIDEFIESLPNKYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLI 1397
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
497-653 |
2.58e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPpsDGFAS---IYGHRVSEIDEMFEARKMIG-ICPQLDIHFDVLT 572
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP--QGYSNdltLFGRRRGSGETIWDIKKHIGyVSSSLHLDYRVST 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 573 VEENLsILA----SIkgipanNIIQEV---QKVLLD--LDMQTIKDNQAKK----LSGGQKRKLSLGIAVLGNPKILLLD 639
Cdd:PRK10938 354 SVRNV-ILSgffdSI------GIYQAVsdrQQKLAQqwLDILGIDKRTADApfhsLSWGQQRLALIVRALVKHPTLLILD 426
|
170
....*....|....
gi 27262626 640 EPTAGMDPCSRHIV 653
Cdd:PRK10938 427 EPLQGLDPLNRQLV 440
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1312-1464 |
2.91e-06 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 50.76 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1312 KKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQiNPLWP-DTT 1390
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQ-NATTPgDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1391 LQE--------HFEIYGAVKgmsaSDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:PRK10253 98 VQElvargrypHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 27262626 1463 MD 1464
Cdd:PRK10253 174 LD 175
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1319-1514 |
2.96e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 2.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETS--------------EDDDSLKCMGYCP-QIN 1383
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaneainhgfalvtEERRSTGIYAYLDiGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1384 PLWpdTTLQEHFEIYGAvkgMSASDMKEVISRITHALDLKEHLQKT-VKKLPAGIKRKLCFALSMLGNPQITLLDEPSTG 1462
Cdd:PRK10982 347 SLI--SNIRNYKNKVGL---LDNSRMKSDTQWVIDSMRVKTPGHRTqIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1463 MDPKAKQHMWRAIrTAFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCI 1514
Cdd:PRK10982 422 IDVGAKFEIYQLI-AELAKKDKGIIIISSEMPELLGITDRILVMSNGLVAGI 472
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
1319-1494 |
3.33e-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: 50.02 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVF----LGDYSSETSEDDDSLKCMGYCPQiNPLWPDTTLQEH 1394
Cdd:cd03290 20 INIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ-KPWLLNATVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 F--------EIYGAVkgMSASDMKEVISRITHAlDLKEHLQKTVKkLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPK 1466
Cdd:cd03290 99 ItfgspfnkQRYKAV--TDACSLQPDIDLLPFG-DQTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDPFSALDIH 174
|
170 180
....*....|....*....|....*....
gi 27262626 1467 AKQH-MWRAIRTAFKNRKRAAILTTHYME 1494
Cdd:cd03290 175 LSDHlMQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1319-1516 |
3.98e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 3.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGdIEPTsgqvflGDYSSETSEDDDSLKCMGYCpqinplwpDTtlqEHFEI- 1397
Cdd:PRK13549 24 VSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPH------GTYEGEIIFEGEELQASNIR--------DT---ERAGIa 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1398 -----YGAVKGMSASDMKEVISRITHA---------LDLKEHLQKT---------VKKLPAGIKRKLCFALSMLGNPQIT 1454
Cdd:PRK13549 86 iihqeLALVKELSVLENIFLGNEITPGgimdydamyLRAQKLLAQLkldinpatpVGNLGLGQQQLVEIAKALNKQARLL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 27262626 1455 LLDEPSTGMDPKAKQHMWRAIRTaFKNRKRAAILTTHYMEEAEAVCDRVAIMVSGqlRCIGT 1516
Cdd:PRK13549 166 ILDEPTASLTESETAVLLDIIRD-LKAHGIACIYISHKLNEVKAISDTICVIRDG--RHIGT 224
|
|
| RsgA |
COG1162 |
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis]; |
489-529 |
4.09e-06 |
|
Ribosome biogenesis GTPase RsgA [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440776 [Multi-domain] Cd Length: 300 Bit Score: 50.50 E-value: 4.09e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27262626 489 KKGENVEALRnlsfDIYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:COG1162 152 KTGEGLDELR----ELLKGKTSVLVGQSGVGKSTLINALLP 188
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
482-698 |
4.24e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 51.33 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 482 GIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS--------DG----FASIyghRVSEid 549
Cdd:NF040905 6 GITKTF----PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyegeilfDGevcrFKDI---RDSE-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 550 emfeaRKMIGIcpqldIHFDVLTVEEnLSILASI--------KGI----PANNIIQE-VQKVLLDLDMQT-IKD-----N 610
Cdd:NF040905 77 -----ALGIVI-----IHQELALIPY-LSIAENIflgnerakRGVidwnETNRRARElLAKVGLDESPDTlVTDigvgkQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 611 Q----AKKLSggqKrklslgiavlgNPKILLLDEPTAGM-DPCSRHIVWNLLKYRK------------------ANRVTV 667
Cdd:NF040905 146 QlveiAKALS---K-----------DVKLLILDEPTAALnEEDSAALLDLLLELKAqgitsiiishklneirrvADSITV 211
|
250 260 270
....*....|....*....|....*....|....*..
gi 27262626 668 F------STHFMDEADILADRkavISQGMlkcVGSSM 698
Cdd:NF040905 212 LrdgrtiETLDCRADEVTEDR---IIRGM---VGRDL 242
|
|
| YadH |
COG0842 |
ABC-type multidrug transport system, permease component [Defense mechanisms]; |
222-417 |
4.79e-06 |
|
ABC-type multidrug transport system, permease component [Defense mechanisms];
Pssm-ID: 440604 [Multi-domain] Cd Length: 200 Bit Score: 49.04 E-value: 4.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 222 LIYLVIAFSPFgYFLAIHIVAEKEKKIKEFLKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATA--SLLFPQSSSIVI 299
Cdd:COG0842 9 LLAMSLLFTAL-MLTALSIAREREQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLffGVPLRGLSLLLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 300 FLLFFLYGLSSVFFALMLTPLFKKSKHVGIVEFFVTVAFGFIGLMIILIESFPKSLVWL--FSPFCHctFVIGIAQVmhl 377
Cdd:COG0842 88 LLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESLPGWLQAIayLNPLTY--FVEALRAL--- 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 27262626 378 edFNEGASFSnltagpyPLIITIIMLTLNSIFYVLLAVYL 417
Cdd:COG0842 163 --FLGGAGLA-------DVWPSLLVLLAFAVVLLALALRL 193
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
489-529 |
5.21e-06 |
|
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: 49.32 E-value: 5.21e-06
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27262626 489 KKGENVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:cd01854 71 KTGEGLDELREL----LKGKTSVLVGQSGVGKSTLLNALLP 107
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
497-658 |
5.26e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.96 E-value: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfaSIygHRVSEIDEMFEARK--MIG------IC-PQLDIH 567
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RI--ARPAGARVLFLPQRpyLPLgtlreaLLyPATAEA 454
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 568 FDVLTVEENLsilasikgipanniiqevQKVLLD-----LDMQtikDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG4178 455 FSDAELREAL------------------EAVGLGhlaerLDEE---ADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170
....*....|....*.
gi 27262626 643 AGMDPCSRHIVWNLLK 658
Cdd:COG4178 514 SALDEENEAALYQLLR 529
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1328-1517 |
5.86e-06 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 50.26 E-value: 5.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1328 ILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSL----KCMGYCPQINPLWPdttlqeHFEIYGAVK- 1402
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLppekRRIGYVFQDARLFP------HYKVRGNLRy 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1403 GMSASdMKEVISRITHALDLkEHLqktVKKLPA----GIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTA 1478
Cdd:PRK11144 100 GMAKS-MVAQFDKIVALLGI-EPL---LDRYPGslsgGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 27262626 1479 FKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTV 1517
Cdd:PRK11144 175 AREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
506-646 |
5.98e-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: 49.67 E-value: 5.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 506 EGQITALLGHSGTGKSTLMNILCG-----LC----PPS-DGFASIYghRVSEIDEMFEarKMIG------ICPQldiHFD 569
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGklkpnLGkfddPPDwDEILDEF--RGSELQNYFT--KLLEgdvkviVKPQ---YVD 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 27262626 570 VLTVEENLSILASIKGIPANNIIQEVQKVlldLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:cd03236 98 LIPKAVKGKVGELLKKKDERGKLDELVDQ---LELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1319-1477 |
6.03e-06 |
|
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: 48.80 E-value: 6.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPT---SGQVFLGDYSSetseDDDSLKCMG---YCPQINPLWPDTTLQ 1392
Cdd:cd03233 26 FSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY----KEFAEKYPGeiiYVSEEDVHFPTLTVR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EHFEIygavkgmsasdmkevisrithALDLKEHlqKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMW 1472
Cdd:cd03233 102 ETLDF---------------------ALRCKGN--EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALEIL 158
|
....*
gi 27262626 1473 RAIRT 1477
Cdd:cd03233 159 KCIRT 163
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
503-646 |
6.75e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 50.94 E-value: 6.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 503 DIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEmfEARkmIGICPQ-LDIHFDvLTVEENLSilA 581
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDE--DLK--ISYKPQyISPDYD-GTVEEFLR--S 424
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 582 SIKGIPANNIIQEvqKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:COG1245 425 ANTDDFGSSYYKT--EIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1330-1359 |
7.54e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 50.66 E-value: 7.54e-06
10 20 30
....*....|....*....|....*....|
gi 27262626 1330 GLLGPNGAGKSTIINILVGDIEPTSGQVFL 1359
Cdd:PRK15064 31 GLIGANGCGKSTFMKILGGDLEPSAGNVSL 60
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1317-1523 |
8.30e-06 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.06 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgDYSSETSedddslkcmgYCPQINPLWPDtTLQEHFe 1396
Cdd:TIGR01271 443 KNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGRIS----------FSPQTSWIMPG-TIKDNI- 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 iygaVKGMSASDMKevISRITHALDLKEHLQKTVKK-----------LPAGIKRKLCFALSMLGNPQITLLDEPSTGMDP 1465
Cdd:TIGR01271 508 ----IFGLSYDEYR--YTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 27262626 1466 KAKQHMW-RAIRTAFKNRKRaaILTTHYMEEAEAVcDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:TIGR01271 582 VTEKEIFeSCLCKLMSNKTR--ILVTSKLEHLKKA-DKILLLHEGVCYFYGTFSELQAK 637
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1319-1523 |
9.80e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSEDDDSLKCMGYCPQINPLWPDTT------LQ 1392
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVrfnldpFN 1337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1393 EH--FEIYGAvkgMSASDMKEVISRITHALDLKehLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQH 1470
Cdd:PLN03130 1338 EHndADLWES---LERAHLKDVIRRNSLGLDAE--VSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDAL 1412
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 27262626 1471 MWRAIRTAFKNrkrAAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHLKSK 1523
Cdd:PLN03130 1413 IQKTIREEFKS---CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
494-647 |
1.06e-05 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 49.52 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 494 VEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPS-----DGFasiyghRVSEIDEM----FEARKMIG--IC- 561
Cdd:COG4170 20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtaDRF------RWNGIDLLklspRERRKIIGreIAm 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 562 ----PQ--LDihfDVLTVEENLsilasIKGIPANN---------------IIQEVQKVlldldmqTIKDNQA------KK 614
Cdd:COG4170 94 ifqePSscLD---PSAKIGDQL-----IEAIPSWTfkgkwwqrfkwrkkrAIELLHRV-------GIKDHKDimnsypHE 158
|
170 180 190
....*....|....*....|....*....|...
gi 27262626 615 LSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMES 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
497-646 |
1.15e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 50.29 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHrvseidemfearkmIGICPQLDIHFDVlTVEEN 576
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 577 LSILASIKGIPANNIIQEVQkVLLDLDMQTIKDNQ-----AKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMD 646
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQ-LEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
1317-1522 |
1.21e-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: 1.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVflgDYSSETSedddslkcmgYCPQINPLWPDtTLQEHFe 1396
Cdd:cd03291 54 KNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRIS----------FSSQFSWIMPG-TIKENI- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1397 iygaVKGMSASDMKevISRITHALDLKEHLQKTVKK-----------LPAGIKRKLCFALSMLGNPQITLLDEPSTGMDP 1465
Cdd:cd03291 119 ----IFGVSYDEYR--YKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 1466 KAKQHMWRA-IRTAFKNRKRaaILTTHYMEEAEaVCDRVAIMVSGQLRCIGTVQHLKS 1522
Cdd:cd03291 193 FTEKEIFEScVCKLMANKTR--ILVTSKMEHLK-KADKILILHEGSSYFYGTFSELQS 247
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1326-1475 |
1.47e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1326 GEILGLLGPNGAGKSTIINILVGDIEPTSGQVF------LGDYSSETSE----DDDSLKCMGycpQINPLWPDTTLQEHF 1395
Cdd:PRK10636 338 GSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGlakgikLGYFAQHQLEflraDESPLQHLA---RLAPQELEQKLRDYL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 EIYGaVKGMSASDMKEVISrithaldlkehlqktvkklpAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAI 1475
Cdd:PRK10636 415 GGFG-FQGDKVTEETRRFS--------------------GGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL 473
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
489-529 |
2.08e-05 |
|
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: 46.77 E-value: 2.08e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 27262626 489 KKGENVEALRNLsfdiYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:pfam03193 92 KTGEGIEALKEL----LKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
497-671 |
2.52e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGFASIYGHRVSEIDEMFearkMIGICPQLDIHFDvLTVEEN 576
Cdd:PRK13541 16 LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY----CTYIGHNLGLKLE-MTVFEN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 577 LSILASIKgipanNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDPCSRHIVWNL 656
Cdd:PRK13541 91 LKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*..
gi 27262626 657 LKYrKANR--VTVFSTH 671
Cdd:PRK13541 166 IVM-KANSggIVLLSSH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
441-536 |
2.72e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.96 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 441 SKSK---RNYEELSEGNVNGNISFSEIIEPVSsEFVGKEAIRISGIQKTYrkkGENVeALRNLSFDIYEGQITALLGHSG 517
Cdd:PRK11819 286 AKSKarlARYEELLSEEYQKRNETNEIFIPPG-PRLGDKVIEAENLSKSF---GDRL-LIDDLSFSLPPGGIVGIIGPNG 360
|
90
....*....|....*....
gi 27262626 518 TGKSTLMNILCGLCPPSDG 536
Cdd:PRK11819 361 AGKSTLFKMITGQEQPDSG 379
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1319-1361 |
3.89e-05 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 48.26 E-value: 3.89e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD 1361
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
497-651 |
4.25e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 47.13 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTLMNILCG-LCPPSD-------GFASIYGHRVSEIDEMFEARkMIGICPQLDIHF 568
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdLTGGGAprgarvtGDVTLNGEPLAAIDAPRLAR-LRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENLSI----LASIKGIPANNIIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAV---------LGNPKI 635
Cdd:PRK13547 96 FAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPRY 175
|
170
....*....|....*.
gi 27262626 636 LLLDEPTAGMDPCSRH 651
Cdd:PRK13547 176 LLLDEPTAALDLAHQH 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1317-1491 |
4.61e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 48.18 E-value: 4.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1317 KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGDYSSETSeDDDSLKCM-----GYCPQINPLWPDTTL 1391
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATL-DADALAQLrrehfGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHFEIYGAVKGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHM 1471
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180
....*....|....*....|
gi 27262626 1472 wRAIRTAFKNRKRAAILTTH 1491
Cdd:PRK10535 184 -MAILHQLRDRGHTVIIVTH 202
|
|
| PRK00098 |
PRK00098 |
GTPase RsgA; Reviewed |
489-527 |
1.01e-04 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234631 [Multi-domain] Cd Length: 298 Bit Score: 46.35 E-value: 1.01e-04
10 20 30
....*....|....*....|....*....|....*....
gi 27262626 489 KKGENVEALRNLsfdiYEGQITALLGHSGTGKSTLMNIL 527
Cdd:PRK00098 150 KEGEGLDELKPL----LAGKVTVLAGQSGVGKSTLLNAL 184
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
501-689 |
1.06e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 501 SFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDG-----FASIygHRVSeidemFEA-RKMIGICPQlDIHFDVLTVE 574
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqFSHI--TRLS-----FEQlQKLVSDEWQ-RNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 575 ENLSilasikGIPANNIIQE-------VQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 647
Cdd:PRK10938 95 EDDT------GRTTAEIIQDevkdparCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 27262626 648 CSRHIVWNLLKYRKANRVTV------FST--HFMDEADILADRkAVISQG 689
Cdd:PRK10938 169 ASRQQLAELLASLHQSGITLvlvlnrFDEipDFVQFAGVLADC-TLAETG 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1309-1491 |
1.29e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 47.03 E-value: 1.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1309 RKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIepTSGQVFLGDYSSETSEDDDSL-KCMGYCPQINPLWP 1387
Cdd:TIGR00956 772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSSFqRSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1388 DTTLQEHFEIYGAV---KGMSASDMKEVISRITHALDLKEHLQKTVKKLPAGI----KRKLCFALSMLGNPQITL-LDEP 1459
Cdd:TIGR00956 850 TSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLfLDEP 929
|
170 180 190
....*....|....*....|....*....|....
gi 27262626 1460 STGMDpkaKQHMWRAIRTAFK--NRKRAAILTTH 1491
Cdd:TIGR00956 930 TSGLD---SQTAWSICKLMRKlaDHGQAILCTIH 960
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
477-646 |
1.88e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.04 E-value: 1.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 477 AIRISGIQKTYrkkgENVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGLCPPSDGfasiyghrvsEIDEMFEARk 556
Cdd:PRK15064 319 ALEVENLTKGF----DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG----------TVKWSENAN- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 557 mIGICPQlDiHFDVLTVEENLSILASIKGIPANNIiQEVQKVL--LDLDMQTIKdNQAKKLSGGQKRKLSLGIAVLGNPK 634
Cdd:PRK15064 384 -IGYYAQ-D-HAYDFENDLTLFDWMSQWRQEGDDE-QAVRGTLgrLLFSQDDIK-KSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170
....*....|..
gi 27262626 635 ILLLDEPTAGMD 646
Cdd:PRK15064 459 VLVMDEPTNHMD 470
|
|
| ABC-2_lan_permease_MutE_EpiE-like |
cd21807 |
lantibiotic immunity ABC transporter MutE/EpiE family permease (also called ABC-2 transporter ... |
229-363 |
2.11e-04 |
|
lantibiotic immunity ABC transporter MutE/EpiE family permease (also called ABC-2 transporter MutE/EpiE family permease) subunit; This subfamily includes lantibiotic ABC transporter permease subunits EpiE, MutE, SlvE and NisE, which are highly hydrophobic, integral membrane proteins, and part of the bacitracin ABC transport system that confers resistance to the Gram-positive bacteria in which this system operates, specifically to the lantibiotics mutacin, epidermin, nisin and salivaricin, respectively. Lantibiotics are small peptides, produced by Gram-positive bacteria, which are ribosomally-synthesized as pre-peptides and act by disrupting membrane integrity. Genes encoding the lantibiotic ABC transporter subunits are highly organized in operons containing all the genes required for maturation, transport, immunity, and synthesis. For example, in Staphylococcus epidermidis Tu3298, the lantibiotic epidermin is active against other Gram-positive bacteria via various modes of actions; however, its self-protection against the pore-forming epidermin is mediated by the ABC transporter immunity proteins composed of EpiF, EpiE and EpiG; the EpiE permease subunit transports epidermin to the surface and expels it from the membrane. This subfamily also includes the lantibiotic ABC transporter permease subunits MutE, SlvF, and NisE. Self-protection of the mutacin-producing strain Streptococcus mutans CH43 against the pore-forming lantibiotic mutacin is mediated by an ABC transporter composed of MutF, MutE and MutG. In salivaricin D-producing strain Streptococcus salivarius 5M6c, self-immunity against the intrinsically trypsin-resistant salivaricin is mediated via ABC transporter proteins SlvF, SlvE and SlvG, while in Lactococcus lactis, self-immunity against nisin is mediated by the ABC transporter NisFEG. The MutE, NisE and SlvF permease subunits transport mutacin, nisin and salivaricin, respectively to the surface and expel them from the membrane.
Pssm-ID: 409632 Cd Length: 234 Bit Score: 44.81 E-value: 2.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 229 FSPFGYFLAIHIVAEKEKKIKEF--LKIMGLHDTAFWLSWVLLYTSLIFLMSLLMAVIATAS-LLFPQSSSIVIFLLF-- 303
Cdd:cd21807 48 FLPGGIALLCALSIQKEKKAGNYraLLSLPVSLKKLWLAKILVLAIYLLLSSLILFVLLLLGgLLLGGGISPPISILLas 127
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 27262626 304 ---FLYGLSSVFFALMLtplfkkSKHVGiveFFVTVAFGFIGLMIILIESFPKSLvWLFSPFC 363
Cdd:cd21807 128 lllWLTSLWQIPLCLFL------AKKFG---MFVTIIINVLLGLLLGVLLATTSY-WWLIPWS 180
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
476-642 |
2.35e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 476 EAIRISGIQKTYRKK-----GENvealrnlSFDIY------EGQITALLGHSGTGKSTLMNILCGLCPPSDGfasIYGHR 544
Cdd:COG1245 64 DAISIVNLPEELEEDpvhryGEN-------GFRLYglpvpkKGKVTGILGPNGIGKSTALKILSGELKPNLG---DYDEE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 545 VSeIDEMFEARKmiGIcpQLDIHFDVLtVEENLSilASIKgipanniIQEVQKV----------LLD------------- 601
Cdd:COG1245 134 PS-WDEVLKRFR--GT--ELQDYFKKL-ANGEIK--VAHK-------PQYVDLIpkvfkgtvreLLEkvdergkldelae 198
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 602 -LDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPT 642
Cdd:COG1245 199 kLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS 240
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1284-1357 |
2.40e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.92 E-value: 2.40e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1284 CEEKPSIMVSNLHKEYDDKKDFllsRKVkkvatkyiSFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV 1357
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGC---RDV--------SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEV 63
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
498-665 |
3.07e-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: 43.75 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 498 RNLSFDIYEGqITALLGHSGTGKSTLMNILcglcppsdgFASIYGHRVSEIDEMFEARKMIGICP---QLDIHFDV---- 570
Cdd:cd03240 14 ERSEIEFFSP-LTLIVGQNGAGKTTIIEAL---------KYALTGELPPNSKGGAHDPKLIREGEvraQVKLAFENangk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 571 -LTVEENLSILasikgipaNNII---QEVQKVLLdLDMqtikdnqAKKLSGGQKRKLSLGI------AVLGNPKILLLDE 640
Cdd:cd03240 84 kYTITRSLAIL--------ENVIfchQGESNWPL-LDM-------RGRCSGGEKVLASLIIrlalaeTFGSNCGILALDE 147
|
170 180
....*....|....*....|....*.
gi 27262626 641 PTAGMDPCSRHIVW-NLLKYRKANRV 665
Cdd:cd03240 148 PTTNLDEENIEESLaEIIEERKSQKN 173
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1319-1520 |
3.67e-04 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 44.72 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEP---TSGQV-FLGDYSSETSEDD-DSLKCmgycPQINPLWPD--TTL 1391
Cdd:PRK09473 35 LNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSAtFNGREILNLPEKElNKLRA----EQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1392 QEHF-------EIYGAVKGMSASDMKEVISRITHALDLKEhLQKTVKKLP----AGIKRKLCFALSMLGNPQITLLDEPS 1460
Cdd:PRK09473 111 NPYMrvgeqlmEVLMLHKGMSKAEAFEESVRMLDAVKMPE-ARKRMKMYPhefsGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 27262626 1461 TGMDPKAKQHmwraIRTAFKNRKR----AAILTTHYMEEAEAVCDRVAIMVSGQLRCIGTVQHL 1520
Cdd:PRK09473 190 TALDVTVQAQ----IMTLLNELKRefntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1288-1341 |
4.13e-04 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 45.08 E-value: 4.13e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 27262626 1288 PSIMVSNLHKEYDDKKDfLLSRKV-KKVATKYISFCVKKGEILGLLGPNGAGKST 1341
Cdd:PRK15134 274 PLLDVEQLQVAFPIRKG-ILKRTVdHNVVVKNISFTLRPGETLGLVGESGSGKST 327
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
1319-1476 |
4.82e-04 |
|
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: 44.74 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILvGDIEPTSGQVFlgdyssetseDDDSLKCMGYCPQiNPLWPDTTLQEHFeIY 1398
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRIL-GELWPVYGGRL----------TKPAKGKLFYVPQ-RPYMTLGTLRDQI-IY 537
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 G------AVKGMSASDMKEVIS--RITHALDLK---EHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKA 1467
Cdd:TIGR00954 538 PdssedmKRRGLSDKDLEQILDnvQLTHILEREggwSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDV 617
|
....*....
gi 27262626 1468 KQHMWRAIR 1476
Cdd:TIGR00954 618 EGYMYRLCR 626
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
1325-1361 |
4.88e-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: 42.36 E-value: 4.88e-04
10 20 30
....*....|....*....|....*....|....*..
gi 27262626 1325 KGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLGD 1361
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYID 37
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1292-1360 |
5.30e-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: 44.68 E-value: 5.30e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1292 VSNLHKEYDDKKDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGdIEPTSGQV-FLG 1360
Cdd:COG4172 278 ARDLKVWFPIKRGLFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIrFDG 346
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1319-1512 |
5.45e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 44.58 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSEDDDSlkcmgYCPQINPLWPDTTLQEHfeIY 1398
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-DGKPVTAEQPED-----YRKLFSAVFTDFHLFDQ--LL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1399 GavKGMSASDMKEVIS-----RITHALDLKEHlQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWR 1473
Cdd:PRK10522 414 G--PEGKPANPALVEKwlerlKMAHKLELEDG-RISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 27262626 1474 AIRTAFKNRKRAAILTTH---YMEEAeavcDRVAIMVSGQLR 1512
Cdd:PRK10522 491 VLLPLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQLS 528
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1303-1529 |
7.31e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.33 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1303 KDFLLSRKVKKVAT-KYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPtsgqvFLGDYSSETSEDDDSLKCMG---- 1377
Cdd:TIGR00956 63 RKLKKFRDTKTFDIlKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDG-----FHIGVEGVITYDGITPEEIKkhyr 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1378 ----YCPQINPLWPDTTLQEHFEIYGA-------VKGMS----ASDMKEVISRiTHALDlkeHLQKT------VKKLPAG 1436
Cdd:TIGR00956 138 gdvvYNAETDVHFPHLTVGETLDFAARcktpqnrPDGVSreeyAKHIADVYMA-TYGLS---HTRNTkvgndfVRGVSGG 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1437 IKRKLCFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfKNRKRAAILTTHYM--EEAEAVCDRVAIMVSGQLRCI 1514
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTS-ANILDTTPLVAIYQcsQDAYELFDKVIVLYEGYQIYF 292
|
250
....*....|....*.
gi 27262626 1515 GTVQHLKSKFGK-GYF 1529
Cdd:TIGR00956 293 GPADKAKQYFEKmGFK 308
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1319-1482 |
1.00e-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: 43.66 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSeddDSL-KCMGYCPQinplwpDTTLqehF 1395
Cdd:COG5265 377 VSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDgqDIRDVTQ---ASLrAAIGIVPQ------DTVL---F 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1396 E-------IYGAVkgmSASDmKEVISRITHAldlkeHLQKTVKKLPAGI---------------KRKLCFALSMLGNPQI 1453
Cdd:COG5265 445 NdtiayniAYGRP---DASE-EEVEAAARAA-----QIHDFIESLPDGYdtrvgerglklsggeKQRVAIARTLLKNPPI 515
|
170 180
....*....|....*....|....*....
gi 27262626 1454 TLLDEPSTGMDPKAKQHMWRAIRTAFKNR 1482
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVARGR 544
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
497-646 |
1.37e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 43.24 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 497 LRNLSFDIYEGQITALLGHSGTGKSTL-MNIlcglcppsdgFASIYGHRVS--------EID-------------EMFEA 554
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELaMSV----------FGRSYGRNISgtvfkdgkEVDvstvsdaidaglaYVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 555 RKMIGIcpqldihfdVL--TVEENLSiLASIKGIPANNIIQEVQKVLLDLDMQT---IK----DNQAKKLSGGQKRKLSL 625
Cdd:NF040905 346 RKGYGL---------NLidDIKRNIT-LANLGKVSRRGVIDENEEIKVAEEYRKkmnIKtpsvFQKVGNLSGGNQQKVVL 415
|
170 180
....*....|....*....|.
gi 27262626 626 GIAVLGNPKILLLDEPTAGMD 646
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGID 436
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1330-1459 |
1.48e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.18 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1330 GLLGPNGAGKSTIINILVGDIEPTSGQVFLgdyssetsedDDSLKCmGYCPQINPLWPDTT---------------LQEH 1394
Cdd:PRK11819 37 GVLGLNGAGKSTLLRIMAGVDKEFEGEARP----------APGIKV-GYLPQEPQLDPEKTvrenveegvaevkaaLDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1395 FEIYGAvkgMSASD---------MKEVISRITHA----LDLK-----EHLQ-----KTVKKLPAGIKRK--LCFALsmLG 1449
Cdd:PRK11819 106 NEIYAA---YAEPDadfdalaaeQGELQEIIDAAdawdLDSQleiamDALRcppwdAKVTKLSGGERRRvaLCRLL--LE 180
|
170
....*....|
gi 27262626 1450 NPQITLLDEP 1459
Cdd:PRK11819 181 KPDMLLLDEP 190
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
507-647 |
1.65e-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: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 507 GQITALLGHSGTGKSTLMNILCGLCPPSdgfasiyGHRVSEIDemfearkmigicpqldihfdvltveenlsilasikgi 586
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPP-------GGGVIYID------------------------------------- 37
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 27262626 587 panniIQEVQKVLLDLDMQTIKDNQAKKLSGGQKRKLSLGIAVLGNPKILLLDEPTAGMDP 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 |
2.13e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.42 E-value: 2.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 613 KKLSGGQKRKLS----LGIAVLGNPKILLLDEPTAGMDPCSRH-IVWNLLKYRKANRVTVFSTH---FMDEADILADRKA 684
Cdd:cd03227 76 LQLSGGEKELSAlaliLALASLKPRPLYILDEIDRGLDPRDGQaLAEAILEHLVKGAQVIVITHlpeLAELADKLIHIKK 155
|
....*
gi 27262626 685 VISQG 689
Cdd:cd03227 156 VITGV 160
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1294-1464 |
2.78e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 41.87 E-value: 2.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1294 NLHKEYDDKKDFLL-SRKVKkvATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLgDYSSETSEDDDS 1372
Cdd:PRK11308 10 DLKKHYPVKRGLFKpERLVK--ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYY-QGQDLLKADPEA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1373 LKCMGYCPQI---NP---LWP----DTTLQEHFEIYGAvkgMSASDMKEVISRITHALDLK-EHLQKTVKKLPAGIKRKL 1441
Cdd:PRK11308 87 QKLLRQKIQIvfqNPygsLNPrkkvGQILEEPLLINTS---LSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRI 163
|
170 180
....*....|....*....|...
gi 27262626 1442 CFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK11308 164 AIARALMLDPDVVVADEPVSALD 186
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
1285-1360 |
3.04e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 41.62 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1285 EEKPSIM-VSNLHKEYD--DKKDFLLSRKVKKVATKYISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQV-FLG 1360
Cdd:PRK15079 3 EGKKVLLeVADLKVHFDikDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVaWLG 82
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
477-525 |
3.22e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.22e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 27262626 477 AIRISGIQKTYRKKGENVEALRNLSFDIYEGQITALLGHSGTGKSTLMN 525
Cdd:TIGR00630 604 AERRPGNGKFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLIN 652
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1319-1348 |
3.66e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 41.70 E-value: 3.66e-03
10 20 30
....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVG 1348
Cdd:NF040905 20 VNLSVREGEIHALCGENGAGKSTLMKVLSG 49
|
|
| ABC2_membrane |
pfam01061 |
ABC-2 type transporter; |
222-362 |
4.68e-03 |
|
ABC-2 type transporter;
Pssm-ID: 426023 [Multi-domain] Cd Length: 204 Bit Score: 40.33 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 222 LIYLVIAFSPFGYFLAIHIVAEKEKKIKEFLKIMGL-HDTAFWLSWVLLYTSLIFLMSLLMAVIATasLLFPQSSSIVIF 300
Cdd:pfam01061 49 LLFFSILFNAFSALSGISPVFEKERGVLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVY--FMVGLPPSAGRF 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 27262626 301 LLFFL----YGLSSVFFALMLTPLFKKSKHVGIVEFFVTVAFGFIGLMIILIESFPKSLVWL--FSPF 362
Cdd:pfam01061 127 FLFLLvlllTALAASSLGLFISALAPSFEDASQLGPLVLLPLLLLSGFFIPIDSMPVWWQWIyyLNPL 194
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
491-529 |
5.47e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 41.07 E-value: 5.47e-03
10 20 30
....*....|....*....|....*....|....*....
gi 27262626 491 GENVEALRNLsfdIYEGQITALLGHSGTGKSTLMNILCG 529
Cdd:PRK01889 182 GEGLDVLAAW---LSGGKTVALLGSSGVGKSTLVNALLG 217
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
493-646 |
5.67e-03 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 40.40 E-value: 5.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 493 NVEALRNLSFDIYEGQITALLGHSGTGKSTLMNILCGlcPPS----DGFASIYGHRVSEIDEMFEARKMIGICPQLDIHF 568
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAHLGIFLAFQYPIEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 569 DVLTVEENLSI----------LASIKGIPANNIIQEVQKvLLDLDMQTIKDNQAKKLSGGQKRKLS-LGIAVLgNPKILL 637
Cdd:CHL00131 97 PGVSNADFLRLaynskrkfqgLPELDPLEFLEIINEKLK-LVGMDPSFLSRNVNEGFSGGEKKRNEiLQMALL-DSELAI 174
|
....*....
gi 27262626 638 LDEPTAGMD 646
Cdd:CHL00131 175 LDETDSGLD 183
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1333-1464 |
5.87e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.85 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1333 GPNGAGKSTIINILVGDIEPTSGQVFlgdYSSETSEDDDSLKCmGYCPQINPLWPDTTLQEHF----EIYGAVkgmsasd 1408
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIY---YKNCNINNIAKPYC-TYIGHNLGLKLEMTVFENLkfwsEIYNSA------- 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 27262626 1409 mkEVISRITHALDLKEHLQKTVKKLPAGIKRKLCFALSMLGNPQITLLDEPSTGMD 1464
Cdd:PRK13541 102 --ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1319-1511 |
7.47e-03 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 40.78 E-value: 7.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1319 ISFCVKKGEILGLLGPNGAGKSTIINILVGDIEPTSGQVFLG--DYSSETSED----------DDSLKcmgycpqinplw 1386
Cdd:COG3845 277 VSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDgeDITGLSPRErrrlgvayipEDRLG------------ 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1387 pdttlqehfeiYGAVKGMSASD-MkeVISRITHA-------LDLK---EHLQKTVKKL---PAGIKR-----------KL 1441
Cdd:COG3845 345 -----------RGLVPDMSVAEnL--ILGRYRRPpfsrggfLDRKairAFAEELIEEFdvrTPGPDTparslsggnqqKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 27262626 1442 CFALSMLGNPQITLLDEPSTGMDPKAKQHMWRAIRTAfKNRKRAAILTTHYMEEAEAVCDRVAIMVSGQL 1511
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| |
