|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
206-1699 |
0e+00 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 985.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 206 YIREGFLAMQHAVDKAIMRYHANTSAqqlfqKLMVITKRFPFPPYISDPFLIAIQYQLPLLLMLSFTYTSLTIIRAVVQE 285
Cdd:TIGR01257 603 YIWGGFAYLQDMVEQGITRSQMQAEP-----PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLE 677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 286 KEKKLKEYMRMMGLNSWLHWSAWFLMFFLFFLIVVSFMTLlFCVKVKkdiaVLSNSDPSLVLAFLLCFAISSISFSFMVS 365
Cdd:TIGR01257 678 KELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTI-FIMHGR----ILHYSDPFILFLFLLAFSTATIMQCFLLS 752
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 366 TFFSKANIAAAVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAMGAQLIGKFEAKGTGIQWRDLLNPVNVDD 445
Cdd:TIGR01257 753 TFFSKASLAAACSGVIYFTLYLPHILCFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGD 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 446 NFCFGQVLGMLLLDSALYGLVTWYVEAVFPGQFGVPQPWHFFLMPSYWCGNPRTVVGKE----------EEGSDPE--KA 513
Cdd:TIGR01257 833 EFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGGEGCSTREEralektepltEEMEDPEhpEG 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 514 LRNEYFEAEPEDLVAGIKIKHLSKVFQVGNKDkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIH 593
Cdd:TIGR01257 913 INDSFFERELPGLVPGVCVKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVG 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 594 GYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKL 673
Cdd:TIGR01257 991 GKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKL 1070
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 674 SIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQK 753
Cdd:TIGR01257 1071 SVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNC 1150
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 754 YGAGYHMTLVKEPH--------------CNPEGIS------------------------QLVHHHVPNAMLESHAGAELS 795
Cdd:TIGR01257 1151 FGTGFYLTLVRKMKniqsqrggcegtcsCTSKGFStrcparvdeitpeqvldgdvnelmDLVYHHVPEAKLVECIGQELI 1230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 796 FILP-KESTHR-FESLFAKLEKKQKELGIASFGASVTTMEEVFLRVgklvdtSMDIQAIQLPALQYQHER---------- 863
Cdd:TIGR01257 1231 FLLPnKNFKQRaYASLFRELEETLADLGLSSFGISDTPLEEIFLKV------TEDADSGSLFAGGAQQKRenanlrhpcs 1304
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 864 ----RASDWALDSNLCG---VMDPTNGIGAlIEEEEVLVKLNTGLALHCQQFWAMFLKKAAYSWREWKMVAAQVLVPLTC 936
Cdd:TIGR01257 1305 gpteKAGQTPQASHTCSpgqPAAHPEGQPP-PEPEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATF 1383
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 937 LTLALLAIHYTSEIFDDPLLKLSLNEYGRTVVPFSV--PGTSRLA----------------------------------- 979
Cdd:TIGR01257 1384 VFLALMLSIIIPPFGEYPALTLHPWMYGQQYTFFSMdePNSEHLEvladvllnkpgfgnrclkeewlpeypcgnstpwkt 1463
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 980 QQLSENLRDMLQAER-------------------------------------QEPREVLGDL-----EEFLV------FR 1011
Cdd:TIGR01257 1464 PSVSPNITHLFQKQKwtaahpspscrcstrekltmlpecpegagglpppqrtQRSTEILQDLtdrniSDFLVktypalIR 1543
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1012 ASVEG--------------GG------FNERCLVATsFKDRGELTVVTA--------------------------LFNNQ 1045
Cdd:TIGR01257 1544 SSLKSkfwvneqryggisiGGklpaipITGEALVGF-LSDLGQMMNVSGgpvtreaskempdflkhletednikvWFNNK 1622
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1046 AYHSPATALAIVDNLLFKLLCGPQASIE---ISNYPQPRNTLQVAKDHFNEGRKGFD--IALNLLIAMAFLASTFSILAV 1120
Cdd:TIGR01257 1623 GWHALVSFLNVAHNAILRASLPKDRDPEeygITVISQPLNLTKEQLSEITVLTTSVDavVAICVIFAMSFVPASFVLYLI 1702
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1121 SERAVQAKHVQFVSGVHVATFWFSALLWDLISFLVPSLLLLVVFQAFNVHAFTRDGHMADLLLLLMLYGWAIIPLMYLMS 1200
Cdd:TIGR01257 1703 QERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPAS 1782
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1201 FFFSAASTAYTRLTIFNILSGI----ATFIMV------TIMRIPAVkleelsrtLDHVFLVLPNHCLGMAVSNFyenyet 1270
Cdd:TIGR01257 1783 FLFDVPSTAYVALSCANLFIGInssaITFVLElfennrTLLRFNAM--------LRKLLIVFPHFCLGRGLIDL------ 1848
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1271 rrycTSSELAAHYCKKYNIQYQESFYAWSTpgVGKFVTSMAASGGIYLTLLFLIETNLlwrlrtficaFRRRWTlAElQN 1350
Cdd:TIGR01257 1849 ----ALSQAVTDVYAQFGEEHSANPFQWDL--IGKNLVAMAVEGVVYFLLTLLIQHHF----------FLSRWI-AE-PA 1910
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1351 RTSVLPEDQDVAEERSRILVPSLDSMLdtpLIINELSKVYD-QRAPllAVDRISLAVQKGECFGLLGFNGAGKTTTFKML 1429
Cdd:TIGR01257 1911 KEPIFDEDDDVAEERQRIISGGNKTDI---LRLNELTKVYSgTSSP--AVDRLCVGVRPGECFGLLGVNGAGKTTTFKML 1985
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1430 TGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHAN 1509
Cdd:TIGR01257 1986 TGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYAD 2065
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1510 KLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQ 1589
Cdd:TIGR01257 2066 RLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVK 2145
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1590 GQFKCLGSPQHLKSKFGSGYSLQAKVRSEgKQDALEEF---KAFVDLTFPGSILEDEHQDMVHYHLPGCDLswAKVFGIL 1666
Cdd:TIGR01257 2146 GAFQCLGTIQHLKSKFGDGYIVTMKIKSP-KDDLLPDLnpvEQFFQGNFPGSVQRERHYNMLQFQVSSSSL--ARIFQLL 2222
|
1690 1700 1710
....*....|....*....|....*....|...
gi 569000489 1667 EKAKEKYGVDDYSVSQISLEQVFLSFAHLQPPT 1699
Cdd:TIGR01257 2223 ISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTET 2255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
530-751 |
7.27e-113 |
|
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: 356.43 E-value: 7.27e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03263 1 LQIRNLTKTY--KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLK 751
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1381-1602 |
9.88e-113 |
|
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: 356.04 E-value: 9.88e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03263 1 LQIRNLTKTYKKG-TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03263 80 CPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARAReSGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLK 1602
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1381-1634 |
3.73e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 272.71 E-value: 3.73e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:COG1131 1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFgsgyslqakvrsegk 1620
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL--------------- 222
|
250
....*....|....
gi 569000489 1621 qdaLEEfkAFVDLT 1634
Cdd:COG1131 223 ---LED--VFLELT 231
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
530-746 |
5.31e-79 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 260.77 E-value: 5.31e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:COG1131 1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:COG1131 77 YVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1381-1602 |
2.70e-64 |
|
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: 218.01 E-value: 2.70e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03265 1 IEVENLVKKYGD---FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1541 PSTGMDPVARRLLWDTV-ARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLK 1602
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIeKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
530-741 |
6.58e-64 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 214.95 E-value: 6.58e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03230 1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYfyaqlkglslqkcpeevkqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03230 77 YLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1381-1592 |
7.00e-61 |
|
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: 206.09 E-value: 7.00e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLvmyarlrgiperlinacventlrglllephanklvkTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03230 78 LPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
530-755 |
1.08e-60 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 208.56 E-value: 1.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:COG4555 2 IEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:COG4555 78 VLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQK-SDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYG 755
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
549-839 |
1.26e-60 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 210.71 E-value: 1.26e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLY 628
Cdd:TIGR01188 9 VDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGRENLE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 FYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ 708
Cdd:TIGR01188 89 MMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDYIR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 709 QQK-SDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGyhmTLVKEPHC-------NPEGISQLVHHH 780
Cdd:TIGR01188 169 ALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD---TLESRPRDiqslkveVSMLIAELGETG 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 781 VPNAMLE--SHAGAELSFILPKESTHRFESLfaklekKQKELGIASFGASVTTMEEVFLRV 839
Cdd:TIGR01188 246 LGLLAVTvdSDRIKILVPDGDETVPEIVEAA------IRNGIRIRSISTERPSLDDVFLKL 300
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1381-1606 |
1.38e-60 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 208.17 E-value: 1.38e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:COG4555 2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFG 1606
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
530-751 |
1.63e-60 |
|
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: 207.22 E-value: 1.63e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03265 1 IEVENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 690 EPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLK 751
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEklKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
530-745 |
7.42e-57 |
|
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: 196.26 E-value: 7.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGqITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03264 1 LQLENLTKRY----GKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03264 76 YLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCG 745
Cdd:cd03264 156 EPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1381-1590 |
7.41e-50 |
|
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: 176.40 E-value: 7.41e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVY-DQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMG 1459
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1540 EPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRG 212
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1374-1601 |
9.68e-50 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 179.23 E-value: 9.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1374 DSMLDTPLIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGK 1453
Cdd:PRK13537 1 GPMSVAPIDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1454 VRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEP 1533
Cdd:PRK13537 78 ARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
530-741 |
5.31e-49 |
|
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: 174.09 E-value: 5.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03266 2 ITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALgKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1381-1591 |
1.31e-47 |
|
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: 169.77 E-value: 1.31e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYdqrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIgkvRQRMGY 1460
Cdd:cd03269 1 LEVENVTKRF---GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1381-1689 |
1.56e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 172.60 E-value: 1.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDigkVRQRMGY 1460
Cdd:COG4152 2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGyslQAKVRSEGK 1620
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRN---TLRLEADGD 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1621 QDALEEFKAFVDLTFPGS----ILEDEHQDMvhyhlpgcdlswakvfGILEKAKEKYGVDDYSVSQISLEQVF 1689
Cdd:COG4152 233 AGWLRALPGVTVVEEDGDgaelKLEDGADAQ----------------ELLRALLARGPVREFEEVRPSLNEIF 289
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
267-849 |
2.28e-47 |
|
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: 187.53 E-value: 2.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 267 LMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLNSWLHWSAWFLMFFLFFLIVVSFMTLLFcVKVKKDIAVLSNSDPSLV 346
Cdd:TIGR01257 1686 VIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYAVSAGLVVGIF-IGFQKKAYTSPENLPALV 1764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 347 lAFLLCFAISSISFSFMVSTFF---SKANIAAAVGGFLYFFTYTPYFFVAP---------RYNWM-----------TLSQ 403
Cdd:TIGR01257 1765 -ALLMLYGWAVIPMMYPASFLFdvpSTAYVALSCANLFIGINSSAITFVLElfennrtllRFNAMlrkllivfphfCLGR 1843
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 404 KLLSCLLSNVAMAMGAQLiGKfEAKGTGIQWrDLLnpvnvddnfcfGQVLGMLLLDSALYGLVTWYVEavfpgqfgvpqp 483
Cdd:TIGR01257 1844 GLIDLALSQAVTDVYAQF-GE-EHSANPFQW-DLI-----------GKNLVAMAVEGVVYFLLTLLIQ------------ 1897
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 484 WHFFLmpSYWCGNP-RTVVGKEEEGSDPEKalrneyfeaepEDLVAG------IKIKHLSKVFQvgNKDKMGIRDLTLNL 556
Cdd:TIGR01257 1898 HHFFL--SRWIAEPaKEPIFDEDDDVAEER-----------QRIISGgnktdiLRLNELTKVYS--GTSSPAVDRLCVGV 1962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 557 YEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGL 636
Cdd:TIGR01257 1963 RPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGV 2042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 637 SLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD-LLQQQKSDRT 715
Cdd:TIGR01257 2043 PAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNtIVSIIREGRA 2122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 716 VLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGYHMTL-VKEPH------CNPegISQLVHHHVPNAMLES 788
Cdd:TIGR01257 2123 VVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMkIKSPKddllpdLNP--VEQFFQGNFPGSVQRE 2200
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 789 HAGAELSFILPKESTHRfesLFAKLEKKQKELGIASFGASVTTMEEVFLRVGKLVDTSMDI 849
Cdd:TIGR01257 2201 RHYNMLQFQVSSSSLAR---IFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTETYDL 2258
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
531-740 |
3.33e-46 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 165.72 E-value: 3.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI-SQDMAQIRKSLG 609
Cdd:cd03225 1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLML 688
Cdd:cd03225 79 LVFQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 689 DEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1383-1591 |
8.73e-46 |
|
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: 164.31 E-value: 8.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIgKVRQRMGYCP 1462
Cdd:cd03268 3 TNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRRIGALI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1463 QFDALLDHMTGREMLVMYARLRGIPERLINACventLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPS 1542
Cdd:cd03268 79 EAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 1543 TGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03268 155 NGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
530-746 |
1.41e-45 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 164.43 E-value: 1.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:COG1122 1 IELENLSFSYP---GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH--DVLFdNLTVAEHLYFyaqlkGLSLQKCPEE-----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIA 681
Cdd:COG1122 78 GLVFQNpdDQLF-APTVEEDVAF-----GPENLGLPREeirerVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 682 GSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1122 152 EPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
530-733 |
3.77e-45 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 162.26 E-value: 3.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:COG4133 3 LEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQkcPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHfmDEADLLGDRI 733
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLARgGAVLLTTH--QPLELAAARV 199
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
530-839 |
4.73e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 165.67 E-value: 4.73e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDmaqIRKSLG 609
Cdd:COG4152 2 LELKGLTKRF----GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQK-SDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGAGyhmTLVKEPHC 768
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRN---TLRLEADG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 769 NPEGISQLvhhhvPNAMLESHAGAELSFILPKESTHrfESLFAKLEKKQkelGIASFGASVTTMEEVFLRV 839
Cdd:COG4152 232 DAGWLRAL-----PGVTVVEEDGDGAELKLEDGADA--QELLRALLARG---PVREFEEVRPSLNEIFIEV 292
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1381-1593 |
5.48e-45 |
|
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: 161.98 E-value: 5.48e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGeCFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03264 77 LPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1541 PSTGMDPVAR---RLLWDTVArareSGKAIVITSHSMEECEALCTRLAIMVQGQFK 1593
Cdd:cd03264 157 PTAGLDPEERirfRNLLSELG----EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1375-1601 |
6.55e-45 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 166.54 E-value: 6.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1375 SMLDTPLIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV 1454
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
528-739 |
9.07e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 163.34 E-value: 9.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIrks 607
Cdd:COG1116 6 PALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 lGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:COG1116 83 -GVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:COG1116 162 MDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
530-738 |
1.10e-44 |
|
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: 161.49 E-value: 1.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIsqdmAQIRKSLG 609
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAK 738
Cdd:cd03293 157 EPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
530-740 |
1.81e-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: 157.83 E-value: 1.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqdmAQIRKSLG 609
Cdd:cd03269 1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03269 74 YLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd03269 154 EPFSGLDPVNVELLKDVIRELARAgKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
549-693 |
1.94e-41 |
|
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: 149.72 E-value: 1.94e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIRKSLGLCPQHDVLFDNLTVAEHL 627
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAQLKGLSLQKCPEEVKQMLHILSLEDKRD----LRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
527-739 |
2.74e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 154.96 E-value: 2.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 527 VAGIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRK 606
Cdd:PRK13537 5 VAPIDFRNVEKRY----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 607 SLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:PRK13537 81 RVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
530-741 |
2.76e-41 |
|
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: 152.35 E-value: 2.76e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:cd03258 2 IELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKV 685
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 686 LMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03258 162 LLCDEATSALDPETTQSILALLRdiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
530-746 |
4.57e-41 |
|
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: 152.06 E-value: 4.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvGnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:COG1127 6 IEVRNLTKSF--G--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFY-AQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:COG1127 82 RRIGMLFQGGALFDSLTVFENVAFPlREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
530-745 |
1.20e-40 |
|
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: 149.59 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQiRKSLG 609
Cdd:cd03259 1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03259 76 MVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCG 745
Cdd:cd03259 156 EPLSALDAKLREELREELKelQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
530-746 |
1.24e-40 |
|
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: 150.91 E-value: 1.24e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIRKSL 608
Cdd:cd03295 1 IEFENVTKRY---GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReQDPVELRRKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDK--RDLRSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:cd03295 78 GYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:cd03295 158 LMDEPFGALDPITRDQLQEEFKrlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1383-1591 |
2.79e-40 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 148.77 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYC 1461
Cdd:cd03225 2 LKNLSFSYPDGARP-ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQF--DALLDHMTGREmlVMYA-RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:cd03225 81 FQNpdDQFFGPTVEEE--VAFGlENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1539 DEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
530-741 |
1.04e-39 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 146.98 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIsQDMAQIRKSLG 609
Cdd:cd03268 1 LKTNDLTKTY----GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSlqkcPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03268 76 ALIEAPGFYPNLTARENLRLLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1381-1572 |
1.29e-39 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 146.47 E-value: 1.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:COG4133 3 LEAENLSCRRGER-LLF--SGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINacVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSH 1572
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
530-746 |
1.10e-38 |
|
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: 144.95 E-value: 1.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:cd03261 1 IELRGLTKSFG----GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYAQLKG-LSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:cd03261 77 RRMGMLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
530-741 |
1.78e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 143.42 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKdkMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:COG4619 1 LELEGLS--FRVGGK--PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNlTVAEHLYFYAQLKGLSLQkcPEEVKQMLHILSL-EDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
531-740 |
3.18e-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: 140.84 E-value: 3.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLG 609
Cdd:cd00267 1 EIENLSFRY----GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQhdvlfdnltvaehlyfyaqlkglslqkcpeevkqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd00267 77 YVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd00267 106 EPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
549-741 |
1.40e-37 |
|
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: 141.81 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCP--QHDVLFDNLTVAE- 625
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRtfQIPRLFPELTVLEn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 ---------HLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:cd03219 96 vmvaaqartGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLN 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 697 AVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03219 176 PEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRV 221
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
530-739 |
1.73e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 144.97 E-value: 1.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:PRK13536 42 IDLAGVSKSYG----DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 690 EPTSGMDAVSRRAIWD----LLQQQKsdrTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK13536 198 EPTTGLDPHARHLIWErlrsLLARGK---TILLTTHFMEEAERLCDRLCVLEAG 248
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
530-741 |
7.70e-37 |
|
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: 139.16 E-value: 7.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 -KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADlLGDRIAILAKGEL 741
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAgtTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1381-1599 |
3.08e-36 |
|
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: 137.85 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-SDIGKVRQRMG 1459
Cdd:COG1122 1 IELENLSFSYPGGTPAL--DDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQF-DALLDHMTGREMlVMYA-RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLStgIA--LIGEPAV 1535
Cdd:COG1122 79 LVFQNpDDQLFAPTVEED-VAFGpENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVA--IAgvLAMEPEV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
530-740 |
3.81e-36 |
|
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: 135.39 E-value: 3.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQI---RK 606
Cdd:cd03229 1 LELKNVSKRY----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 607 SLGLCPQHDVLFDNLTVAEHLYFYaqlkglslqkcpeevkqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVL 686
Cdd:cd03229 77 RIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd03229 123 LLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
530-740 |
9.79e-36 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 134.05 E-value: 9.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:cd03228 1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFdNLTVAEHLyfyaqlkglslqkcpeevkqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVLML 688
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 689 DEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADlLGDRIAILAKGE 740
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
530-745 |
1.14e-35 |
|
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: 137.39 E-value: 1.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF----------QVGNKDKM----------GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGH 589
Cdd:cd03294 1 IKIKGLYKIFgknpqkafklLAKGKSKEeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 590 AYIHGYEISQ----DMAQIR-KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF 664
Cdd:cd03294 81 VLIDGQDIAAmsrkELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 665 LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD-LLQ-QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDeLLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
|
...
gi 569000489 743 CCG 745
Cdd:cd03294 241 QVG 243
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
530-741 |
1.15e-35 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 135.99 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAqirKSLG 609
Cdd:TIGR03740 1 LETKNLSKRF----GKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTRKDL---HKIG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQkcpeEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:TIGR03740 74 SLIESPPLYENLTARENLKVHTTLLGLPDS----RIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQgITVILSSHILSEVQQLADHIGIISEGVL 202
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
543-745 |
2.03e-35 |
|
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: 135.09 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 543 NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP---TSGHAYIHGYEISQDmaQIRKSLGLCPQHDVLFD 619
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 620 NLTVAEHLYFYAQLKglsLQKC-PEEVKQM------LHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:cd03234 95 GLTVRETLTYTAILR---LPRKsSDAIRKKrvedvlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 693 SGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHfMDEADL--LGDRIAILAKGELQCCG 745
Cdd:cd03234 172 SGLDSFTALNLVSTLSQlARRNRIVILTIH-QPRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
530-742 |
3.60e-35 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 134.77 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKD-----------------KMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYI 592
Cdd:cd03267 1 IEVSNLSKSYRVYSKEpgligslkslfkrkyreVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 593 HGYEISQDMAQIRKSLGLC-PQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKR 671
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 672 KLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
530-741 |
1.01e-34 |
|
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: 140.81 E-value: 1.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKM-GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS----QDMAQI 604
Cdd:COG1123 261 LEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSLGLCPQH--DVLFDNLTVAEHLYF-YAQLKGLSLQKCPEEVKQMLHILSLEdkRDLRSKF---LSGGMKRKLSIGIA 678
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLP--PDLADRYpheLSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 679 LIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRI 483
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
530-741 |
1.13e-34 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 133.24 E-value: 1.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:COG1136 5 LELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 -KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:COG1136 85 rRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHfmdEADLLG--DRIAILAKGEL 741
Cdd:COG1136 165 LILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTH---DPELAAraDRVIRLRDGRI 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1381-1591 |
1.94e-34 |
|
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: 131.87 E-value: 1.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDqraPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIsSDIGKVRQRMGY 1460
Cdd:cd03259 1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03259 77 VFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
530-741 |
2.64e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 131.86 E-value: 2.64e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03257 2 LEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 -------------LCPQHdvlfdnlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF---LSGGMKRKL 673
Cdd:cd03257 82 keiqmvfqdpmssLNPRM-------TIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYpheLSGGQRQRV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 674 SIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03257 155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
531-746 |
2.68e-34 |
|
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: 132.86 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSKVFqvgnkdkmG----IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIR 605
Cdd:COG0411 6 EVRGLTKRF--------GglvaVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITgLPPHRIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KsLGLCP--QHDVLFDNLTVAEHL----------YFYAQLKGL-----SLQKCPEEVKQMLHILSLEDKRDLRSKFLSGG 668
Cdd:COG0411 78 R-LGIARtfQNPRLFPELTVLENVlvaaharlgrGLLAALLRLprarrEEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 669 MKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1383-1591 |
3.02e-34 |
|
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: 129.29 E-value: 3.02e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYC 1461
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQFdalldhmtgremlvmyarlrgiperlinacventlrglllephanklvktySGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 1542 STGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
530-746 |
3.46e-34 |
|
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: 132.47 E-value: 3.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:COG1120 2 LEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNLTVAE--------HLYFYAQLKGLSLQKCpEEVKQMLHILSLEDkRDLRSkfLSGGMKRKLSIGIALI 680
Cdd:COG1120 78 AYVPQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDREAV-EEALERTGLEHLAD-RPVDE--LSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
528-746 |
6.60e-34 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 6.60e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQI--- 604
Cdd:COG3842 4 PALELENVSKRY----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLppe 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSLGLCPQHDVLFDNLTVAEHLYFyaqlkGLSLQKCPEE-----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIAL 679
Cdd:COG3842 76 KRNVGMVFQDYALFPHLTVAENVAF-----GLRMRGVPKAeirarVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG3842 151 APEPRVLLLDEPLSALDAKLREEMREELRrlQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGT 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1398-1632 |
7.78e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 142.19 E-value: 7.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI-SSDIgKVRQRMGYCPQFDALLDHMTGREM 1476
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDI-ATRRRVGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:NF033858 360 LELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1557 VAR-ARESGKAIVITSHSMEECEaLCTRLAIMVQGQFKCLGSPQHLKSKFGSgyslqakvrsegkqDALEEfkAFVD 1632
Cdd:NF033858 440 LIElSREDGVTIFISTHFMNEAE-RCDRISLMHAGRVLASDTPAALVAARGA--------------ATLEE--AFIA 499
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
530-746 |
9.04e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 9.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQD-MAQIRKSL 608
Cdd:PRK13632 8 IKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:PRK13632 86 GIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEAdLLGDRIAILAKGELQCCGS 746
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1381-1601 |
2.39e-33 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 129.59 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMG- 1459
Cdd:cd03218 1 LRAENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 -YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:cd03218 78 gYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1539 DEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEI 220
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1376-1600 |
2.71e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLI-INELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDIGKV 1454
Cdd:COG1121 1 MMMMPAIeLENLTVSYGGR---PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQFDALLDH--MTGREMLVM--YARLR--GIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIA 1528
Cdd:COG1121 74 RRRIGYVPQRAEVDWDfpITVRDVVLMgrYGRRGlfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFkCLGSPQH 1600
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPPEE 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
530-747 |
3.47e-33 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 128.81 E-value: 3.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03218 1 LRAENLSKRY----GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LC--PQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:cd03218 77 IGylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQQKsDRT--VLLTTHFMDEADLLGDRIAILAKGELQCCGSS 747
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILK-DRGigVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
530-741 |
3.79e-33 |
|
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: 128.84 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP-----PTSGHAYIHG---YEISQDM 601
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGkdiYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIRKSLGLCPQHDVLFDnLTVAEHLYFYAQLKGLSLQKCPEE-VKQMLHILSLED--KRDLRSKFLSGGMKRKLSIGIA 678
Cdd:cd03260 77 LELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDErVEEALRKAALWDevKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 679 LIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
520-760 |
8.20e-33 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 136.05 E-value: 8.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 520 EAEPEDLVAGIKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ 599
Cdd:COG4987 324 EPAPAPGGPSLELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRD 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 600 -DMAQIRKSLGLCPQHDVLF-----DNLTVAehlyfyaqlkglslqkCP----EEVKQMLHILSLEDkrDLRS------- 662
Cdd:COG4987 402 lDEDDLRRRIAVVPQRPHLFdttlrENLRLA----------------RPdatdEELWAALERVGLGD--WLAAlpdgldt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 663 ------KFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADlLGDRIAIL 736
Cdd:COG4987 464 wlgeggRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVL 542
|
250 260
....*....|....*....|....
gi 569000489 737 AKGELQCCGSSLFLKQKYGAGYHM 760
Cdd:COG4987 543 EDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1396-1600 |
1.10e-32 |
|
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: 127.55 E-value: 1.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1396 LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISsdiGK-----VRQRMGYCPQFDALLDH 1470
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDIT---GLppheiARLGIGRTFQIPRLFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1471 MTGRE--MLVMYARLRGIP--------ERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03219 90 LTVLEnvMVAAQARTGSGLllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQH 1600
Cdd:cd03219 170 PAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDE 229
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1381-1601 |
2.91e-32 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 126.68 E-value: 2.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMG- 1459
Cdd:COG1137 4 LEAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 -YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:COG1137 81 gYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1539 DEPSTGMDPVA----RRLlwdtVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:COG1137 161 DEPFAGVDPIAvadiQKI----IRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1386-1601 |
3.61e-32 |
|
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: 126.26 E-value: 3.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSKVYDQRAPllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQF 1464
Cdd:cd03295 6 VTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYVIQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPhaNKLVKTY----SGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03295 84 IGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDP--AEFADRYphelSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRlQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
549-740 |
4.32e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.62 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI----SQDMAqiRKSLGLCPQHDVLFDNLTVA 624
Cdd:cd03224 16 LFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItglpPHERA--RAGIGYVPEGRRIFPELTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHLYFYAQ-LKGLSLQKCPEEVKQMLHIlsLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:cd03224 94 ENLLLGAYaRRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEI 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 569000489 704 WDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd03224 172 FEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
528-746 |
1.21e-31 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 128.27 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFqvGNKDkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ------DM 601
Cdd:COG3839 2 ASLELENVSKSY--GGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDlppkdrNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIrkslglcPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIA 681
Cdd:COG3839 78 AMV-------FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 682 GSKVLMLDEPTSGMDAVSR---RA-IWDLlqQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRvemRAeIKRL--HRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
528-739 |
1.59e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.97 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQiRks 607
Cdd:COG4525 2 SMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 lGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:COG4525 79 -GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:COG4525 158 MDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVEEALFLATRLVVMSPG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
541-741 |
1.71e-31 |
|
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: 122.66 E-value: 1.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 541 VGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGL--FPPTSGHAYIHGyeISQDMAQIRKSLGLCPQHDVLF 618
Cdd:cd03213 17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLING--RPLDKRSFRKIIGYVPQDDILH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 619 DNLTVAEHLYFYAQLKGLSlqkcpeevkqmlhilsledkrdlrskflsGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAV 698
Cdd:cd03213 95 PTLTVRETLMFAAKLRGLS-----------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 699 SRRAIWDLLQQQKSD-RTVLLTTH---------FmdeadllgDRIAILAKGEL 741
Cdd:cd03213 146 SALQVMSLLRRLADTgRTIICSIHqpsseifelF--------DKLLLLSQGRV 190
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
522-741 |
1.95e-31 |
|
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: 133.42 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 522 EPEDLVAGIKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-D 600
Cdd:COG2274 466 SLPRLKGDIELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiD 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLCPQHDVLF-----DNLTVA------EHLYFYAQLKGLSlqkcpEEVKQM---LHILSLEdkrdlRSKFLS 666
Cdd:COG2274 544 PASLRRQIGVVLQDVFLFsgtirENITLGdpdatdEEIIEAARLAGLH-----DFIEALpmgYDTVVGE-----GGSNLS 613
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 667 GGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTH---FMDEAdllgDRIAILAKGEL 741
Cdd:COG2274 614 GGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRI 687
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
530-742 |
2.29e-31 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 123.13 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqDMAQIRKSLG 609
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03301 76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 690 EPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:cd03301 156 EPLSNLDAKLRVQMRAELKrlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1396-1599 |
2.51e-31 |
|
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: 124.38 E-value: 2.51e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1396 LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIgkVRQRMGYCPQFDALLDHM 1471
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITglppHRI--ARLGIARTFQNPRLFPEL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1472 TGRE--MLVMYARLRGIP-------------ERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:COG0411 95 TVLEnvLVAAHARLGRGLlaallrlprarreEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:COG0411 175 LLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1383-1602 |
3.44e-31 |
|
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: 123.38 E-value: 3.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLlavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKVRQRM 1458
Cdd:cd03261 3 LRGLTKSFGGRTVL---KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 GYCPQFDALLDHMTGRE----MLVMYARLrgiPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:cd03261 80 GMLFQSGALFDSLTVFEnvafPLREHTRL---SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLK 1602
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELR 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
530-746 |
4.39e-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: 130.02 E-value: 4.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPT---SGHAYIHGYEISQDMAQIR- 605
Cdd:COG1123 5 LEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:COG1123 83 RRIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGP 226
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
530-803 |
6.29e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.20 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKD-----------------KMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYI 592
Cdd:COG4586 2 IEVENLSKTYRVYEKEpglkgalkglfrreyreVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 593 HGYEISQDMAQIRKSLGLcpqhdV------LFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKrdlrskfls 666
Cdd:COG4586 82 LGYVPFKRRKEFARRIGV-----VfgqrsqLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGEL--------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 667 ggMK---RKLSIG--------IALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRI 733
Cdd:COG4586 148 --LDtpvRQLSLGqrmrcelaAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEALCDRV 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 734 AILAKGELQCCGSSLFLKQKYGAGYHMTLVKEPHCNPEGISQLVHhhvpnamLESHAGAELSFILPKEST 803
Cdd:COG4586 226 IVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGE-------VIEREGNRVRLEVDPRES 288
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
530-746 |
9.89e-31 |
|
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: 121.96 E-value: 9.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQI---RK 606
Cdd:cd03300 1 IELENVSKFYG----GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDG----KDITNLpphKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 607 SLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:cd03300 73 PVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKrlQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
530-746 |
1.07e-30 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 122.12 E-value: 1.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvfqVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDmaqiRKSLG 609
Cdd:COG1121 7 IELENLT----VSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHdVLFDN---LTVAE--HLYFYAQ---LKGLSlQKCPEEVKQMLHILSLEDKRD--LRSkfLSGGMKRKLSIGIAL 679
Cdd:COG1121 79 YVPQR-AEVDWdfpITVRDvvLMGRYGRrglFRRPS-RADREAVDEALERVGLEDLADrpIGE--LSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGeLQCCGS 746
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGP 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
528-747 |
2.10e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 121.29 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQD-MAQ-IR 605
Cdd:COG1137 2 MTLEAENLVKSY----GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpMHKrAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKV 685
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 686 LMLDEPTSGMD--AVSRraIWDLLQQQKsDR--TVLLTTHFMDEAdlLG--DRIAILAKGELQCCGSS 747
Cdd:COG1137 158 ILLDEPFAGVDpiAVAD--IQKIIRHLK-ERgiGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1381-1596 |
4.53e-30 |
|
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: 119.28 E-value: 4.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS------DIGKV 1454
Cdd:cd03301 1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMgycpqfdALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:cd03301 78 FQNY-------ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLG 1596
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1378-1602 |
6.93e-30 |
|
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: 119.70 E-value: 6.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1378 DTPLI-INELSKVYDQRAPLlavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIG 1452
Cdd:COG1127 2 SEPMIeVRNLTKSFGDRVVL---DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1453 KVRQRMGYCPQFDALLDHMTGRE--MLVMYaRLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLstGIA-- 1528
Cdd:COG1127 79 ELRRRIGMLFQGGALFDSLTVFEnvAFPLR-EHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRV--ALAra 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLK 1602
Cdd:COG1127 156 LALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELL 230
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
530-742 |
7.64e-30 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 119.00 E-value: 7.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:COG2884 2 IRFENVSKRYP---GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQhDV-LFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:COG2884 79 RRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHfmDEA--DLLGDRIAILAKGELQ 742
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEiNRRGTTVLIATH--DLElvDRMPKRVLELEDGRLV 216
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
1381-1601 |
8.61e-30 |
|
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: 119.30 E-value: 8.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMG- 1459
Cdd:TIGR04406 2 LVAENLIKSYKKR---KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGi 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 -YCPQFDALLDHMTGREMLVMYARLRgipERLINACVENTLRGLLLEPH----ANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:TIGR04406 79 gYLPQEASIFRKLTVEENIMAVLEIR---KDLDRAEREERLEALLEEFQishlRDNKAMSLSGGERRRVEIARALATNPK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:TIGR04406 156 FILLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEI 222
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
530-741 |
9.30e-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: 119.52 E-value: 9.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRrRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH--DVLFDNLTVAEHLYFYAQLKGLSLQKcpEEVKQMLHILSLEDkrDLRSKF---LSGGMKRKLSIGIALIAGS 683
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRILAEPLRIHGLPDRE--ERIAELLEQVGLPP--SFLDRYphqLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKdlREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
530-746 |
1.07e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 120.54 E-value: 1.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ---DMAQIR 605
Cdd:PRK13637 3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLC---PQHDvLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHI--LSLEDKRDlRSKF-LSGGMKRKLSIGIAL 679
Cdd:PRK13637 83 KKVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIvgLDYEDYKD-KSPFeLSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
549-740 |
1.08e-29 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 118.93 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQ--IRKSLGLCPQHDVLFDNLTVAEH 626
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHriARLGIGYVPEGRRIFPSLTVEEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LyfyaQLkGLSLQKCPEEVKQML-HILS----LEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:COG0410 99 L----LL-GAYARRDRAEVRADLeRVYElfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 702 AIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:COG0410 174 EIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1383-1599 |
1.11e-29 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 118.88 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIsSDIGKVRQRMGYCP 1462
Cdd:cd03300 3 LENVSKFYGGF---VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1463 QFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPS 1542
Cdd:cd03300 79 QNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1543 TGMDPVARR-LLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:cd03300 159 GALDLKLRKdMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPE 216
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
530-741 |
1.34e-29 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 121.72 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:COG1135 2 IELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKV 685
Cdd:COG1135 82 RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 686 LMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG1135 162 LLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1383-1688 |
1.49e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 121.35 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYD--QRAPLL----------------AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG 1444
Cdd:COG4586 4 VENLSKTYRvyEKEPGLkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1445 YSIS-------SDIGKVrqrMGycpQFDALLDHMTGREMLVMYARLRGIPERLINACVEnTLRGLL-LEPHANKLVktys 1516
Cdd:COG4586 84 YVPFkrrkefaRRIGVV---FG---QRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLD-ELVELLdLGELLDTPV---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1517 ggnkRKLSTG--------IALIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:COG4586 153 ----RQLSLGqrmrcelaAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVIVI 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1588 VQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQDALEEFKAFVDLTFPGSILEDEHQDMVHyhlpgcdlswakvfGILE 1667
Cdd:COG4586 229 DHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRGGEVIEREGNRVRLEVDPRESLA--------------EVLA 294
|
330 340
....*....|....*....|.
gi 569000489 1668 KAKEKYGVDDYSVSQISLEQV 1688
Cdd:COG4586 295 RLLARYPVRDLTIEEPPIEEV 315
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1381-1591 |
1.60e-29 |
|
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: 117.98 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYD-QRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS--SDIGKV--- 1454
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEEcEALCTRLAIMVQGQ 1591
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
531-745 |
2.17e-29 |
|
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: 116.38 E-value: 2.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSkvfqVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLG 609
Cdd:cd03214 1 EVENLS----VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LcpqhdvlfdnltvaehlyfyaqlkglslqkcpeeVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03214 77 Y----------------------------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCG 745
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
549-741 |
2.35e-29 |
|
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: 116.97 E-value: 2.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQdmAQIRKSLGLCPQH--DVLFDNlTVAEH 626
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--KERRKSIGYVMQDvdYQLFTD-SVREE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYFYAQLKGLSlqkcPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDL 706
Cdd:cd03226 93 LLLGLKELDAG----NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGEL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 707 LQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03226 169 IRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1381-1587 |
3.19e-29 |
|
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: 117.19 E-value: 3.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQ-RAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSdigkVRQRMG 1459
Cdd:cd03293 1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 1540 EPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
559-734 |
4.79e-29 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 126.39 E-value: 4.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 559 GQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI-SQDMAqIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLS 637
Cdd:NF033858 292 GEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdAGDIA-TRRRVGYMSQAFSLYGELTVRQNLELHARLFHLP 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 638 LQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDR-T 715
Cdd:NF033858 371 AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIElSREDGvT 450
|
170
....*....|....*....
gi 569000489 716 VLLTTHFMDEAdLLGDRIA 734
Cdd:NF033858 451 IFISTHFMNEA-ERCDRIS 468
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
549-739 |
6.24e-29 |
|
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: 116.09 E-value: 6.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDmaqiRKSLGLCPQH-DVLFD-NLTVAE- 625
Cdd:cd03235 15 LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQRrSIDRDfPISVRDv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 -------HLYFYAQLKglslQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAV 698
Cdd:cd03235 91 vlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 699 SRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:cd03235 167 TQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1381-1591 |
7.71e-29 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 114.59 E-value: 7.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG---YSISSDIGKVRQR 1457
Cdd:cd03229 1 LELKNVSKRYGQK---TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGedlTDLEDELPPLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGRemlvmyarlrgiperlinacvENTLRGLllephanklvktySGGNKRKLSTGIALIGEPAVIF 1537
Cdd:cd03229 78 IGMVFQDFALFPHLTVL---------------------ENIALGL-------------SGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1538 LDEPSTGMDPVARRLLWDTVARARE-SGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
529-746 |
8.23e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 117.92 E-value: 8.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 529 GIKIKHLSKVFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-----QDMA 602
Cdd:PRK13649 2 GINLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 603 QIRKSLGLCPQ--HDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIAL 679
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKNPFeLSGGQMRRVAIAGIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13649 161 AMEPKILVLDEPTAGLDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGK 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
530-740 |
1.03e-28 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 116.51 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:cd03256 1 IEVENLSKTY---PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEH-----LYFYAQLKGLSLQKCPEEVKQMLHILS---LEDKRDLRSKFLSGGMKRKLSIGI 677
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGLFPKEEKQRALAALErvgLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 678 ALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRinREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1381-1599 |
1.48e-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: 116.30 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMG 1459
Cdd:COG1120 2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREmLVMYAR------LRGIPERLINAcVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEP 1533
Cdd:COG1120 79 YVPQEPPAPFGLTVRE-LVALGRyphlglFGRPSAEDREA-VEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1398-1590 |
1.81e-28 |
|
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: 115.51 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYC-PQFDALLDHMTGREM 1476
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*
gi 569000489 1557 VARA-RESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:cd03267 196 LKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKG 230
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
530-741 |
1.82e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 118.36 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHdvlFdNL----TVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIA 681
Cdd:PRK11153 82 RQIGMIFQH---F-NLlssrTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 682 GSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK11153 158 NPKVLLCDEATSALDPATTRSILELLKDinRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1399-1543 |
2.06e-28 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 112.36 E-value: 2.06e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGK-VRQRMGYCPQFDALLDHMTGREML 1477
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKsLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRGIPERLINACVENTLRGLLLEPHANKLV----KTYSGGNKRKLSTGIALIGEPAVIFLDEPST 1543
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVgerpGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
530-741 |
3.38e-28 |
|
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: 114.74 E-value: 3.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKvfqvgNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqDMAQIRKSLG 609
Cdd:cd03299 1 LKVENLSK-----DWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDIS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQ---MLHILSLEDKRDLRskfLSGGMKRKLSIGIALIAGSKVL 686
Cdd:cd03299 75 YVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEiaeMLGIDHLLNRKPET---LSGGEQQRVAIARALVVNPKIL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03299 152 LLDEPFSALDVRTKEKLREELKkiRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
549-741 |
3.61e-28 |
|
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: 114.22 E-value: 3.61e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLF-----DNLT 622
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFygtlrDNIT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VA------EHLYFYAQLKGLS--LQKCPeevkqmlHILSLEDKRdlRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSG 694
Cdd:cd03245 100 LGapladdERILRAAELAGVTdfVNKHP-------NGLDLQIGE--RGRGLSGGQRQAVALARALLNDPPILLLDEPTSA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 695 MDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLgDRIAILAKGEL 741
Cdd:cd03245 171 MDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
549-746 |
3.98e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 114.83 E-value: 3.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQI------RKSlglcpQHDVLFDNL 621
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGlDEHEIarlgigRKF-----QKPTVFEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYF-YAQLKGL--SL-----QKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:COG4674 101 TVFENLELaLKGDRGVfaSLfarltAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVA 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 694 GMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG4674 181 GMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1365-1601 |
8.29e-28 |
|
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: 120.01 E-value: 8.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1365 RSRILVPSLDSMLDTPLI-INELSKVYDQRAP--LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAF 1441
Cdd:COG1123 244 GAARGRAAPAAAAAEPLLeVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSIL 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1442 VGGYSIS----SDIGKVRQRMGYCPQ--FDALLDHMTGREMLVMYARLRGI-PERLINACVENTLR--GLLLEpHANKLV 1512
Cdd:COG1123 324 FDGKDLTklsrRSLRELRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLErvGLPPD-LADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1513 KTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVAR----RLLWDtvaRARESGKAIVITSHSMEECEALCTRLAIMV 1588
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQaqilNLLRD---LQRELGLTYLFISHDLAVVRYIADRVAVMY 479
|
250
....*....|...
gi 569000489 1589 QGQFKCLGSPQHL 1601
Cdd:COG1123 480 DGRIVEDGPTEEV 492
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1383-1591 |
8.38e-28 |
|
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: 113.37 E-value: 8.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVY-DQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV----RQR 1457
Cdd:cd03257 4 VKNLSVSFpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQ--FDALLDHMTGREML--VMYARLRGIPERLINACVENTLRGLLLEP-HANKLVKTYSGGNKRKLSTGIALIGE 1532
Cdd:cd03257 84 IQMVFQdpMSSLNPRMTIGEQIaePLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1533 PAVIFLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
530-746 |
1.14e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.73 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-----QDMAQ 603
Cdd:PRK13634 3 ITFQKVEHRYQYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IRKSLGLC---PQHDvLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIAL 679
Cdd:PRK13634 83 LRKKVGIVfqfPEHQ-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFeLSGGQMRRVAIAGVL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDL---LQQQKsDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMfykLHKEK-GLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
551-742 |
1.15e-27 |
|
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: 112.39 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNL---YEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGY-----EISQDMAQIRKSLGLCPQHDVLFDNLT 622
Cdd:cd03297 12 DFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VAEHLYF-YAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:cd03297 92 VRENLAFgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQ---LSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000489 702 AIWDLLQQQKSD--RTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:cd03297 169 QLLPELKQIKKNlnIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
530-741 |
2.30e-27 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 111.47 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI---SQDMAQIRK 606
Cdd:cd03262 1 IEIKNLHKSF----GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 607 SLGLCPQHDVLFDNLTVAEHLYFyAQLK--GLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:cd03262 77 KVGMVFQQFNLFPHLTVLENITL-APIKvkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDlAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1381-1601 |
2.80e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 115.17 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDIGKV--RQR- 1457
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLppKDRn 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIF 1537
Cdd:COG3839 77 IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1538 LDEPSTGMDPVARrllwdTVARA------RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:COG3839 157 LDEPLSNLDAKLR-----VEMRAeikrlhRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1376-1601 |
7.02e-27 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 114.04 E-value: 7.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDIGKV- 1454
Cdd:COG3842 1 MAMPALELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLp 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 -RQR-MGYCPQFDALLDHMTGREMlVMYA-RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNK------Rklst 1525
Cdd:COG3842 74 pEKRnVGMVFQDYALFPHLTVAEN-VAFGlRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQqrvalaR---- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1526 giALIGEPAVIFLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:COG3842 149 --ALAPEPRVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
530-747 |
1.13e-26 |
|
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: 110.44 E-value: 1.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:TIGR04406 2 LVAENLIKSY----KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 L--CPQHDVLFDNLTVAEHLYFYAQL-KGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:TIGR04406 78 IgyLPQEASIFRKLTVEENIMAVLEIrKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 687 MLDEPTSGMDAVsrrAIWDLLQQQKSDRT----VLLTTHFMDEADLLGDRIAILAKGELQCCGSS 747
Cdd:TIGR04406 158 LLDEPFAGVDPI---AVGDIKKIIKHLKErgigVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
549-746 |
1.15e-26 |
|
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: 117.17 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFdNLTVAEHL 627
Cdd:COG4988 353 LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAWVPQNPYLF-AGTIRENL 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAqlKGLSlqkcPEEVKQMLH-------ILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:COG4988 432 RLGR--PDAS----DEELEAALEaagldefVAALPDGLDTplgeGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLD 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 697 AVSRRAIWDLLQQQKSDRTVLLTTHfmDEADL-LGDRIAILAKGELQCCGS 746
Cdd:COG4988 506 AETEAEILQALRRLAKGRTVILITH--RLALLaQADRILVLDDGRIVEQGT 554
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1402-1603 |
1.86e-26 |
|
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: 109.06 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIgkVRQRMGYCPQFDALLDHMTGREML 1477
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlpphER--ARAGIGYVPEGRRIFPELTVEENL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRGIPERlinacvENTLRGLL-----LEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRL 1552
Cdd:cd03224 97 LLGAYARRRAKR------KARLERVYelfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1553 LWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:cd03224 171 IFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1383-1601 |
1.89e-26 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 109.59 E-value: 1.89e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLL-AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKVRQR 1457
Cdd:cd03258 4 LKNVSKVFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGREMlVMYA-RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFEN-VALPlEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1537 FLDEPSTGMDPVARR----LLWDTvarARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:cd03258 163 LCDEATSALDPETTQsilaLLRDI---NRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
530-741 |
3.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 110.30 E-value: 3.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI-----SQDMAQ 603
Cdd:PRK13641 3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IRKSLGLCPQ--HDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIALI 680
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFeLSGGQMRRVAIAGVMA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDyQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
530-740 |
4.34e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.41 E-value: 4.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKD-KMGIRDLTLNLYEGQ-ITVLlGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--------- 598
Cdd:COG1101 2 LELKNLSKTFNPGTVNeKRALDGLNLTIEEGDfVTVI-GSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 599 ------QDMaqirkSLGLCPqhdvlfdNLTVAEHL---YFYAQLKGLSL---QKCPEEVKQMLHILS--LEDKRDLRSKF 664
Cdd:COG1101 81 yigrvfQDP-----MMGTAP-------SMTIEENLalaYRRGKRRGLRRgltKKRRELFRELLATLGlgLENRLDTKVGL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 665 LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:COG1101 149 LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1399-1591 |
4.98e-26 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 106.87 E-value: 4.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG--EETITSGDAFVGGYSISSDigKVRQRMGYCPQFDALLDHMTGREM 1476
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKR--SFRKIIGYVPQDDILHPTLTVRET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGIperlinacventlrglllephanklvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:cd03213 103 LMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1557 VARARESGKAIVITSHS-MEECEALCTRLAIMVQGQ 1591
Cdd:cd03213 154 LRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
529-739 |
5.60e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 111.39 E-value: 5.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 529 GIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDM-AQIRKs 607
Cdd:COG1118 2 SIEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLpPRERR- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDVLFDNLTVAEHLYFyaqlkGLSLQKCPEE-----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAG 682
Cdd:COG1118 77 VGFVFQHYALFPHMTVAENIAF-----GLRVRPPSKAeirarVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 683 SKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRlhDELGGTTVFVTHDQEEALELADRVVVMNQG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1379-1613 |
6.86e-26 |
|
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: 114.23 E-value: 6.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLI-INELSKVYDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG---EETITSGDAFVGGYSISSDIGKV 1454
Cdd:COG1123 2 TPLLeVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 R-QRMGYCPQ-FDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGE 1532
Cdd:COG1123 81 RgRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1533 PAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLkskFGSGYSL 1611
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI---LAAPQAL 237
|
..
gi 569000489 1612 QA 1613
Cdd:COG1123 238 AA 239
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1384-1572 |
8.35e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 107.36 E-value: 8.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1384 NELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG---EETITSGDAFVGGYSISsdIGKVRQRMGY 1460
Cdd:cd03234 8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRK--PDQFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRG---IPERLINACVENT-LRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRLprkSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARARESGKAIVITSH 1572
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
549-739 |
1.02e-25 |
|
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: 107.55 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDmaqirkslglCPQHDVLFDN------LT 622
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP----------GPDRMVVFQNysllpwLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VAEHLYFY--AQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR 700
Cdd:TIGR01184 71 VRENIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569000489 701 RAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:TIGR01184 151 GNLQEELMQiwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1375-1587 |
1.29e-25 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 107.87 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1375 SMLDTPLIINELSKVYDQR-APLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISsdigK 1453
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGgGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1454 VRQRMGYCPQFDALLDHMTGRE--MLVMyaRLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKlsTGIA--L 1529
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDnvALGL--ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQR--VAIAraL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1530 IGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:COG1116 154 ANDPEVLLMDEPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1387-1575 |
1.29e-25 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 106.68 E-value: 1.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1387 SKVYDQRAPllAVDRISLAVQKGE-CFgLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKVRQRMGYC 1461
Cdd:COG2884 8 SKRYPGGRE--ALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQfDA-LLDHMTGRE--MLVMyaRLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKlsTGI--ALIGEPAVI 1536
Cdd:COG2884 85 FQ-DFrLLPDRTVYEnvALPL--RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQR--VAIarALVNRPELL 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSME 1575
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1383-1587 |
1.35e-25 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 106.46 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYsissDIGKVRQRMGYCP 1462
Cdd:cd03235 2 VEDLTVSYGGH---PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1463 QFdALLDH---MTGREMLVM----YARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAV 1535
Cdd:cd03235 75 QR-RSIDRdfpISVRDVVLMglygHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
549-725 |
1.61e-25 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 107.48 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSG-HAYIHGYEISQ-DMAQIRKSLGLC-PQ-HDVLFDNLTVA 624
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGeDVWELRKRIGLVsPAlQLRFPRDETVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHLY--FYAQLkGLSlQKCPEE----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAV 698
Cdd:COG1119 99 DVVLsgFFDSI-GLY-REPTDEqrerARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLG 176
|
170 180
....*....|....*....|....*....
gi 569000489 699 SRRAIWDLLQQ--QKSDRTVLLTTHFMDE 725
Cdd:COG1119 177 ARELLLALLDKlaAEGAPTLVLVTHHVEE 205
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1381-1601 |
1.83e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 106.90 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGeetITSGDAfvGGYSI-SSDIG------K 1453
Cdd:PRK10895 4 LTAKNLAKAYKGRR---VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG---IVPRDA--GNIIIdDEDISllplhaR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1454 VRQRMGYCPQFDALLDHMTGREMLVMYARLRgipERLINACVENTLRGLLLEPHA----NKLVKTYSGGNKRKLSTGIAL 1529
Cdd:PRK10895 76 ARRGIGYLPQEASIFRRLSVYDNLMAVLQIR---DDLSAEQREDRANELMEEFHIehlrDSMGQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1530 IGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1402-1592 |
2.12e-25 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 105.67 E-value: 2.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALLDHMTGREMLVMY 1480
Cdd:COG4619 19 VSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAYVPQ-EPALWGGTVRDNLPFP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1481 ARLRGI---PERLINAcventLRGLLLEPHA-NKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:COG4619 98 FQLRERkfdRERALEL-----LERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRRVEEL 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000489 1557 VAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:COG4619 173 LREyLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
530-746 |
2.24e-25 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.04 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKsLG 609
Cdd:PRK09452 15 VELRGISKSFD----GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH-VN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFyaqlkGLSLQKCPEE-----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:PRK09452 90 TVFQSYALFPHMTVFENVAF-----GLRMQKTPAAeitprVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKalQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1381-1617 |
3.32e-25 |
|
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: 106.43 E-value: 3.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLL-AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV-RQRM 1458
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 GYCPQ--FDALLDHMTGREMLVMYARLRGIP---ERLINACVENTLRGLLLE--PHanKLvktySGGNKRKLSTGIALIG 1531
Cdd:COG1124 82 QMVFQdpYASLHPRHTVDRILAEPLRIHGLPdreERIAELLEQVGLPPSFLDryPH--QL----SGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1532 EPAVIFLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYS 1610
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
....*....
gi 569000489 1611 --LQAKVRS 1617
Cdd:COG1124 236 reLLAASLA 244
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
551-741 |
3.96e-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: 105.18 E-value: 3.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS----QDMAQIRKSLGLCPQHDVLFDNLTVAEH 626
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIGVVFQDFRLLPDRNVYEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDL 706
Cdd:cd03292 99 VAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNL 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 707 LQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03292 179 LKKiNKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
530-745 |
6.35e-25 |
|
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: 104.92 E-value: 6.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF------------------QVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY 591
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 592 IHGyeisQDMAQIRKSLGLCPqhdvlfdNLTVAEHLYFYAQLKGLSlqkcPEEVKQMLH-ILS---LEDKRDLRSKFLSG 667
Cdd:cd03220 81 VRG----RVSSLLGLGGGFNP-------ELTGRENIYLNGRLLGLS----RKEIDEKIDeIIEfseLGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 668 GMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGELQCCG 745
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQgKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
547-746 |
8.14e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 108.97 E-value: 8.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 547 MGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQI-RKSLGLCPQHDVLFDNL 621
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVrRKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 702 AIWDLL--QQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK10070 202 EMQDELvkLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGT 248
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
530-742 |
3.97e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 104.04 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQD-MAQIRKSL 608
Cdd:PRK13650 5 IEVKNLTFKYK-EDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:PRK13650 84 GMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 688 LDEPTSGMDAVSRRaiwDLLQQQKSDR-----TVLLTTHFMDEAdLLGDRIAILAKGELQ 742
Cdd:PRK13650 164 LDEATSMLDPEGRL---ELIKTIKGIRddyqmTVISITHDLDEV-ALSDRVLVMKNGQVE 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
529-746 |
4.16e-24 |
|
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: 102.80 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 529 GIKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKsL 608
Cdd:cd03296 2 SIEVRNVSKRFG----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-V 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNLTVAEHLYFyaqlkGLSLQKCPEE---------VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIAL 679
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAF-----GLRVKPRSERppeaeirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELRRWLRRlhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
530-741 |
4.63e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 103.94 E-value: 4.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMA-QIRKSL 608
Cdd:PRK13635 6 IRVEHIS--FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwDVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:PRK13635 84 GMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEAdLLGDRIAILAKGEL 741
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQlkEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
530-762 |
9.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 103.32 E-value: 9.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-----QDMAQ 603
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IRKSLGLCPQ--HDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLhiLSLEDKRDLRSKF---LSGGMKRKLSIGIA 678
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLL--MDLGFSRDVMSQSpfqMSGGQMRKIAIVSI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 679 LIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL--QCCGSSLFLKQKY 754
Cdd:PRK13646 160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKslQTDENKTIILVSHDMNEVARYADEVIVMKEGSIvsQTSPKELFKDKKK 239
|
....*...
gi 569000489 755 GAGYHMTL 762
Cdd:PRK13646 240 LADWHIGL 247
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
543-741 |
1.00e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 102.85 E-value: 1.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 543 NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQD---MAQIRKSLGLCPQH--DVL 617
Cdd:PRK13639 12 PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNpdDQL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 618 FDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA 697
Cdd:PRK13639 92 FAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 698 VSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK13639 171 MGASQIMKLLYDlNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
530-741 |
1.14e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.04 E-value: 1.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnkdkmG----IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqdmaqir 605
Cdd:cd03216 1 LELRGITKRF--------GgvkaLDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 kslGLCPQHdvlfdnltvaehlyfyAQLKGLSLqkcpeeVKQmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKV 685
Cdd:cd03216 66 ---FASPRD----------------ARRAGIAM------VYQ-----------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 686 LMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03216 104 LILDEPTAALTPAEVERLFKVIRRLRAQgVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
530-741 |
1.37e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 102.52 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIRKSL 608
Cdd:PRK13648 8 IVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:PRK13648 86 GIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEAdLLGDRIAILAKGEL 741
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1379-1591 |
1.59e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 101.70 E-value: 1.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIinELSKV---YDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSG-DAFV-----GGYSISs 1449
Cdd:COG1119 1 DPLL--ELRNVtvrRGGK-TIL--DDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfgerrGGEDVW- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 digKVRQRMGYC-PQF-DALLDHMTGREMLV--MYA---RLRGIPERLINAcVENTLRGLLLEPHANKLVKTYSGGNKRK 1522
Cdd:COG1119 75 ---ELRKRIGLVsPALqLRFPRDETVLDVVLsgFFDsigLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1523 LSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:COG1119 151 VLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
530-746 |
1.75e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 101.31 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGI------------------RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY 591
Cdd:COG1134 5 IEVENVSKSYRLYHEPSRSLkelllrrrrtrreefwalKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 592 IHGyEISqdmAQIRKSLGLCPQhdvlfdnLTVAEHLYFYAQLKGLSlqkcPEEVKQML-HILS---LEDKRDLRSKFLSG 667
Cdd:COG1134 85 VNG-RVS---ALLELGAGFHPE-------LTGRENIYLNGRLLGLS----RKEIDEKFdEIVEfaeLGDFIDQPVKTYSS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 668 GMKRKLSIGIALIAGSKVLMLDEPTSGMDAV-SRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG1134 150 GMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1386-1599 |
1.83e-23 |
|
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: 101.26 E-value: 1.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDigKVRQR-MGYCPQF 1464
Cdd:cd03296 8 VSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV--PVQERnVGFVFQH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DALLDHMTGREM----LVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03296 83 YALFRHMTVFDNvafgLRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1541 PSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:cd03296 163 PFGALDAKVRKELRRWLRRLHdELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPD 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1389-1601 |
2.68e-23 |
|
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: 101.57 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1389 VYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIGKVR-QRMGYCPQ 1463
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkELRELRrKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1464 FDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPST 1543
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFS 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1544 GMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:cd03294 190 ALDPLIRREMQDELLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1374-1591 |
3.01e-23 |
|
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: 100.44 E-value: 3.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1374 DSMLDtpliINELSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS---- 1449
Cdd:COG0410 1 MPMLE----VENLHAGYGG---IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpph 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 DIgkVRQRMGYCPQFDALLDHMTGREMLVMYARLRGIPERlinacVENTLRGLL-----LEPHANKLVKTYSGGNKRKLS 1524
Cdd:COG0410 74 RI--ARLGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAE-----VRADLERVYelfprLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1525 TGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
551-767 |
4.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 101.35 E-value: 4.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQ-----IRKSLGLCPQ--HDVLFDNlTV 623
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeikpVRKKVGVVFQfpESQLFEE-TV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRA 702
Cdd:PRK13643 103 LKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFeLSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 703 IWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCG--SSLFLKQKYGAGYHMTLVKEPH 767
Cdd:PRK13643 183 MMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGtpSDVFQEVDFLKAHELGVPKATH 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1379-1610 |
4.59e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 103.38 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLI-INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIsSDIGKVRQR 1457
Cdd:PRK11607 17 TPLLeIRNLTKSFDGQH---AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIF 1537
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1538 LDEPSTGMDPVAR-RLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYS 1610
Cdd:PRK11607 173 LDEPMGALDKKLRdRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
527-746 |
5.28e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 5.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 527 VAGIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--QDMAQI 604
Cdd:PRK10895 1 MATLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSLGLCPQHDVLFDNLTVAEHLYFYAQL-KGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGS 683
Cdd:PRK10895 77 RRGIGYLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHlRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1398-1598 |
7.16e-23 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.39 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGySISS--DIGkvrqrMGYCPQfdalldhMTGRE 1475
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAllELG-----AGFHPE-------LTGRE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1476 MLVMYARLRGIPERLINACV-------EntlrgllLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP-STGmDP 1547
Cdd:COG1134 108 NIYLNGRLLGLSRKEIDEKFdeivefaE-------LGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVlAVG-DA 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1548 VARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:COG1134 180 AFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1379-1591 |
8.06e-23 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 98.96 E-value: 8.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLI-INELSKVYDQ-RAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIG 1452
Cdd:COG1136 2 SPLLeLRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1453 KVR-QRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIG 1531
Cdd:COG1136 82 RLRrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1532 EPAVIFLDEPsTG-MDPVARRLLWDTVAR-ARESGKAIVITSHSmEECEALCTRLAIMVQGQ 1591
Cdd:COG1136 162 RPKLILADEP-TGnLDSKTGEEVLELLRElNRELGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
523-741 |
1.00e-22 |
|
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: 98.70 E-value: 1.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 523 PEDLVAGIKIKHLSkvFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-D 600
Cdd:cd03248 5 PDHLKGIVKFQNVT--FAYPTRpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLCPQHDVLFDNlTVAEHLYFyaqlkglSLQKCP-EEVK---QMLH----ILSLEDKRDL----RSKFLSGG 668
Cdd:cd03248 83 HKYLHSKVSLVGQEPVLFAR-SLQDNIAY-------GLQSCSfECVKeaaQKAHahsfISELASGYDTevgeKGSQLSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 669 MKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADlLGDRIAILAKGEL 741
Cdd:cd03248 155 QKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
530-736 |
1.04e-22 |
|
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: 100.90 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP---TSGHAYIHGYEISQ----DMA 602
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 603 QIR-KSLGLCPQhdvlfD-----N--LTVAEHLY-FYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF---LSGGMK 670
Cdd:COG0444 82 KIRgREIQMIFQ-----DpmtslNpvMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYpheLSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 671 RKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHfmdeaDL-----LGDRIAIL 736
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKdlQRELGLAILFITH-----DLgvvaeIADRVAVM 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
530-746 |
1.41e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 99.03 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:COG4559 2 LEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwspwELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 kslGLCPQHDVL-FDnLTVAE--------HLYFYAQLKGLslqkcPEEVKQMLHILSLEDkRDLRSkfLSGGMKRKLSIG 676
Cdd:COG4559 78 ---AVLPQHSSLaFP-FTVEEvvalgrapHGSSAAQDRQI-----VREALALVGLAHLAG-RSYQT--LSGGEQQRVQLA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 677 IALI-------AGSKVLMLDEPTSGMdavsrraiwDLLQQQKSDR----------TVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:COG4559 146 RVLAqlwepvdGGPRWLFLDEPTSAL---------DLAHQHAVLRlarqlarrggGVVAVLHDLNLAAQYADRILLLHQG 216
|
....*..
gi 569000489 740 ELQCCGS 746
Cdd:COG4559 217 RLVAQGT 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1380-1599 |
1.42e-22 |
|
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: 103.73 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1380 PLI-INELSKVY--DQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKML-------TGEETITSGDAFVGGYSISS 1449
Cdd:TIGR03269 278 PIIkVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIagvleptSGEVNVRVGDEWVDMTKPGP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 DI-GKVRQRMGYCPQFDALLDHMT---------GREMLVMYARLRGIPERLINACVENTLRGLLlephaNKLVKTYSGGN 1519
Cdd:TIGR03269 358 DGrGRAKRYIGILHQEYDLYPHRTvldnlteaiGLELPDELARMKAVITLKMVGFDEEKAEEIL-----DKYPDELSEGE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1520 KRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
.
gi 569000489 1599 Q 1599
Cdd:TIGR03269 513 E 513
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
530-739 |
2.07e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 2.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQ-IRKSL 608
Cdd:PRK13647 5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQ--HDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:PRK13647 82 GLVFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEG 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
543-721 |
2.80e-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: 97.30 E-value: 2.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 543 NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFdNL 621
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLF-SG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYF---YAQLKglSLQKCPEEVKQMLHILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSG 694
Cdd:cd03254 92 TIMENIRLgrpNATDE--EVIEAAKEAGAHDFIMKLPNGYDTvlgeNGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180
....*....|....*....|....*..
gi 569000489 695 MDAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAH 196
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
551-746 |
2.88e-22 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 100.57 E-value: 2.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyEISQDMAQI------RKSLGLCPQHDVLFDNLTVA 624
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDSRKGiflppeKRRIGYVFQEARLFPHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHL-YFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:TIGR02142 94 GNLrYGMKRARPSERRISFERVIELLGIGHLLGRLPGR---LSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 704 WDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:TIGR02142 171 LPYLERlhAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1383-1591 |
3.03e-22 |
|
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: 97.64 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGK----VRQRM 1458
Cdd:cd03256 3 VENLSKTYPNGKK--ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 GYCPQFDALLDHMTGREMlVMYARL----------RGIPERLINACVENtLRGLLLEPHANKLVKTYSGGNKRKLSTGIA 1528
Cdd:cd03256 81 GMIFQQFNLIERLSVLEN-VLSGRLgrrstwrslfGLFPKEEKQRALAA-LERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRiNREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
530-746 |
3.26e-22 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.16 E-value: 3.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgNKDKMgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKsLG 609
Cdd:PRK10851 3 IEIANIKKSF---GRTQV-LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK-VG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFyaQLKGLSLQKCP------EEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGS 683
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIAF--GLTVLPRRERPnaaaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQlhEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
530-746 |
3.33e-22 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 97.78 E-value: 3.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvfqVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMA-QIRKSL 608
Cdd:PRK11231 3 LRTENLT----VGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNLTVAEhLYFYAQLKGLSL-----QKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGS 683
Cdd:PRK11231 79 ALLPQHHLTPEGITVRE-LVAYGRSPWLSLwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK11231 158 PVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1398-1591 |
3.46e-22 |
|
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: 96.83 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGySISSDIGkvrqrMGYcpqfdALLDHMTGREML 1477
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLG-----LGG-----GFNPELTGRENI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP-STG----MDPVARRL 1552
Cdd:cd03220 106 YLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVlAVGdaafQEKCQRRL 185
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 1553 lwdtvARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03220 186 -----RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGK 219
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1383-1591 |
3.53e-22 |
|
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: 96.87 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG-----EETITSGDAFVGG---YSISSDIGKV 1454
Cdd:cd03260 3 LRDLNVYYGDKH---ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGkdiYDLDVDVLEL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQFDALLdHMTGREMLVMYARLRGI-PERLINACVENTLRGLLL------EPHANKLvktySGGNKRKLSTGI 1527
Cdd:cd03260 80 RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwdevkdRLHALGL----SGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1528 ALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESgKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
543-741 |
4.15e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 98.24 E-value: 4.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 543 NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--QDMAQIRKSLGLCPQHDvlfDN 620
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVFQNP---DN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 621 LTVA----EHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:PRK13633 97 QIVAtiveEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 697 AVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEAdLLGDRIAILAKGEL 741
Cdd:PRK13633 177 PSGRREVVNTIKElnKKYGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
551-746 |
4.30e-22 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 100.18 E-value: 4.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyEISQDMAQI------RKSLGLCPQHDVLFDNLTVA 624
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGG-EVLQDSARGiflpphRRRIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHLYF-----YAQLKGLSLqkcpEEVKQMLHILSLEDKRDLRskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:COG4148 96 GNLLYgrkraPRAERRISF----DEVVELLGIGHLLDRRPAT---LSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 700 RRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:COG4148 169 KAEILPYLERlrDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGP 217
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
549-736 |
4.48e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 95.76 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisqdmaqiRKSLGLCPQHDVLFDNL--TVAE- 625
Cdd:NF040873 8 LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG----------GARVAYVPQRSEVPDSLplTVRDl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 -------HLYFYAQLKGLSLQkcpeEVKQMLHILSLED--KRDLRSkfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:NF040873 78 vamgrwaRRGLWRRLTRDDRA----AVDDALERVGLADlaGRQLGE--LSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569000489 697 AVSRRAIWDLLQQQKSD-RTVLLTTHFMDEAdLLGDRIAIL 736
Cdd:NF040873 152 AESRERIIALLAEEHARgATVVVVTHDLELV-RRADPCVLL 191
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1383-1596 |
7.62e-22 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 94.42 E-value: 7.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYC 1461
Cdd:cd03214 2 VENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQFDALLDhmtgremlvmyarlrgiperlinacventlrgllLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:cd03214 79 PQALELLG----------------------------------LAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1542 STGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLG 1596
Cdd:cd03214 125 TSHLDIAHQIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
533-739 |
9.21e-22 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 94.62 E-value: 9.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 533 KHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLL-----TGLfppTSGHAYIHGYEISQDmaqIRKS 607
Cdd:cd03232 7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDKN---FQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKcpeevkqmlhilsledkrdlrskflsggmKRKLSIGIALIAGSKVLM 687
Cdd:cd03232 81 TGYVEQQDVHSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILF 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 688 LDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHfMDEADLLG--DRIAILAKG 739
Cdd:cd03232 132 LDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIH-QPSASIFEkfDRLLLLKRG 185
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
546-741 |
1.41e-21 |
|
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: 93.65 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 546 KMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHG--YEISQDMAQIRKSLGLCP---QHDVLFDN 620
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 621 LTVAEHLyfyaqlkglslqkcpeevkqmlhILSLedkrdlrskFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR 700
Cdd:cd03215 93 LSVAENI-----------------------ALSS---------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 701 RAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:cd03215 141 AEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
550-721 |
1.64e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 94.56 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHG--YEISQDMAQIRkSLGlcpQHDVLFDNLTVAEHL 627
Cdd:PRK13539 19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEACH-YLG---HRNAMKPALTVAENL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAQLKGLSlqkcPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL 707
Cdd:PRK13539 95 EFWAAFLGGE----ELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELI 170
|
170
....*....|....*
gi 569000489 708 Q-QQKSDRTVLLTTH 721
Cdd:PRK13539 171 RaHLAQGGIVIAATH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
549-760 |
1.73e-21 |
|
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: 95.37 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHL 627
Cdd:cd03253 17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND-TIGYNI 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YfYAQLKGlslqkCPEEV-----KQMLH--ILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:cd03253 96 R-YGRPDA-----TDEEVieaakAAQIHdkIMRFPDGYDTivgeRGLKLSGGEKQRVAIARAILKNPPILLLDEATSALD 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 697 AVSRRAIWDLLQQQKSDRTVLLTTH----FMDeadllGDRIAILAKGELQCCGSSLFLKQKYGAGYHM 760
Cdd:cd03253 170 THTEREIQAALRDVSKGRTTIVIAHrlstIVN-----ADKIIVLKDGRIVERGTHEELLAKGGLYAEM 232
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
530-746 |
1.75e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 96.41 E-value: 1.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY---IHGYEISQD-MAQIR 605
Cdd:PRK13640 6 VEFKHVS--FTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAKtVWDIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:PRK13640 84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADlLGDRIAILAKGELQCCGS 746
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLKKKNnlTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1398-1592 |
3.32e-21 |
|
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: 92.88 E-value: 3.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSISSDIGKVRQRMGYCPQfdalldhmtgre 1475
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAYVPE------------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1476 mlvmyarlrgipERLINACV------ENTLRGLLLephanklvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVA 1549
Cdd:cd03215 83 ------------DRKREGLVldlsvaENIALSSLL-----------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000489 1550 RRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:cd03215 140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1386-1591 |
3.64e-21 |
|
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: 92.11 E-value: 3.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSKVYdqrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISsdigkvrqrmgycpqFD 1465
Cdd:cd03216 6 ITKRF---GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS---------------FA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 ALLDhmtgremlvmyARLRGIperlinACVentlrglllephanklvktY--SGGNKRKLSTGIALIGEPAVIFLDEPST 1543
Cdd:cd03216 68 SPRD-----------ARRAGI------AMV-------------------YqlSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569000489 1544 GMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03216 112 ALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
549-746 |
3.92e-21 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 94.48 E-value: 3.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLF-----DNLT 622
Cdd:cd03252 18 LDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFnrsirDNIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VA------EHLYFYAQLKGLS--LQKCPEEVKQMLhilsledkrDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSG 694
Cdd:cd03252 98 LAdpgmsmERVIEAAKLAGAHdfISELPEGYDTIV---------GEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 695 MDAVSRRAIWDLLQQQKSDRTVLLTTHFMdEADLLGDRIAILAKGELQCCGS 746
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
530-739 |
4.53e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 4.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQirksLG 609
Cdd:PRK11248 2 LQISHLYADYG----GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11248 154 EPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
550-759 |
4.72e-21 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 97.02 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIhGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYF 629
Cdd:PRK11000 20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFI-GEKRMNDVPPAERGVGMVFQSYALYPHLSVAENMSF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 630 YAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA---VSRRA-IWD 705
Cdd:PRK11000 99 GLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAalrVQMRIeISR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 706 LlqQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLkqkygagYH 759
Cdd:PRK11000 179 L--HKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL-------YH 223
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
532-750 |
5.74e-21 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 96.71 E-value: 5.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKslgLC 611
Cdd:PRK11432 9 LKNITKRF----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRD---IC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 612 P--QHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:PRK11432 82 MvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 690 EPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS---------SLFL 750
Cdd:PRK11432 162 EPLSNLDANLRRSMREKIRelQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFM 233
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1398-1703 |
5.79e-21 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 96.73 E-value: 5.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAG--KTTTFKMLTGEETITSGDAFVggySISSDIGKVRQRMG-YCPQFDALLDHMTGR 1474
Cdd:NF000106 28 AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*---TWCANRRALRRTIG*HRPVR*GRRESFSGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLW 1554
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1555 DTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGsGYSLQAKVRSEGKQDALEEFKAFVDLT 1634
Cdd:NF000106 185 DEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMVGAIAQAGLD 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1635 FPGSILEDEHQDMVHYHLPGcDLSWAKVFGILekAKEKYGVDDYSVSQISLEQVFLSFAHLQPPTTEDG 1703
Cdd:NF000106 264 GIAGATADHEDGVVNVPIVS-DEQLSAVVGML--GERGFTISGHQHPSAQL*EVFLAITGQKTSEAADG 329
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
530-736 |
5.82e-21 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 98.55 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF---QVgnkdkmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHG--YEISQDMAQI 604
Cdd:COG1129 5 LEMRGISKSFggvKA-------LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSL---QKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIA 681
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 682 GSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAIL 736
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVL 213
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
549-760 |
6.77e-21 |
|
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: 93.76 E-value: 6.77e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHL 627
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 -Y--FYAQLkglslqkcpEEVKQM-----LH--ILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:cd03249 98 rYgkPDATD---------EEVEEAakkanIHdfIMSLPDGYDTlvgeRGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 694 GMDAVSRRAIWDLLQQQKSDRTVLLTTHfmdeaDLL----GDRIAILAKGELQCCGSSLFLKQKYGAGYHM 760
Cdd:cd03249 169 ALDAESEKLVQEALDRAMKGRTTIVIAH-----RLStirnADLIAVLQNGQVVEQGTHDELMAQKGVYAKL 234
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
530-741 |
6.97e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 98.56 E-value: 6.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQ--VGNKDkmgirdLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYE--ISQDMAQIR 605
Cdd:COG3845 6 LELRGITKRFGgvVANDD------VSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPvrIRSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYA-QLKGLSLQKcpEEVKQMLHILSledKR-----DLRSKF--LSGGMKRKLSIGI 677
Cdd:COG3845 80 LGIGMVHQHFMLVPNLTVAENIVLGLePTKGGRLDR--KAARARIRELS---ERygldvDPDAKVedLSVGEQQRVEILK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 678 ALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEgKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
530-721 |
8.35e-21 |
|
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: 93.06 E-value: 8.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:cd03251 1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFDNlTVAEHLYFYAqlkglsLQKCPEEVKQMLH-------ILSLEDKRDL----RSKFLSGGMKRKLSIGI 677
Cdd:cd03251 79 GLVSQDVFLFND-TVAENIAYGR------PGATREEVEEAARaanahefIMELPEGYDTvigeRGVKLSGGQRQRIAIAR 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569000489 678 ALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIAH 195
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
504-741 |
1.07e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 98.31 E-value: 1.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 504 EEEGSDPEKALrneyfeaEPEDLVAGIKIKHLSkvFQvGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLF 583
Cdd:COG1132 321 PPEIPDPPGAV-------PLPPVRGEIEFENVS--FS-YPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 584 PPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFdNLTVAEHLYFYAqlKGLSLqkcpEEVKQMLH-------ILSLE 655
Cdd:COG1132 391 DPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLF-SGTIRENIRYGR--PDATD----EEVEEAAKaaqahefIEALP 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 656 DKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTH------FMde 725
Cdd:COG1132 464 DGYDTvvgeRGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-- 541
|
250
....*....|....*.
gi 569000489 726 adllgDRIAILAKGEL 741
Cdd:COG1132 542 -----DRILVLDDGRI 552
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
564-797 |
1.40e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 93.71 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 564 LLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQH--DVLFDNlTVAEHLYFYAQLKGLSLQK 640
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKeNIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 641 CPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLL 718
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDlpETYGMTVIF 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 719 TTHFMDEADLLGDRIAILAKGELQCCGS--SLFLKQKYGAGYHMTLVKEPHCnpegISQLVHHHVPNAMLESHAGAELSF 796
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHLDLPSLPKL----IRSLQAQGIAIDMAYTYQEAEDAF 269
|
.
gi 569000489 797 I 797
Cdd:PRK13652 270 L 270
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
530-741 |
1.67e-20 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.45 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG 609
Cdd:cd03247 1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNlTVAEHLyfyaqlkglslqkcpeevkqmlhilsledkrdlrSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHfmdeaDLLG----DRIAILAKGEL 741
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTLIWITH-----HLTGiehmDKILFLENGKI 174
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
530-746 |
1.87e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.91 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:PRK13548 3 LEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLglcPQHDVL-FDnLTVAE--------HlyfyaqlkGLSLQKCPEEVKQMLHILSLED--KRDLRSkfLSGGMKRKLS 674
Cdd:PRK13548 79 AVL---PQHSSLsFP-FTVEEvvamgrapH--------GLSRAEDDALVAAALAQVDLAHlaGRDYPQ--LSGGEQQRVQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 675 IGIALI------AGSKVLMLDEPTSGMdavsrraiwDLLQQQKSDR-----------TVLLTTHFMDEADLLGDRIAILA 737
Cdd:PRK13548 145 LARVLAqlwepdGPPRWLLLDEPTSAL---------DLAHQHHVLRlarqlaherglAVIVVLHDLNLAARYADRIVLLH 215
|
....*....
gi 569000489 738 KGELQCCGS 746
Cdd:PRK13548 216 QGRLVADGT 224
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1383-1541 |
2.23e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 2.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAfvggySISSDIgkvrqRMGYCP 1462
Cdd:COG0488 1 LENLSKSFGGR-PLL--DDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----SIPKGL-----RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1463 QFDALLDHMTGREMLVM----------------------------YARLRGIPERL----INACVENTLRGL-LLEPHAN 1509
Cdd:COG0488 68 QEPPLDDDLTVLDTVLDgdaelraleaeleeleaklaepdedlerLAELQEEFEALggweAEARAEEILSGLgFPEEDLD 147
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1510 KLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:COG0488 148 RPVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
550-721 |
2.28e-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: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHLY 628
Cdd:TIGR02868 352 DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVRENLR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 FYAQlkglslQKCPEEVKQML-------HILSLEDKRDLR----SKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA 697
Cdd:TIGR02868 431 LARP------DATDEELWAALervgladWLRALPDGLDTVlgegGARLSGGERQRLALARALLADAPILLLDEPTEHLDA 504
|
170 180
....*....|....*....|....
gi 569000489 698 VSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:TIGR02868 505 ETADELLEDLLAALSGRTVVLITH 528
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
530-767 |
3.36e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 92.60 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI---SQDMAQIRK 606
Cdd:PRK13636 6 LKVEELNYNYSDGTH---ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 607 SLGLC---PQHDvLFdNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGS 683
Cdd:PRK13636 83 SVGMVfqdPDNQ-LF-SASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGE--LQCCGSSLFLKQKYGAGYH 759
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVemQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRviLQGNPKEVFAEKEMLRKVN 240
|
....*...
gi 569000489 760 MTLVKEPH 767
Cdd:PRK13636 241 LRLPRIGH 248
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
549-746 |
3.62e-20 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 91.02 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHL 627
Cdd:cd03244 20 LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFSG-TIRSNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLR----SKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:cd03244 99 DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVveegGENLSVGQRQLLCLARALLRKSKILVLDEATASVDPETDALI 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 704 WDLLQQQKSDRTVLLTTH----FMDEadllgDRIAILAKGELQCCGS 746
Cdd:cd03244 179 QKTIREAFKDCTVLTIAHrldtIIDS-----DRILVLDKGRVVEFDS 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
538-741 |
3.88e-20 |
|
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: 89.58 E-value: 3.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 538 VFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDV 616
Cdd:cd03246 7 SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 617 LFDNlTVAEHLyfyaqlkglslqkcpeevkqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:cd03246 87 LFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 697 AVSRRAIWDLLQQ-QKSDRTVLLTTHFMdEADLLGDRIAILAKGEL 741
Cdd:cd03246 129 VEGERALNQAIAAlKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1381-1591 |
4.45e-20 |
|
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: 88.98 E-value: 4.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMG 1459
Cdd:cd03228 1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQfDALLDHMTgremlvmyarLRgiperlinacvENTLrglllephanklvktySGGNKRKLStgIA--LIGEPAVIF 1537
Cdd:cd03228 80 YVPQ-DPFLFSGT----------IR-----------ENIL----------------SGGQRQRIA--IAraLLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1538 LDEPSTGMDPVARRLLWDTVARAREsGKAIVITSHSMEECEaLCTRLAIMVQGQ 1591
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1354-1611 |
4.67e-20 |
|
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: 96.37 E-value: 4.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1354 VLPEDQDVAEERSRILVPSldsmlDTPLIINELSKVYDQrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEE 1433
Cdd:COG4987 312 LLDAPPAVTEPAEPAPAPG-----GPSLELEDVSFRYPG-AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1434 TITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALLDHMTGREMLVMyARLRGIPERLINAC--------VENTLRGL-- 1502
Cdd:COG4987 386 DPQSGSITLGGVDLRDlDEDDLRRRIAVVPQ-RPHLFDTTLRENLRL-ARPDATDEELWAALervglgdwLAALPDGLdt 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1503 LLEPHANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARAREsGKAIVITSHSMEECEAlCT 1582
Cdd:COG4987 464 WLGEGGRRL----SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MD 537
|
250 260
....*....|....*....|....*....
gi 569000489 1583 RLAIMVQGQFKCLGSPQHLKSKFGSGYSL 1611
Cdd:COG4987 538 RILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
545-747 |
7.87e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 90.88 E-value: 7.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 545 DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP------PTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVL 617
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 618 FDNLTVAEHLYFYAQLKGL----SLQKCPEEVKQMLHIL-SLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIkekrEIKKIVEECLRKVGLWkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 693 SGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSS 747
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSS 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
530-745 |
8.45e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 95.24 E-value: 8.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNkdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIr 605
Cdd:PRK09700 6 ISMAGIGKSFGPVH----ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhkLAAQL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 kSLGLCPQHDVLFDNLTVAEHLYF----YAQLKGLSL---QKCPEEVKQMLHILSLedKRDLRSKF--LSGGMKRKLSIG 676
Cdd:PRK09700 81 -GIGIIYQELSVIDELTVLENLYIgrhlTKKVCGVNIidwREMRVRAAMMLLRVGL--KVDLDEKVanLSISHKQMLEIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 677 IALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGELQCCG 745
Cdd:PRK09700 158 KTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEgTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1381-1604 |
1.01e-19 |
|
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: 90.09 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQraplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISsDIGKVRQRMGY 1460
Cdd:cd03299 1 LKVENLSKDWKE----FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT-NLPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVI-TSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSK 1604
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
556-739 |
1.12e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 556 LYEGQITVLLGHNGAGKTTTMSLLTGLFPP---TSGHAYIHGYEIsqDMAQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQ 632
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEMRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 633 LK---GLSLQKCPEEVKQMLHILSLEDKRDL------RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSV 205
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 704 WDLLQQ-QKSDRTVLLTTHfMDEADL--LGDRIAILAKG 739
Cdd:TIGR00955 206 VQVLKGlAQKGKTIICTIH-QPSSELfeLFDKIILMAEG 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
530-740 |
1.13e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 92.98 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQdMAQIRKSLG 609
Cdd:PRK11607 20 LEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH-VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 690 EPTSGMDAVSRraiwDLLQQQKSD------RTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK11607 175 EPMGALDKKLR----DRMQLEVVDilervgVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1397-1593 |
1.47e-19 |
|
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: 88.85 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSdigKVRQRM-GYCPQ--FDALLDHMTG 1473
Cdd:cd03226 14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA---KERRKSiGYVMQdvDYQLFTDSVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1474 REMLVmyaRLRGIPERliNACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLL 1553
Cdd:cd03226 91 EELLL---GLKELDAG--NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERV 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 1554 WDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFK 1593
Cdd:cd03226 166 GELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
549-758 |
1.48e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 89.55 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQI-RKSLGLCPQHDVLFDNLTVAEH 626
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKImREAVAIVPEGRRVFSRMTVEEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LY---FYAqlkglSLQKCPEEVKQMLHIL-SLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRA 702
Cdd:PRK11614 101 LAmggFFA-----ERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQ 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 703 IWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGE--LQCCGSSLFLKQKYGAGY 758
Cdd:PRK11614 176 IFDTIEQLREQgMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGDALLANEAVRSAY 234
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1354-1611 |
1.62e-19 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 95.29 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1354 VLPEDQDVAEERSRILVPSLDSMLdtpliinELSKV---YDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLT 1430
Cdd:COG2274 451 ILDLPPEREEGRSKLSLPRLKGDI-------ELENVsfrYPGDSPP-VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLL 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1431 GEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALLDHMTGREMLVMYArlRGIP-ERLINAC--------VENTLR 1500
Cdd:COG2274 523 GLYEPTSGRILIDGIDLRQiDPASLRRQIGVVLQ-DVFLFSGTIRENITLGD--PDATdEEIIEAArlaglhdfIEALPM 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1501 GL--LLEPHANKLvktySGGNKRKLstGIA--LIGEPAVIFLDEPSTGMDPVARRLLWDTVARAREsGKAIVITSHSMeE 1576
Cdd:COG2274 600 GYdtVVGEGGSNL----SGGQRQRL--AIAraLLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-S 671
|
250 260 270
....*....|....*....|....*....|....*
gi 569000489 1577 CEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSL 1611
Cdd:COG2274 672 TIRLADRIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1381-1599 |
1.83e-19 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 91.75 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIgKVRQR-MG 1459
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNL-PPRERrVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMlVMYA-RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNK------RklstgiALIGE 1532
Cdd:COG1118 79 FVFQHYALFPHMTVAEN-IAFGlRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRqrvalaR------ALAVE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1533 PAVIFLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:COG1118 152 PEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPD 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
530-753 |
2.09e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 89.83 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgNKDKmGIRDLTLNLYEGQITVLLGHNGAGKTT---TMSLLTGLFP--PTSGHAYIHGYEI---SQDM 601
Cdd:PRK14239 6 LQVSDLSVYY---NKKK-ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIRKSLGLCPQHDVLFDnLTVAEHLYFYAQLKGL------------SLQKCP--EEVKQMLHILSLEdkrdlrskfLSG 667
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIkdkqvldeavekSLKGASiwDEVKDRLHDSALG---------LSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 668 GMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS- 746
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDt 231
|
....*...
gi 569000489 747 -SLFLKQK 753
Cdd:PRK14239 232 kQMFMNPK 239
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
523-760 |
2.28e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 94.79 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 523 PEDLVAGIKIKHLSkvFQVGNK-DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-D 600
Cdd:TIGR00958 472 PLNLEGLIEFQDVS--FSYPNRpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyD 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLCPQHDVLFdNLTVAEHLyfyaqlkGLSLQKCPEE----VKQMLH----ILSLEDKRDL----RSKFLSGG 668
Cdd:TIGR00958 550 HHYLHRQVALVGQEPVLF-SGSVRENI-------AYGLTDTPDEeimaAAKAANahdfIMEFPNGYDTevgeKGSQLSGG 621
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 669 MKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRaiwdLLQQQKS--DRTVLLTTHFMDEADlLGDRIAILAKGELQCCGS 746
Cdd:TIGR00958 622 QKQRIAIARALVRKPRVLILDEATSALDAECEQ----LLQESRSraSRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGT 696
|
250
....*....|....
gi 569000489 747 SLFLKQKYGAGYHM 760
Cdd:TIGR00958 697 HKQLMEDQGCYKHL 710
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
548-721 |
2.47e-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: 93.89 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 548 GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEH 626
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYFY------AQLKGLS----LQKCPEEVKQMLHILSLEDKRDLrskflSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:TIGR02857 416 IRLArpdasdAEIREALeragLDEFVAALPQGLDTPIGEGGAGL-----SGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180
....*....|....*....|....*
gi 569000489 697 AVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:TIGR02857 491 AETEAEVLEALRALAQGRTVLLVTH 515
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1385-1575 |
2.81e-19 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 88.23 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRAP-LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKVRQRMG 1459
Cdd:cd03292 2 EFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYLRRKIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:cd03292 82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1540 EPSTGMDPVARRLLWDTVARARESGKAIVITSHSME 1575
Cdd:cd03292 162 EPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKE 197
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1385-1601 |
3.31e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 88.61 E-value: 3.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI---SSDIGKVRQRMGYC 1461
Cdd:PRK09493 3 EFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQFDALLDHMTGREMlVMYA--RLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:PRK09493 83 FQQFYLFPHLTALEN-VMFGplRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1540 EPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1383-1638 |
3.49e-19 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.91 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQR-APLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIGKVRQR 1457
Cdd:COG1135 4 LENLSKTFPTKgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserELRAARRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGREMlVMYA-RLRGIPERLINACVENtlrgLL----LEPHANKLVKTYSGGNKRKLstGIA--LI 1530
Cdd:COG1135 84 IGMIFQHFNLLSSRTVAEN-VALPlEIAGVPKAEIRKRVAE----LLelvgLSDKADAYPSQLSGGQKQRV--GIAraLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1531 GEPAVIFLDEPSTGMDP------------VARRLlwdtvararesGKAIVITSHSMEECEALCTRLAIMVQGQ------- 1591
Cdd:COG1135 157 NNPKVLLCDEATSALDPettrsildllkdINREL-----------GLTIVLITHEMDVVRRICDRVAVLENGRiveqgpv 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1592 FKCLGSPQH-LKSKF-------GSGYSLQAKVRSEGKQDALeefkafVDLTFPGS 1638
Cdd:COG1135 226 LDVFANPQSeLTRRFlptvlndELPEELLARLREAAGGGRL------VRLTFVGE 274
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
530-742 |
4.22e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 4.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHaYIHGYEIsqdmaqirkSLG 609
Cdd:COG0488 316 LELEGLSKSYG----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV---------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQH-DVLFDNLTVAEHlyfyaqLKGLSLQKCPEEVKQMLhilsledKR------DLRSK--FLSGGMKRKLSIGIALI 680
Cdd:COG0488 382 YFDQHqEELDPDKTVLDE------LRDGAPGGTEQEVRGYL-------GRflfsgdDAFKPvgVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSdrTVLLTTH---FMDEadlLGDRIAILAKGELQ 742
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDFPG--TVLLVSHdryFLDR---VATRILEFEDGGVR 508
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
549-741 |
4.36e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.82 E-value: 4.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLF-----PPTSGHAYIHGYEI-SQDMAQIRKSLGLCPQHDVLFDNLT 622
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VAEHLYFYAQLKGL--SLQKCPEEVKQMLHILSL----EDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:PRK14247 99 IFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 697 AVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1408-1591 |
4.49e-19 |
|
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: 87.74 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1408 KGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGY-----SISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYAR 1482
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1483 LRGIPERLInaCVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARE 1562
Cdd:cd03297 102 RKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|
gi 569000489 1563 SGKAIVI-TSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03297 180 NLNIPVIfVTHDLSEAEYLADRIVVMEDGR 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1376-1599 |
4.89e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 91.16 E-value: 4.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLI-INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----- 1449
Cdd:PRK09452 9 SSLSPLVeLRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaen 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 -DIGKVRQrmGYcpqfdALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIA 1528
Cdd:PRK09452 86 rHVNTVFQ--SY-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKAlQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPR 230
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
530-741 |
5.22e-19 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 92.86 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIsQD--MAQIRKS 607
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDL-ADytLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDVLFDNlTVAEHLYfYAQLKGLSLQKCpEEVKQMLHILSLEDKRDLRSKF--------LSGGMKRKLSIGIAL 679
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIA-YGRTEQADRAEI-ERALAAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARAL 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADlLGDRIAILAKGEL 741
Cdd:TIGR02203 485 LKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
495-741 |
5.90e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.56 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 495 GNPRTVVGKEEEG-SDPEKAlrnEYFEAEpEDLvagIKIKHLSKVF-QVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGK 572
Cdd:TIGR03269 251 GTPDEVVAVFMEGvSEVEKE---CEVEVG-EPI---IKVRNVSKRYiSVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGK 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 573 TTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIR--------KSLGLCPQHDVLFDNLTVAEHLyfyAQLKGLSLqkcPEE 644
Cdd:TIGR03269 324 TTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYPHRTVLDNL---TEAIGLEL---PDE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 645 VKQMLHILSL------EDK-RDLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD--LLQQQKS 712
Cdd:TIGR03269 398 LARMKAVITLkmvgfdEEKaEEILDKYpdeLSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsiLKAREEM 477
|
250 260
....*....|....*....|....*....
gi 569000489 713 DRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:TIGR03269 478 EQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1385-1591 |
6.99e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 92.00 E-value: 6.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRA-----PLLAVDR---------ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSIS 1448
Cdd:COG1129 240 ELEDLFPKRAaapgeVVLEVEGlsvggvvrdVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1449 SDIGKVRQRMGYCP---QFDALLDHMTGRE-----MLVMYARLRGIPERLINACVENTLRGLLLE-PHANKLVKTYSGGN 1519
Cdd:COG1129 320 SPRDAIRAGIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGN 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1520 KRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:COG1129 400 QQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1392-1572 |
8.87e-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: 86.14 E-value: 8.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1392 QRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEET--ITSGDAFVGGYSISSDIgkvRQRMGYCPQFDALLD 1469
Cdd:cd03232 18 GKRQLL--NNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNF---QRSTGYVEQQDVHSP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1470 HMTGREMLVMYARLRGIperlinaCVENtlrglllephanklvktysggnKRKLSTGIALIGEPAVIFLDEPSTGMDPVA 1549
Cdd:cd03232 93 NLTVREALRFSALLRGL-------SVEQ----------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
|
170 180
....*....|....*....|...
gi 569000489 1550 RRLLWDTVARARESGKAIVITSH 1572
Cdd:cd03232 144 AYNIVRFLKKLADSGQAILCTIH 166
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1394-1591 |
1.22e-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: 86.49 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1394 APLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALLDHMT 1472
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQ-DVTLFYGT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1473 GREMLVMyARLRGIPERLINACvenTLRGllLEPHANKLVKTY-----------SGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:cd03245 94 LRDNITL-GAPLADDERILRAA---ELAG--VTDFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1542 STGMDPVARRLLwdtVARARE--SGKAIVITSH--SMEEceaLCTRLAIMVQGQ 1591
Cdd:cd03245 168 TSAMDMNSEERL---KERLRQllGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
551-739 |
1.30e-18 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 86.39 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQI---RKSLGLCPQHDVLFDNLTVAEHL 627
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING----VDVTAAppaDRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFyAQLKGLSLQkcPEEVKQMLHILS---LEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIW 704
Cdd:cd03298 92 GL-GLSPGLKLT--AEDRQAIEVALArvgLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 705 DLL----QQQKSdrTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:cd03298 169 DLVldlhAETKM--TVLMVTHQPEDAKRLAQRVVFLDNG 205
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
552-721 |
1.46e-18 |
|
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: 85.49 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYFYA 631
Cdd:TIGR01189 19 LSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 632 QLKGlSLQKCPEEVkqmLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRraiwDLLQQQK 711
Cdd:TIGR01189 99 AIHG-GAQRTIEDA---LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV----ALLAGLL 170
|
170
....*....|....*
gi 569000489 712 SDRT-----VLLTTH 721
Cdd:TIGR01189 171 RAHLarggiVLLTTH 185
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1380-1598 |
1.65e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 87.80 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1380 PLIINELSKVYDQRAPL--LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS---DIGKV 1454
Cdd:PRK13637 2 SIKIENLTHIYMEGTPFekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQF-DALLDHMTGREMLVMYARLRGIPERLINACVENTLR--GLLLEPHANKLVKTYSGGNKRKLSTGIALIG 1531
Cdd:PRK13637 82 RKKVGLVFQYpEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1532 EPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVI-TSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIIlVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1386-1591 |
1.75e-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: 84.58 E-value: 1.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSKVYDQRAPLLaVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQF 1464
Cdd:cd03246 6 VSFRYPGAEPPV-LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DALLDhmtgremlvmyarlrgiperlinacventlrGLLLEphaNKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTG 1544
Cdd:cd03246 85 DELFS-------------------------------GSIAE---NIL----SGGQRQRLGLARALYGNPRILVLDEPNSH 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 1545 MDPVARRLLWDTVARARESGKAIVITSHSMEECEAlCTRLAIMVQGQ 1591
Cdd:cd03246 127 LDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
551-740 |
3.11e-18 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 85.58 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNlyEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQIRkslglcP---------QHDVLFDNL 621
Cdd:COG3840 19 DLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNG----QDLTALP------PaerpvsmlfQENNLFPHL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYFyaqlkGLS--LQKCPEEVKQMLHIL---SLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:COG3840 87 TVAQNIGL-----GLRpgLKLTAEQRAQVEQALervGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALD 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 697 AVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:COG3840 162 PALRQEMLDLVDELCRERglTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1383-1591 |
3.49e-18 |
|
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: 84.89 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYdqrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI---SSDIGKVRQRMG 1459
Cdd:cd03262 3 IKNLHKSF---GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMlVMYA--RLRGIPErlinACVENTLRGLL----LEPHANKLVKTYSGGNKRKLSTGIALIGEP 1533
Cdd:cd03262 80 MVFQQFNLFPHLTVLEN-ITLApiKVKGMSK----AEAEERALELLekvgLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
526-721 |
3.54e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 90.55 E-value: 3.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 526 LVAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DM 601
Cdd:PRK10535 1 MTALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIRKS-LGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALI 680
Cdd:PRK10535 81 AQLRREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTH 721
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTH 202
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1398-1592 |
4.29e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.69 E-value: 4.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSISSD-------IGKVRQRMGYCPQFDA-- 1466
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPrdaqaagIAIIHQELNLVPNLSVae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 --LLDHMTGREMLV----MYARLRGIPERLinacventlrGLLLEPHAnkLVKTYSGGNK------RklstgiALIGEPA 1534
Cdd:COG1129 99 niFLGREPRRGGLIdwraMRRRARELLARL----------GLDIDPDT--PVGDLSVAQQqlveiaR------ALSRDAR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1377-1601 |
4.45e-18 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 4.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1377 LDTPLIINELSKVYDQRAPLLAVDrisLAVQKGECFGLLGFNGAGKTTTFKMLTGeetITSGDAFVGGY----------- 1445
Cdd:PRK09984 1 MQTIIRVEKLAKTFNQHQALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGSHiellgrtvqre 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1446 -SISSDIGKVRQRMGYCPQFDALLDHMTGREMLVMYArLRGIPerLINACV--------ENTLRGLL---LEPHANKLVK 1513
Cdd:PRK09984 75 gRLARDIRKSRANTGYIFQQFNLVNRLSVLENVLIGA-LGSTP--FWRTCFswftreqkQRALQALTrvgMVHFAHQRVS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1514 TYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:PRK09984 152 TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
....*....
gi 569000489 1593 KCLGSPQHL 1601
Cdd:PRK09984 232 FYDGSSQQF 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
544-721 |
4.66e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 84.23 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 544 KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTV 623
Cdd:PRK13540 12 HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYFYAQLKGLSLqkcpeEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:PRK13540 92 RENCLYDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170
....*....|....*....
gi 569000489 704 WDLLQQ-QKSDRTVLLTTH 721
Cdd:PRK13540 167 ITKIQEhRAKGGAVLLTSH 185
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
549-746 |
5.67e-18 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 84.73 E-value: 5.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP----TSGHAYIHGYEISQdMAQIRKSLGLCPQHDVLFDN--LT 622
Cdd:TIGR02770 2 VQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLP-LSIRGRHIATIMQNPRTAFNplFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:TIGR02770 81 MGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEEVLKKYpfqLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 700 RRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:TIGR02770 161 QARVLKLLRelRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGT 209
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
530-741 |
6.50e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIrdlTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR 605
Cdd:PRK10908 2 IRFEHVSKAYLGGRQALQGV---TFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQ-HDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:PRK10908 79 RQIGMIFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1376-1591 |
9.17e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 84.55 E-value: 9.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDI 1451
Cdd:PRK11614 1 MEKVMLSFDKVSAHYGK---IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITdwqtAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1452 gkVRQRMGYCPQFDALLDHMTGREMLVM---YARLRGIPERLINAcveNTLRGLLLEPHANKlVKTYSGGNKRKLSTGIA 1528
Cdd:PRK11614 78 --MREAVAIVPEGRRVFSRMTVEENLAMggfFAERDQFQERIKWV---YELFPRLHERRIQR-AGTMSGGEQQMLAIGRA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
530-741 |
1.05e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.70 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTT---TMSLLTGLFPP--TSGHAYIHGYEI---SQDM 601
Cdd:COG1117 12 IEVRNLN--VYYG--DKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGEDIydpDVDV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIRKSLGLCPQHDVLF-----DNltVAehlyFYAQLKGL------------SLQKC--PEEVKQMLHILSLEdkrdlrs 662
Cdd:COG1117 88 VELRRRVGMVFQKPNPFpksiyDN--VA----YGLRLHGIkskseldeiveeSLRKAalWDEVKDRLKKSALG------- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 663 kfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:COG1117 155 --LSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
550-727 |
1.07e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 89.80 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQIRKSLGLCPQhdV----------LFD 619
Cdd:NF033858 18 DDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG----GDMADARHRRAVCPR--IaympqglgknLYP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 620 NLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:NF033858 92 TLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLS 171
|
170 180 190
....*....|....*....|....*....|.
gi 569000489 700 RRAIWDLLQQQKSDR---TVLLTTHFMDEAD 727
Cdd:NF033858 172 RRQFWELIDRIRAERpgmSVLVATAYMEEAE 202
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
549-740 |
1.34e-17 |
|
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: 83.08 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPT---SGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAE 625
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGlslqkcpeevKQMLhilsledkrdlrsKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSrrAIwD 705
Cdd:cd03233 103 TLDFALRCKG----------NEFV-------------RGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST--AL-E 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569000489 706 LLQQQKSDRTVLLTTHFM------DEADLLGDRIAILAKGE 740
Cdd:cd03233 157 ILKCIRTMADVLKTTTFVslyqasDEIYDLFDKVLVLYEGR 197
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1381-1587 |
1.44e-17 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 84.53 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQ-RAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI---SSDIGKVRQ 1456
Cdd:COG4525 4 LTVRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpGADRGVVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1457 RmgycpqfDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:COG4525 84 K-------DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
549-760 |
1.47e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 88.34 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLF-----DNLT 622
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAISVVSQRVHLFsatlrDNLL 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 623 VAehlyfyaqlkglslqkCPEEV-KQMLHILS-------LEDKRDLRS------KFLSGGMKRKLSIGIALIAGSKVLML 688
Cdd:PRK11160 436 LA----------------APNASdEALIEVLQqvgleklLEDDKGLNAwlgeggRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 689 DEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHfmdeaDLLG----DRIAILAKGELQCCGSSLFLKQKYGAGYHM 760
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQNKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
530-739 |
1.76e-17 |
|
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: 83.25 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF---QVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGH-AYIHGYEISqDMAQI- 604
Cdd:COG4778 5 LEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSiLVRHDGGWV-DLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 --------RKSLGLCPQH----------DVlfdnltVAEHLYfyaqLKGLSLQKCPEEVKQMLHILSLEDKR-DLRSKFL 665
Cdd:COG4778 84 preilalrRRTIGYVSQFlrviprvsalDV------VAEPLL----ERGVDREEARARARELLARLNLPERLwDLPPATF 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 666 SGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTThFMDEA--DLLGDRIAILAKG 739
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGI-FHDEEvrEAVADRVVDVTPF 228
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1386-1609 |
1.93e-17 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 86.63 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSK--VYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKV-RQRM 1458
Cdd:PRK10070 29 LSKeqILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVrRKKI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 GYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:PRK10070 109 AMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLM 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1539 DEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGY 1609
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
535-742 |
2.32e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 83.33 E-value: 2.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 535 LSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMAQIR-KSLG 609
Cdd:PRK11629 11 LCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaAKAELRnQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLgDRIAILAKGELQ 742
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLT 224
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
522-741 |
3.13e-17 |
|
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: 87.87 E-value: 3.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 522 EPEDLVAGIKIKHLSkvFQVGNKDKMgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-D 600
Cdd:TIGR01193 466 ELNNLNGDIVINDVS--YSYGYGSNI-LSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiD 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLCPQHDVLFDNlTVAEHLYFYAQ--------LKGLSLQKCPEEVKQMLhiLSLEDKRDLRSKFLSGGMKRK 672
Cdd:TIGR01193 543 RHTLRQFINYLPQEPYIFSG-SILENLLLGAKenvsqdeiWAACEIAEIKDDIENMP--LGYQTELSEEGSSISGGQKQR 619
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 673 LSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKsDRTVLLTTHFMDEADLLgDRIAILAKGEL 741
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQ-DKTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
553-746 |
3.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 83.90 E-value: 3.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 553 TLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQI------RKSLGLC---PQHDVLFDnlTV 623
Cdd:PRK13645 31 SLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevkrlRKEIGLVfqfPEYQLFQE--TI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRA 702
Cdd:PRK13645 109 EKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEED 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 703 IWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13645 189 FINLFERlnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
523-767 |
5.98e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 5.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 523 PEDLVAGI--KIKHLSKVFQVGNKDKM-GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ 599
Cdd:PRK13631 13 PNPLSDDIilRVKNLYCVFDEKQENELvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 600 DMA-----------------QIRKSLGLC---PQHDVLFDnlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRD 659
Cdd:PRK13631 93 KKNnhelitnpyskkiknfkELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 660 LRSKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDL-LQQQKSDRTVLLTTHFMDEADLLGDRIAILA 737
Cdd:PRK13631 171 ERSPFgLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLiLDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
250 260 270
....*....|....*....|....*....|..
gi 569000489 738 KGELQCCGS--SLFLKQKYgagYHMTLVKEPH 767
Cdd:PRK13631 251 KGKILKTGTpyEIFTDQHI---INSTSIQVPR 279
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
535-749 |
6.49e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.83 E-value: 6.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 535 LSKVFQVGN--------KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIR 605
Cdd:PRK13642 1 MNKILEVENlvfkyekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQH-DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSK 684
Cdd:PRK13642 81 RKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 685 VLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEAdLLGDRIAILAKGEL--QCCGSSLF 749
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEikEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIikEAAPSELF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1357-1584 |
6.59e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 85.89 E-value: 6.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1357 EDQDVAEERSRILVPSLDSMLDTPLIINELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETIT 1436
Cdd:COG0488 292 EEPPRRDKTVEIRFPPPERLGKKVLELEGLSKSYGDK-TLL--DDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1437 SGDAFVGgysissdigkVRQRMGYCPQ----FDA---LLDHM--TGREMLVMYARlrgiperlinacveNTLRGLLLEP- 1506
Cdd:COG0488 369 SGTVKLG----------ETVKIGYFDQhqeeLDPdktVLDELrdGAPGGTEQEVR--------------GYLGRFLFSGd 424
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1507 HANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDtvARARESGkAIVITSHSMEECEALCTRL 1584
Cdd:COG0488 425 DAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEE--ALDDFPG-TVLLVSHDRYFLDRVATRI 499
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
548-741 |
6.70e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 85.84 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 548 GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS----QDM--AQI------RKSLGLCPQHD 615
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRirspRDAirAGIayvpedRKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 616 VLfDNLTVAeHLYFYAQLKGLSLQKCPEEVKQMLHILSLedK---RDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:COG1129 347 IR-ENITLA-SLDRLSRGGLLDRRRERALAEEYIKRLRI--KtpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 693 SGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEadLLG--DRIAILAKGEL 741
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAEgKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1379-1587 |
7.24e-17 |
|
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: 81.71 E-value: 7.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIINELSKVYD----QRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKML-------TGEETITSGDAFVGGYSI 1447
Cdd:COG4778 3 TLLEVENLSKTFTlhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygnylpdSGSILVRHDGGWVDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1448 S-SDIGKVRQR-MGYCPQF--------------DALLD--------HMTGREMLvmyARLrGIPERLINacventlrgll 1503
Cdd:COG4778 83 SpREILALRRRtIGYVSQFlrviprvsaldvvaEPLLErgvdreeaRARARELL---ARL-NLPERLWD----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1504 LEPHanklvkTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTR 1583
Cdd:COG4778 148 LPPA------TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADR 221
|
....
gi 569000489 1584 LAIM 1587
Cdd:COG4778 222 VVDV 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1379-1591 |
7.41e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 7.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLI-INELSKVYDqraPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSISS--D--- 1450
Cdd:COG3845 3 PPALeLRGITKRFG---GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprDaia 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1451 --IGKVRQrmgycpQFdALLDHMTGREMLVMY---------------ARLRGIPERLinacventlrGLLLEPHAnkLVK 1513
Cdd:COG3845 80 lgIGMVHQ------HF-MLVPNLTVAENIVLGleptkggrldrkaarARIRELSERY----------GLDVDPDA--KVE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1514 TysggnkrkLSTGI--------ALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLA 1585
Cdd:COG3845 141 D--------LSVGEqqrveilkALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVT 212
|
....*.
gi 569000489 1586 IMVQGQ 1591
Cdd:COG3845 213 VLRRGK 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1401-1605 |
9.32e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.87 E-value: 9.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1401 RISLAVQKGECFGLLGFNGAGKTT-----TFKMLTGEETitSGDAFVGGYSISSDigKVRQRMGYCPQFDALLDHMTGRE 1475
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1476 MLVMYARLRgIPERLIN----ACVENTLRGLLLEPHANKL------VKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:TIGR00955 119 HLMFQAHLR-MPRRVTKkekrERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1546 DPVARRLLWDTVARARESGKAIVITSH--SMEECEaLCTRLAIMVQGQFKCLGSPQHLKSKF 1605
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFF 258
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1398-1603 |
1.26e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 82.05 E-value: 1.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD---IGKVRQRMGYCPQF-DALLDHMTG 1473
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNpDDQLFAPTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1474 REMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVA---- 1549
Cdd:PRK13639 97 EEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGasqi 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1550 RRLLWDTvaraRESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:PRK13639 177 MKLLYDL----NKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
532-753 |
1.65e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 84.73 E-value: 1.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFqvgnkdkmGIR----DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisqdmaqiRKS 607
Cdd:COG0488 1 LENLSKSF--------GGRplldDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLR 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDVLFDNLTV--------------------AEHLYFYAQLKGLSLQKCPEE------------VKQMLHILSLE 655
Cdd:COG0488 63 IGYLPQEPPLDDDLTVldtvldgdaelraleaeleeLEAKLAEPDEDLERLAELQEEfealggweaearAEEILSGLGFP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 656 DkRDLRSKF--LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRaiW--DLLQQQKSdrTVLLTTH---FMDEadl 728
Cdd:COG0488 143 E-EDLDRPVseLSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYPG--TVLVVSHdryFLDR--- 214
|
250 260
....*....|....*....|....*..
gi 569000489 729 LGDRIAILAKGELQC--CGSSLFLKQK 753
Cdd:COG0488 215 VATRILELDRGKLTLypGNYSAYLEQR 241
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1381-1587 |
3.09e-16 |
|
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: 81.64 E-value: 3.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLL-AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG---EETITSGDAFVGGYSISS----DIG 1452
Cdd:COG0444 2 LEVRNLKVYFPTRRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1453 KVR-QRMGYCPQfDAL--LD-HMT-GREMLVMYARLRGIPERLINACVENTLR--GLllePHANKLVKTY----SGGNKR 1521
Cdd:COG0444 82 KIRgREIQMIFQ-DPMtsLNpVMTvGDQIAEPLRIHGGLSKAEARERAIELLErvGL---PDPERRLDRYphelSGGMRQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1522 KLSTGIALIGEPAVIFLDEPSTGMDPVARR----LLWDtvaRARESGKAIVITSHSMEECEALCTRLAIM 1587
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAqilnLLKD---LQRELGLAILFITHDLGVVAEIADRVAVM 224
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
545-749 |
3.34e-16 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.13 E-value: 3.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 545 DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP----TSGHAYIHGYEISQdmAQIR-KSLGLCPQHD-VLF 618
Cdd:PRK10418 15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP--CALRgRKIATIMQNPrSAF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 619 DNL-TVAEHlyfyAQLKGLSLQKcPEEVKQMLHILS---LEDKRDLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEP 691
Cdd:PRK10418 93 NPLhTMHTH----ARETCLALGK-PADDATLTAALEavgLENAARVLKLYpfeMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 692 TSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS--SLF 749
Cdd:PRK10418 168 TTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1397-1604 |
3.44e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 80.90 E-value: 3.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS--SDIGKVRQRMGYC---P--QFDALL- 1468
Cdd:PRK13633 24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeENLWDIRNKAGMVfqnPdnQIVATIv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 --DHMTGREMLvmyarlrGIPERLINACVENTLRGLLL---EPHANKLVktySGGNKRKLSTGIALIGEPAVIFLDEPST 1543
Cdd:PRK13633 104 eeDVAFGPENL-------GIPPEEIRERVDESLKKVGMyeyRRHAPHLL---SGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1544 GMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECeALCTRLAIMVQGQFKCLGSPQHLKSK 1604
Cdd:PRK13633 174 MLDPSGRREVVNTIKElNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
545-741 |
3.76e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.27 E-value: 3.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 545 DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLF-----PPTSGHAYIHG---YEISQDMAQIRKSLGLCPQHDV 616
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGrniYSPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 617 LFDNLTVAEHLYFYAQLKGL--SLQKCPEEVKQMLHILSLEDKRDLRSK----FLSGGMKRKLSIGIALIAGSKVLMLDE 690
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 691 PTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1383-1599 |
4.41e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 81.67 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLlavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRqRMGYCP 1462
Cdd:PRK10851 5 IANIKKSFGRTQVL---NDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1463 QFDALLDHMTGREMLVMyaRLRGIPER------LINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:PRK10851 81 QHYALFRHMTVFDNIAF--GLTVLPRRerpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQIL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARARESGK-AIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
551-696 |
4.45e-16 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYI--HGYEISQ-----DMAQIRKSLGLCPQHDVLFDNLTV 623
Cdd:PRK11124 20 DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKtpsdkAIRELRRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 624 AEHLyFYAQLK--GLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:PRK11124 100 QQNL-IEAPCRvlGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
529-696 |
4.58e-16 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 4.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 529 GIKIKHLSK---VFQVgnkdkmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS------- 598
Cdd:COG4161 2 SIQLKNINCfygSHQA-------LFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpse 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 599 QDMAQIRKSLGLCPQHDVLFDNLTVAEHLyFYAQLK--GLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIG 676
Cdd:COG4161 75 KAIRLLRQKVGMVFQQYNLWPHLTVMENL-IEAPCKvlGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIA 153
|
170 180
....*....|....*....|
gi 569000489 677 IALIAGSKVLMLDEPTSGMD 696
Cdd:COG4161 154 RALMMEPQVLLFDEPTAALD 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1396-1603 |
4.69e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 80.03 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1396 LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFD--ALLDHMTG 1473
Cdd:PRK11300 18 LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQhvRLFREMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1474 REMLvMYARlrgipERLINAcveNTLRGLL------------------------LEPHANKLVKTYSGGNKRKLSTGIAL 1529
Cdd:PRK11300 98 IENL-LVAQ-----HQQLKT---GLFSGLLktpafrraesealdraatwlervgLLEHANRQAGNLAYGQQRRLEIARCM 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1530 IGEPAVIFLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:PRK11300 169 VTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
495-772 |
5.17e-16 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 84.39 E-value: 5.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 495 GNPRTVVGKEEEGSDPEKALRNEYFEAEPEDLVAGIKIKHLSKV-FQVGNK--DKMGIRDLTLNLYEGQITVLLGHNGAG 571
Cdd:TIGR00956 722 SNKNDIEAGEVLGSTDLTDESDDVNDEKDMEKESGEDIFHWRNLtYEVKIKkeKRVILNNVDGWVKPGTLTALMGASGAG 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 572 KTTTMSLL-----TGLFppTSGHAYIHGYEISQDMAqirKSLGLCPQHDVLFDNLTVAEHLYFYAQL---KGLSLQKCPE 643
Cdd:TIGR00956 802 KTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAYLrqpKSVSKSEKME 876
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 644 EVKQMLHILSLEDKRD----LRSKFLSGGMKRKLSIGIALIAGSKVLM-LDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVL 717
Cdd:TIGR00956 877 YVEEVIKLLEMESYADavvgVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAIL 956
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 718 LTTHfMDEADLLG--DRIAILAK-------GEL-QCCGSSLFLKQKYGAgyhmtlvkePHCNPEG 772
Cdd:TIGR00956 957 CTIH-QPSAILFEefDRLLLLQKggqtvyfGDLgENSHTIINYFEKHGA---------PKCPEDA 1011
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1398-1604 |
5.36e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 80.28 E-value: 5.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG----YSiSSDIGKVRQRMGYCPQF-DALLDHMT 1472
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpidYS-RKGLMKLRESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1473 GREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVA-RR 1551
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGvSE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1552 LLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSK 1604
Cdd:PRK13636 180 IMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
532-756 |
5.77e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 81.32 E-value: 5.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFQVGNKDkmgirdltLNLYEGQITVLLGHNGAGKTTTmSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLC 611
Cdd:NF000106 20 VKHFGEVKAVDGVD--------LDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 612 -PQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDE 690
Cdd:NF000106 91 rPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 691 PTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQKYGA 756
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDgATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG 237
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1383-1591 |
6.57e-16 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 6.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRA-PLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIGKVRQR 1457
Cdd:PRK11153 4 LKNISKVFPQGGrTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIF 1537
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1538 LDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK11153 164 CDEATSALDPATTRSILELLKDInRELGLTIVLITHEMDVVKRICDRVAVIDAGR 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
554-739 |
8.73e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 8.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 554 LNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI----SQDMAqiRKSLGLCPQHDVLFDNLTVAEHLyF 629
Cdd:PRK11300 26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIeglpGHQIA--RMGVVRTFQHVRLFREMTVIENL-L 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 630 YAQ--------LKGL--------SLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:PRK11300 103 VAQhqqlktglFSGLlktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAA 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569000489 694 GMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11300 183 GLNPKETKELDELIAELRNEHnvTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
530-725 |
1.08e-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: 75.56 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHaYIHGyeisqdmaqirkslg 609
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWG--------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 lcpqhdvlfDNLTVAehlyFYAQLkglslqkcpeevkqmlhilsledkrdlrskflSGGMKRKLSIGIALIAGSKVLMLD 689
Cdd:cd03221 61 ---------STVKIG----YFEQL--------------------------------SGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 690 EPTSGMDAVSRRAIWDLLQQQKsdRTVLLTTH---FMDE 725
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYP--GTVILVSHdryFLDQ 132
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
552-721 |
1.20e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 77.15 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYFYA 631
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFWH 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 632 QLKGlslqkcPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQ- 710
Cdd:cd03231 99 ADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGHc 172
|
170
....*....|.
gi 569000489 711 KSDRTVLLTTH 721
Cdd:cd03231 173 ARGGMVVLTTH 183
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1399-1601 |
1.46e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.15 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDIGK--VRQRmGYCPQFD--ALLDHMTGR 1474
Cdd:PRK11432 22 IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDG----EDVTHrsIQQR-DICMVFQsyALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLW 1554
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1555 DTVaraRESGKAIVITS----HSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK11432 177 EKI---RELQQQFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
530-721 |
1.72e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 81.99 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIsQD--MAQIRKS 607
Cdd:PRK11176 342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDytLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDVLFdNLTVAEHLYfYAQLKGLSLQKCpEEVKQMLH----ILSLEDKRDL----RSKFLSGGMKRKLSIGIAL 679
Cdd:PRK11176 419 VALVSQNVHLF-NDTIANNIA-YARTEQYSREQI-EEAARMAYamdfINKMDNGLDTvigeNGVLLSGGQRQRIAIARAL 495
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:PRK11176 496 LRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAH 537
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1413-1603 |
2.32e-15 |
|
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: 79.77 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1413 GLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV-----RQRMGYCPQFDALLDHMTGREMLVM-YARLRGi 1486
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1487 PERLINAcvENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-ARESGK 1565
Cdd:TIGR02142 106 SERRISF--ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERlHAEFGI 183
|
170 180 190
....*....|....*....|....*....|....*...
gi 569000489 1566 AIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:TIGR02142 184 PILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
549-727 |
2.61e-15 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 76.75 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP---TSGHAYIHGYEISQDMAQIRKsLGLCPQHDVLFDNLTVAE 625
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRR-IGILFQDDLLFPHLSVGE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFyAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD 705
Cdd:COG4136 96 NLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRAQFRE 174
|
170 180
....*....|....*....|....
gi 569000489 706 LLQQQKSDRT--VLLTTHfmDEAD 727
Cdd:COG4136 175 FVFEQIRQRGipALLVTH--DEED 196
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
552-741 |
2.84e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.04 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGlFPPTSGHAYIHGYEISQ-DMAQIRKSL---GLCPQ--HDVLFDNLTVAE 625
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLGN 447
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLsLQKC--PEEVKQMLHILSLEDKRdlRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAI 703
Cdd:PRK11174 448 PDASDEQLQQA-LENAwvSEFLPLLPQGLDTPIGD--QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLV 524
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 704 WDLLQQQKSDRTVLLTTHFMDeaDLLG-DRIAILAKGEL 741
Cdd:PRK11174 525 MQALNAASRRQTTLMVTHQLE--DLAQwDQIWVMQDGQI 561
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
521-741 |
3.11e-15 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 81.16 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 521 AEPEDLVAGIKIKHLSkvFQVGNKdKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ- 599
Cdd:PRK13657 326 IDLGRVKGAVEFDDVS--FSYDNS-RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTv 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 600 DMAQIRKSLGLCPQHDVLFdNLTVAEHlyfyaqlkgLSLQK---CPEEVKQMLH-------ILSLEDKRDL----RSKFL 665
Cdd:PRK13657 403 TRASLRRNIAVVFQDAGLF-NRSIEDN---------IRVGRpdaTDEEMRAAAEraqahdfIERKPDGYDTvvgeRGRQL 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 666 SGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMD---EAdllgDRIAILAKGEL 741
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
551-739 |
4.17e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.34 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYE---------ISQDMAQIRKSLGLCPqhdvlfdNL 621
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEmrfasttaaLAAGVAIIYQELHLVP-------EM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYFyAQLKG----LSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA 697
Cdd:PRK11288 95 TVAENLYL-GQLPHkggiVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSA 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000489 698 VSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11288 174 REIEQLFRVIRELRAEgRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
538-741 |
7.93e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.44 E-value: 7.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 538 VFQVGN---KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--QDMAQIRKSLGLCP 612
Cdd:PRK09700 265 VFEVRNvtsRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 613 QH---DVLFDNLTVAEHLYFYAQLK--------GL----SLQKCPEEVKQMLHILSLEDKRDLRSkfLSGGMKRKLSIGI 677
Cdd:PRK09700 345 ESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLfhevDEQRTAENQRELLALKCHSVNQNITE--LSGGNQQKVLISK 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 678 ALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK09700 423 WLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1381-1591 |
8.63e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 76.28 E-value: 8.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPL--LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--------YSISSD 1450
Cdd:COG1101 2 LELKNLSKTFNPGTVNekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGkdvtklpeYKRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1451 IGKVRQ--RMGYCPqfdalldHMTGREMLVMyARLRGIPERLINAcVENTLR----------GLLLEPHANKLVKTYSGG 1518
Cdd:COG1101 82 IGRVFQdpMMGTAP-------SMTIEENLAL-AYRRGKRRGLRRG-LTKKRRelfrellatlGLGLENRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1519 NKRKLSTGIALIGEPAVIFLDEPSTGMDP-VARRLLWDTVARARESG-KAIVITsHSMEECEALCTRLAIMVQGQ 1591
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPkTAALVLELTEKIVEENNlTTLMVT-HNMEQALDYGNRLIMMHEGR 226
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1397-1633 |
8.99e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 8.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFV-GGysissDIGKVRQR------MGYCPQfdalld 1469
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGG-----DMADARHRravcprIAYMPQ------ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1470 hmtG-----------REMLVMYARLRGIP----ERLINACVENTlrGLL--LEPHANKLvktySGGNKRKLSTGIALIGE 1532
Cdd:NF033858 84 ---GlgknlyptlsvFENLDFFGRLFGQDaaerRRRIDELLRAT--GLApfADRPAGKL----SGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1533 PAVIFLDEPSTGMDPVARRLLWDTVARARESGKA---IVITSHsMEECEAlCTRLAIMVQGQFKCLGSPQHLKSKFGSgy 1609
Cdd:NF033858 155 PDLLILDEPTTGVDPLSRRQFWELIDRIRAERPGmsvLVATAY-MEEAER-FDWLVAMDAGRVLATGTPAELLARTGA-- 230
|
250 260
....*....|....*....|....
gi 569000489 1610 slqakvrsegkqDALEEfkAFVDL 1633
Cdd:NF033858 231 ------------DTLEA--AFIAL 240
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1383-1604 |
1.09e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.31 E-value: 1.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD-IGKVRQRMGYC 1461
Cdd:PRK13650 7 VKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQF-DALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:PRK13650 87 FQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVIT-SHSMEECeALCTRLAIMVQGQFKCLGSPQHLKSK 1604
Cdd:PRK13650 167 ATSMLDPEGRLELIKTIKGIRDDYQMTVISiTHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
523-741 |
1.11e-14 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 523 PEDLVAGIK--IKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGH-----AYIHgy 595
Cdd:PRK11247 4 TARLNQGTPllLNAVSKRY----GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEllagtAPLA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 596 EISQDMAQIRKSLGLCPQHDVLfDNLtvaehlyfyaqlkGLSLQ-KCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLS 674
Cdd:PRK11247 78 EAREDTRLMFQDARLLPWKKVI-DNV-------------GLGLKgQWRDAALQALAAVGLADRANEWPAALSGGQKQRVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 675 IGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK11247 144 LARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
530-747 |
1.12e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP----PTS-----GHAYIHGYEISQD 600
Cdd:PRK09984 5 IRVEKLAKTFN----QHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGShiellGRTVQREGRLARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKC-----PEEVKQMLHILS---LEDKRDLRSKFLSGGMKRK 672
Cdd:PRK09984 81 IRKSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCfswftREQKQRALQALTrvgMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 673 LSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGSS 747
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1400-1572 |
1.37e-14 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 79.77 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1400 DRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEET---ITSGDAFVGGYSISSDIgkvRQRMGYCPQFDALLDHMTGREM 1476
Cdd:TIGR00956 780 NNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTtgvITGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRES 856
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLR---GIPERLINACVENTLRGLLLEPHANKLVKTYSGG----NKRKLSTGIALIGEPA-VIFLDEPSTGMDPV 1548
Cdd:TIGR00956 857 LRFSAYLRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQ 936
|
170 180
....*....|....*....|....
gi 569000489 1549 ARRLLWDTVARARESGKAIVITSH 1572
Cdd:TIGR00956 937 TAWSICKLMRKLADHGQAILCTIH 960
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
530-739 |
1.43e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 75.13 E-value: 1.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF---QVgnkdkmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI---SQDMAQ 603
Cdd:PRK09493 2 IEFKNVSKHFgptQV-------LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IRKSLGLCPQHDVLFDNLTVAEHLYFYA-QLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAG 682
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 683 SKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKG 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
530-758 |
1.72e-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: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSkvfqVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGlFP---PTSGHAYIHGYEISqDMA---Q 603
Cdd:cd03217 1 LEIKDLH----VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDIT-DLPpeeR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IRKSLGLCPQHDVLFDNLTVAEHLyfyaqlkglslqkcpeevkqmlhilsledkRDLRSKFlSGGMKRKLSIGIALIAGS 683
Cdd:cd03217 75 ARLGIFLAFQYPPEIPGVKNADFL------------------------------RYVNEGF-SGGEKKRNEILQLLLLEP 123
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 684 KVLMLDEPTSGMDAVSRRAIWDLLQQQKS-DRTVLLTTHFMDEADLL-GDRIAILAKGELQCCGSSLFLKQKYGAGY 758
Cdd:cd03217 124 DLAILDEPDSGLDIDALRLVAEVINKLREeGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1388-1592 |
2.19e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 78.17 E-value: 2.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1388 KVYDQRAPLLAVDR--------ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDigKVRQRMG 1459
Cdd:PRK15439 260 RQQAAGAPVLTVEDltgegfrnISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINAL--STAQRLA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 ----YCPQ--------FDALLdhmTGREMLVMYAR----LRGIPERlinACVENTLRGLLLE-PHANKLVKTYSGGNKRK 1522
Cdd:PRK15439 338 rglvYLPEdrqssglyLDAPL---AWNVCALTHNRrgfwIKPAREN---AVLERYRRALNIKfNHAEQAARTLSGGNQQK 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1523 LSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:PRK15439 412 VLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1398-1603 |
2.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 75.41 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS--SDIGKVRQRMGYCpqFDALLDHMTGR- 1474
Cdd:PRK13644 17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIV--FQNPETQFVGRt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 --EMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRL 1552
Cdd:PRK13644 95 veEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1553 LWDTVARARESGKAIVITSHSMEECEAlCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVLS 224
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1380-1573 |
2.48e-14 |
|
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: 77.79 E-value: 2.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1380 PLIINELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRM 1458
Cdd:TIGR02868 334 TLELRDLSAGYPGAPPVL--DGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 GYCPQfDALLDHMTGREMLvMYARLRGIPERLINAcventLRGLLLEPHANKLV-----------KTYSGGNKRKLSTGI 1527
Cdd:TIGR02868 412 SVCAQ-DAHLFDTTVRENL-RLARPDATDEELWAA-----LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 1528 ALIGEPAVIFLDEPSTGMDP-VARRLLWDTvaRARESGKAIVITSHS 1573
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAeTADELLEDL--LAALSGRTVVLITHH 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
556-739 |
2.63e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.78 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 556 LYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLG--LCPQHDVLFDNLTVAEHLYFYAQL 633
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKENILFGLPK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 634 KGLSLQKcpeeVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKS 712
Cdd:PRK15439 114 RQASMQK----MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRElLAQ 189
|
170 180
....*....|....*....|....*..
gi 569000489 713 DRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK15439 190 GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1398-1592 |
3.39e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 77.26 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGY---------SISSDIGKVRQRMGYCPQF---- 1464
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQemrfasttaALAAGVAIIYQELHLVPEMtvae 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DALLDHMTGREMLV----MYARLRGIPERLinacventlrGLLLEPHANklVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:PRK11288 99 NLYLGQLPHKGGIVnrrlLNYEAREQLEHL----------GVDIDPDTP--LKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1384-1601 |
3.87e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 74.82 E-value: 3.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1384 NELSKVYDQRAPL--LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD-----IGKVRQ 1456
Cdd:PRK13646 6 DNVSYTYQKGTPYehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1457 RMGYCPQF--DALLDHMTGREMLVMYARLRGIPERlinacVENTLRGLLLEPHANKLVKT-----YSGGNKRKLSTGIAL 1529
Cdd:PRK13646 86 RIGMVFQFpeSQLFEDTVEREIIFGPKNFKMNLDE-----VKNYAHRLLMDLGFSRDVMSqspfqMSGGQMRKIAIVSIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1530 IGEPAVIFLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK13646 161 AMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
524-741 |
5.23e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 5.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 524 EDLVAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS----Q 599
Cdd:PRK10762 243 EDQYPRLDKAPGEVRLKVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspQ 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 600 D-----MAQI---RKSLGLcpqhdVLfdNLTVAEHL------YF---YAQLKGLSLQKCPEEVKQMLHILSleDKRDLRS 662
Cdd:PRK10762 323 DglangIVYIsedRKRDGL-----VL--GMSVKENMsltalrYFsraGGSLKHADEQQAVSDFIRLFNIKT--PSMEQAI 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 663 KFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTHFMDEadLLG--DRIAILAKG 739
Cdd:PRK10762 394 GLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPE--VLGmsDRILVMHEG 471
|
..
gi 569000489 740 EL 741
Cdd:PRK10762 472 RI 473
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1399-1599 |
5.74e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 76.03 E-value: 5.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQFDALLDHMTGREML 1477
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VM-----YARLRGIPERlINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMD-PVARR 1551
Cdd:PRK09536 99 EMgrtphRSRFDTWTET-DRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569000489 1552 LLwDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPA 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
530-739 |
6.71e-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: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvGNKDKMGIrDLTLNlyEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMA------- 602
Cdd:PRK11264 4 IEVKNLVKKFH-GQTVLHGI-DLEVK--PGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 603 --QIRKSLGLCPQHDVLFDNLTVAEHLY-FYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIAL 679
Cdd:PRK11264 80 irQLRQHVGFVFQNFNLFPHRTVLENIIeGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 680 IAGSKVLMLDEPTSGMDA-------VSRRAiwdlLQQQKsdRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPelvgevlNTIRQ----LAQEK--RTMVIVTHEMSFARDVADRAIFMDQG 220
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1392-1591 |
7.17e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 73.69 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1392 QRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQR------MGYCPQFD 1465
Cdd:TIGR02769 22 QRAPVL--TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvqLVFQDSPS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 ALLDHMTGREMLVMYAR-LRGIPERLINACVENTLRGLLLEP-HANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPST 1543
Cdd:TIGR02769 100 AVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSeDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1544 GMDPV----ARRLLwdtVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:TIGR02769 180 NLDMVlqavILELL---RKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1376-1613 |
8.95e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 73.51 E-value: 8.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYDQrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD-IGKV 1454
Cdd:PRK13635 1 MKEEIIRVEHISFRYPD-AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQF-DALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEP 1533
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVIT-SHSMEECeALCTRLAIMVQGQFKCLGSPQHLkskFGSGYSLQ 1612
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEILEEGTPEEI---FKSGHMLQ 235
|
.
gi 569000489 1613 A 1613
Cdd:PRK13635 236 E 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
538-741 |
9.11e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 9.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 538 VFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLC--P--- 612
Cdd:PRK15439 268 VLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 613 QHDVLFDNLTVAEHLYFYAQ-LKGLSLQ-----KCPEEVKQMLHILSLEDKRDLRSkfLSGGMKRKLSIGIALIAGSKVL 686
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHnRRGFWIKparenAVLERYRRALNIKFNHAEQAART--LSGGNQQKVLIAKCLEASPQLL 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQQQKSDRT-VLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK15439 426 IVDEPTRGVDVSARNDIYQLIRSIAAQNVaVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
530-741 |
1.30e-13 |
|
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: 72.92 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVG-----NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----D 600
Cdd:TIGR02769 3 LEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrkQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIRKSLGLC---------PQHDVlfdNLTVAEHLYFYAQLKglslqkcpeEVKQMLHILSLEDKRDLRSKF------- 664
Cdd:TIGR02769 83 RRAFRRDVQLVfqdspsavnPRMTV---RQIIGEPLRHLTSLD---------ESEQKARIAELLDMVGLRSEDadklprq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 665 LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:TIGR02769 151 LSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1385-1598 |
1.55e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 73.23 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRAPLL--AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG-----EETITSGDAFVGGYSISSDIGKVRQR 1457
Cdd:PRK13643 6 KVNYTYQPNSPFAsrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQF-DALLDHMTGREMLVMYARLRGIPERLINACVENTLRGL-LLEPHANKLVKTYSGGNKRKLSTGIALIGEPAV 1535
Cdd:PRK13643 86 VGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVgLADEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
553-739 |
1.68e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 553 TLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisQDMAQI---RKSLGLCPQHDVLFDNLTVAEH--L 627
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTppsRRPVSMLFQENNLFSHLTVAQNigL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAQLKGLSLQKcpEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL 707
Cdd:PRK10771 95 GLNPGLKLNAAQR--EKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
|
170 180 190
....*....|....*....|....*....|....
gi 569000489 708 QQQKSDR--TVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK10771 173 SQVCQERqlTLLMVSHSLEDAARIAPRSLVVADG 206
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1385-1591 |
1.74e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRA-----PLLAVDR---------ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSIS 1448
Cdd:PRK11288 241 EIGDIYGYRPrplgeVRLRLDGlkgpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIR 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1449 SDIGKVRQRMGYCPQ---FDALLDHMTGREMLVMYARLRGIPER-LINACVENTLRGLLLE------PHANKLVKTYSGG 1518
Cdd:PRK11288 321 SPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARRHHLRAGcLINNRWEAENADRFIRslniktPSREQLIMNLSGG 400
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1519 NKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK11288 401 NQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1381-1604 |
2.40e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 72.75 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPL--LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-----DIGK 1453
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFerRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1454 VRQRMGYCPQF--------------------------DALLdhmTGREMLvmyaRLRGIPERLinacventlrgllLEPH 1507
Cdd:PRK13634 83 LRKKVGIVFQFpehqlfeetvekdicfgpmnfgvseeDAKQ---KAREMI----ELVGLPEEL-------------LARS 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1508 ANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAI 1586
Cdd:PRK13634 143 PFEL----SGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVV 218
|
250
....*....|....*...
gi 569000489 1587 MVQGQFKCLGSPQHLKSK 1604
Cdd:PRK13634 219 MHKGTVFLQGTPREIFAD 236
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1033-1263 |
2.73e-13 |
|
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: 73.19 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1033 GELTVVTALFNNQAYHSPATALAIVDNLLFKLL---CGPQASIEISNYPQPRNTLQVakdhfNEGRKGFDIALNLLIAMA 1109
Cdd:pfam12698 96 GESATVTVYINSSNLLVSKLILNALQSLLQQLNasaLVLLLEALSTSAPIPVESTPL-----FNPQSGYAYYLVGLILMI 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1110 FLASTFSILA---VSERAVQAKHVQFVSGVHVATFWFSALLWDLISFLVPSLLLLvvfqAFNVHAFTRDGHMADLLLLLM 1186
Cdd:pfam12698 171 IILIGAAIIAvsiVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIIL----LLLFGIGIPFGNLGLLLLLFL 246
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1187 LYGWAIIPLMYLMSFFFSAASTAYTRLTIFNILSGIATFIMVTIMRIPAvkleelsrTLDHVFLVLPNHCLGMAVSN 1263
Cdd:pfam12698 247 LYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPS--------FLQWIFSIIPFFSPIDGLLR 315
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1379-1596 |
2.78e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 2.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIinELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS--------- 1449
Cdd:PRK09700 3 TPYI--SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKldhklaaql 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 DIGKVRQRMGYCPQFDALLDHMTGREM--------LVMYARLRGIPERLinacvenTLR-GLLLEPhaNKLVKTYSGGNK 1520
Cdd:PRK09700 81 GIGIIYQELSVIDELTVLENLYIGRHLtkkvcgvnIIDWREMRVRAAMM-------LLRvGLKVDL--DEKVANLSISHK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1521 RKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLG 1596
Cdd:PRK09700 152 QMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1398-1601 |
3.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.14 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-SDIGKVRQRMGYCPQFDALLDHMTGREM 1476
Cdd:PRK13652 19 ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLVFQNPDDQIFSPTVEQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLR-GIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWD 1555
Cdd:PRK13652 99 DIAFGPINlGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELID 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 1556 TVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK13652 179 FLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1381-1572 |
3.35e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 68.63 E-value: 3.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDafvggYSISSDIgkvrqRMGY 1460
Cdd:cd03221 1 IELENLSKTYGGK-LLL--KDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-----VTWGSTV-----KIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFdalldhmtgremlvmyarlrgiperlinacventlrglllephanklvktySGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03221 68 FEQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVaraRESGKAIVITSH 1572
Cdd:cd03221 97 PTNHLDLESIEALEEAL---KEYPGTVILVSH 125
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1381-1604 |
3.41e-13 |
|
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: 74.41 E-value: 3.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMG 1459
Cdd:COG4988 337 IELEDVSFSYPGGRPAL--DGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQfDALLDHMTGREMLVMYArlRGIPERLINACVENTlrglllepHANKLVKTY---------------SGGNKRKLS 1524
Cdd:COG4988 415 WVPQ-NPYLFAGTIRENLRLGR--PDASDEELEAALEAA--------GLDEFVAALpdgldtplgeggrglSGGQAQRLA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1525 TGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARAREsGKAIVITSHSMEECeALCTRLAIMVQGQFKCLGSPQHLKSK 1604
Cdd:COG4988 484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1399-1591 |
3.97e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 3.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGG--YSISSDIGKVRQRMGYC----------PQFDA 1466
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISPRSPLDAVKKGMAYItesrrdngffPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 LLDHMTGREMlvMYARLRG----IPERLINACVENTLRGLLLEPHA-NKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:PRK09700 359 AQNMAISRSL--KDGGYKGamglFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 1542 STGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1402-1604 |
4.85e-13 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 70.93 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD---------IGKVRQRMGYCPQFDALLDHMT 1472
Cdd:PRK11264 22 IDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQLRQHVGFVFQNFNLFPHRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1473 GREMLVM-YARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARR 1551
Cdd:PRK11264 102 VLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVG 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1552 LLWDTVARARESGKAIVITSHSMEECEALCTRL------AIMVQGQFKCL-GSPQHLKSK 1604
Cdd:PRK11264 182 EVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAifmdqgRIVEQGPAKALfADPQQPRTR 241
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1381-1599 |
6.04e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 70.57 E-value: 6.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMG 1459
Cdd:PRK13548 3 LEARNLSVRLGGR-TLL--DDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVM----YARLRGIPERLINACVENT-LRGLllephANKLVKTYSGGNK------RKLSTGIA 1528
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMgrapHGLSRAEDDALVAAALAQVdLAHL-----AGRDYPQLSGGEQqrvqlaRVLAQLWE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1529 LIGEPAVIFLDEPSTGMDP--------VARRLlwdtvarARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK13548 155 PDGPPRWLLLDEPTSALDLahqhhvlrLARQL-------AHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1399-1590 |
6.67e-13 |
|
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: 70.19 E-value: 6.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDiGKvrQRMgYCPQFDALLDHMTGRE--M 1476
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEP-GP--DRM-VVFQNYSLLPWLTVREniA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 569000489 1557 VAR-ARESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:TIGR01184 157 LMQiWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1381-1619 |
7.79e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 71.19 E-value: 7.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPL--LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV---- 1454
Cdd:PRK13645 7 IILDNVSYTYAKKTPFefKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIkevk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 --RQRMGYCPQFD--ALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTG--IA 1528
Cdd:PRK13645 87 rlRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAgiIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1529 LIGEPAVifLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP------QHL 1601
Cdd:PRK13645 167 MDGNTLV--LDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPfeifsnQEL 244
|
250 260
....*....|....*....|..
gi 569000489 1602 KSKFG----SGYSLQAKVRSEG 1619
Cdd:PRK13645 245 LTKIEidppKLYQLMYKLKNKG 266
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
549-721 |
8.11e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 74.11 E-value: 8.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGlfPPTSGH----AYIHGYEISQD-MAQIRkslGLCPQHDVLFDNLTV 623
Cdd:PLN03140 896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYiegdIRISGFPKKQEtFARIS---GYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYFYAQLKgLSLQKCPEE----VKQMLHILSLEDKRDLRSKF-----LSGGMKRKLSIGIALIAGSKVLMLDEPTSG 694
Cdd:PLN03140 971 RESLIYSAFLR-LPKEVSKEEkmmfVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180 190
....*....|....*....|....*....|.
gi 569000489 695 MD----AVSRRAIWDLLQqqkSDRTVLLTTH 721
Cdd:PLN03140 1050 LDaraaAIVMRTVRNTVD---TGRTVVCTIH 1077
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
550-721 |
1.07e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 68.68 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQHDVLFDNLTVAEHLYF 629
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 630 YAQLKGLSLQkcpEEVKQMLHILSLEDKRDLRSKFLSGGMKRKlsigIAL----IAGSKVLMLDEPTSGMDAVSRRAIWD 705
Cdd:PRK13538 98 YQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAIDKQGVARLEA 170
|
170
....*....|....*..
gi 569000489 706 LLQQQ-KSDRTVLLTTH 721
Cdd:PRK13538 171 LLAQHaEQGGMVILTTH 187
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1376-1590 |
1.11e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 69.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKM------LTGEETITSGDAFVGG--YSI 1447
Cdd:PRK14239 1 MTEPILQVSDLSVYYNKKK---ALNSVSLDFYPNEITALIGPSGSGKSTLLRSinrmndLNPEVTITGSIVYNGHniYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1448 SSDIGKVRQRMGYCPQ----FDalldhMTGREMLVMYARLRGIPER-LINACVENTLRGLLL------EPHANKLvkTYS 1516
Cdd:PRK14239 78 RTDTVDLRKEIGMVFQqpnpFP-----MSIYENVVYGLRLKGIKDKqVLDEAVEKSLKGASIwdevkdRLHDSAL--GLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1517 GGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITsHSMEECEALCTRLAIMVQG 1590
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDG 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
544-746 |
1.19e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.04 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 544 KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIsqDMAQiRKSLGLCPQHDVLFDNltv 623
Cdd:PRK13638 12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL--DYSK-RGLLALRQQVATVFQD--- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYFYAQLK---GLSLQK--CPEE--VKQMLHILSLEDKRDLRSK---FLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:PRK13638 86 PEQQIFYTDIDsdiAFSLRNlgVPEAeiTRRVDEALTLVDAQHFRHQpiqCLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 694 GMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
549-721 |
1.43e-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: 73.02 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPpTSGHAYIHGyeISQD---MAQIRKSLGLCPQHDVLFDNlTVAE 625
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNsvtLQTWRKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLR----SKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:TIGR01271 1311 NLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVlvdgGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQ 1390
|
170 180
....*....|....*....|
gi 569000489 702 AIWDLLQQQKSDRTVLLTTH 721
Cdd:TIGR01271 1391 IIRKTLKQSFSNCTVILSEH 1410
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1392-1599 |
1.51e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 72.47 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1392 QRAPLLAvdRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQ----FDA 1466
Cdd:COG4618 343 SKRPILR--GVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRHIGYLPQdvelFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 lldhmTGREMLvmyARLRGI-PERLINACvenTLRGLllepHA--NKLVKTY-----------SGGNKRKLSTGIALIGE 1532
Cdd:COG4618 421 -----TIAENI---ARFGDAdPEKVVAAA---KLAGV----HEmiLRLPDGYdtrigeggarlSGGQRQRIGLARALYGD 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1533 PAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMeecEAL--CTRLAIMVQGQFKCLGSPQ 1599
Cdd:COG4618 486 PRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFGPRD 551
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
547-734 |
1.54e-12 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 547 MGIRDLTLNLYEGQITVLLGHNGAGKTTTM---SLLTGLFPP--TSGHAYIHGYEISQ---DMAQIRKSLGLCPQHDVLF 618
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfNRLNDLIPGfrVEGKVTFHGKNLYApdvDPVEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 619 DNlTVAEHLYFYAQLKGLSlQKCPEEVKQMLHILSLED--KRDLRSK--FLSGGMKRKLSIGIALIAGSKVLMLDEPTSG 694
Cdd:PRK14243 104 PK-SIYDNIAYGARINGYK-GDMDELVERSLRQAALWDevKDKLKQSglSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 695 MDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEADLLGDRIA 734
Cdd:PRK14243 182 LDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1378-1546 |
1.56e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.07 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1378 DTPLII-NELSKVYDQRAPLLAVDR-ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVR 1455
Cdd:PRK11629 2 NKILLQcDNLCKRYQEGSVQTDVLHnVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1456 -----QRMGYCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALI 1530
Cdd:PRK11629 82 aelrnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170
....*....|....*.
gi 569000489 1531 GEPAVIFLDEPSTGMD 1546
Cdd:PRK11629 162 NNPRLVLADEPTGNLD 177
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
530-760 |
1.59e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.44 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSL 608
Cdd:PRK10790 341 IDIDNVSFAYR---DDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQH-----DVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQM---LHILSLEDKRDlrskfLSGGMKRKLSIGIALI 680
Cdd:PRK10790 418 AMVQQDpvvlaDTFLANVTLGRDISEEQVWQALETVQLAELARSLpdgLYTPLGEQGNN-----LSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTHFMD---EAdllgDRIAILAKGELQCCGSSLFLKQKYGAG 757
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHQQLLAAQGRY 568
|
...
gi 569000489 758 YHM 760
Cdd:PRK10790 569 WQM 571
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
526-740 |
1.84e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 69.30 E-value: 1.84e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 526 LVAGIKIKHLSKVFqvgNKDKMgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLfPPTSGHAYIHG---------YE 596
Cdd:PRK14258 4 LIPAIKVNNLSFYY---DTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRM-NELESEVRVEGrveffnqniYE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 597 ISQDMAQIRKSLGLCPQHDVLFDnLTVAEHLYFYAQLKG----LSLQKCPE----------EVKQMLHILSLEdkrdlrs 662
Cdd:PRK14258 79 RRVNLNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkLEIDDIVEsalkdadlwdEIKHKIHKSALD------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 663 kfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQ--KSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK14258 151 --LSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrlRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
549-741 |
1.94e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 69.63 E-value: 1.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--QDMAQIRKSLGLCPQH-DVLFDNLTVAE 625
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGdfSKLQGIRKLVGIVFQNpETQFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD 705
Cdd:PRK13644 98 DLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000489 706 LLQQ-QKSDRTVLLTTHFMDEADlLGDRIAILAKGEL 741
Cdd:PRK13644 178 RIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKI 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1393-1592 |
2.00e-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: 2.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1393 RAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDIGkvrqrmgycpqfdalldHMT 1472
Cdd:COG3845 268 DRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG----EDIT-----------------GLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1473 GREMlvmyaRLRG---IPE-RLINACV------ENTL----------RGLLLEP-----HANKLVKTY------------ 1515
Cdd:COG3845 327 PRER-----RRLGvayIPEdRLGRGLVpdmsvaENLIlgryrrppfsRGGFLDRkairaFAEELIEEFdvrtpgpdtpar 401
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1516 --SGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:COG3845 402 slSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
530-741 |
2.23e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 69.73 E-value: 2.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKM-GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSG------------------HA 590
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 591 YIHGYEIS-------QDMAQIRKSLGLCPQHD--VLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLR 661
Cdd:PRK13651 83 VLEKLVIQktrfkkiKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 662 SKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK13651 162 SPFeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
..
gi 569000489 740 EL 741
Cdd:PRK13651 242 KI 243
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1372-1597 |
2.33e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 68.99 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1372 SLDSMLDTPLIINELSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysisSDI 1451
Cdd:COG4674 2 SLDTMHGPILYVEDLTVSFDG---FKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGG----TDL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1452 GKVRQ----RMGYCPQFD--ALLDHMTGRE-MLVMYARLRGI-------PERLINACVENTLRGLLLEPHANKLVKTYSG 1517
Cdd:COG4674 75 TGLDEheiaRLGIGRKFQkpTVFEELTVFEnLELALKGDRGVfaslfarLTAEERDRIEEVLETIGLTDKADRLAGLLSH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1518 GNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRL---LWDTVARAResgkAIVITSHSMEECEALCTRLAIMVQGQFKC 1594
Cdd:COG4674 155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERtaeLLKSLAGKH----SVVVVEHDMEFVRQIARKVTVLHQGSVLA 230
|
...
gi 569000489 1595 LGS 1597
Cdd:COG4674 231 EGS 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
559-721 |
3.55e-12 |
|
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: 71.39 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 559 GQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqDMAQ--IRKSLGLCPQHDVLFdNLTVAEHLYfYAQLkGL 636
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIR-DVTQasLRAAIGIVPQDTVLF-NDTIAYNIA-YGRP-DA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 637 SlqkcPEEVKQ-----MLH--ILSLEDK-------RDLRskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRA 702
Cdd:COG5265 460 S----EEEVEAaaraaQIHdfIESLPDGydtrvgeRGLK---LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERA 532
|
170
....*....|....*....
gi 569000489 703 IWDLLQQQKSDRTVLLTTH 721
Cdd:COG5265 533 IQAALREVARGRTTLVIAH 551
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1402-1601 |
3.83e-12 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.66 E-value: 3.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQR-MGYCPQFDALLDHMTGREMLVM- 1479
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQQLPAAEGMTVRELVAIg 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1480 -------YARLrGIPERlinACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRL 1552
Cdd:PRK10575 110 rypwhgaLGRF-GAADR---EKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 1553 LWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK10575 186 VLALVHRlSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
258-469 |
3.93e-12 |
|
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: 69.73 E-value: 3.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 258 AIQYQLPLLLMLSFTYTSLTIIRAVVQEKEKKLKEYMRMMGLNSWLHWSAWflmffLFFLIVVSFMTLLFCVKVKKDIAV 337
Cdd:pfam12698 159 YAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGK-----ILGDFLVGLLQLLIILLLLFGIGI 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 338 lSNSDPSLVLAFLLCFAISSISFSFMVSTFFSKANIAAAVGGFLYFFTYTPYFFVAPRYNWMTLSQKLLSCLLSNVAMAM 417
Cdd:pfam12698 234 -PFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPSFLQWIFSIIPFFSPIDG 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 418 gaqligkfeakgtgiqwrdLLNPVNVDDNFCFGQVLGMLLLDSALYGLVTWY 469
Cdd:pfam12698 313 -------------------LLRLIYGDSLWEIAPSLIILLLFAVVLLLLALL 345
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1402-1599 |
3.99e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 68.62 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-----DIGKVRQRMGYCPQF-------DALLD 1469
Cdd:PRK13649 26 VNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQFpesqlfeETVLK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1470 HM----------------TGREMLvmyaRLRGIPERLINacventlrglllephanKLVKTYSGGNKRKLSTGIALIGEP 1533
Cdd:PRK13649 106 DVafgpqnfgvsqeeaeaLAREKL----ALVGISESLFE-----------------KNPFELSGGQMRRVAIAGILAMEP 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK13649 165 KILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPK 230
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1385-1591 |
4.55e-12 |
|
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: 67.13 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYD--QRAPLlavdRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-SDIGKVRQRMGYc 1461
Cdd:cd03298 2 RLDKIRFsyGEQPM----HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTaAPPADRPVSMLF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 pQFDALLDHMTGREM--LVMYARLRGIPERliNACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:cd03298 77 -QENNLFAHLTVEQNvgLGLSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLD 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1540 EPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:cd03298 154 EPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
530-721 |
4.59e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 4.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKvfQVGNKDKMgIRDLT---LNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ----DMA 602
Cdd:PRK10584 7 VEVHHLKK--SVGQGEHE-LSILTgveLVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 603 QIR-KSLGLCPQHDVLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIA 681
Cdd:PRK10584 84 KLRaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 682 GSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTH 721
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHgtTLILVTH 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1379-1599 |
4.71e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.12 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIINELSKVY-DQRApllaVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV-RQ 1456
Cdd:PRK11231 1 MTLRTENLTVGYgTKRI----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQlAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1457 RMGYCPQFDALLDHMTGREmLVMYAR---------LRGIPERLINACVENTlrglLLEPHANKLVKTYSGGNKRKLSTGI 1527
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRE-LVAYGRspwlslwgrLSAEDNARVNQAMEQT----RINHLADRRLTDLSGGQRQRAFLAM 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1528 ALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1381-1591 |
4.76e-12 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 67.71 E-value: 4.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQrapLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS---SDIGKVRQR 1457
Cdd:COG1126 2 IEIENLHKSFGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 MGYCPQ-FdALLDHMTGREMlVMYA--RLRGIPErlinACVENTLRGLL----LEPHANKLVKTYSGGNK-RklsTGIA- 1528
Cdd:COG1126 79 VGMVFQqF-NLFPHLTVLEN-VTLApiKVKKMSK----AEAEERAMELLervgLADKADAYPAQLSGGQQqR---VAIAr 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1529 -LIGEPAVIFLDEPSTGMDP--VARRLlwDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:COG1126 150 aLAMEPKVMLFDEPTSALDPelVGEVL--DVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGR 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
549-742 |
4.88e-12 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 68.07 E-value: 4.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS--------------QDMAQIRKSLGLCPQH 614
Cdd:PRK10619 21 LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTRLTMVFQH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 615 DVLFDNLTVAEH-LYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRdlRSKF---LSGGMKRKLSIGIALIAGSKVLMLDE 690
Cdd:PRK10619 101 FNLWSHMTVLENvMEAPIQVLGLSKQEARERAVKYLAKVGIDERA--QGKYpvhLSGGQQQRVSIARALAMEPEVLLFDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 691 PTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:PRK10619 179 PTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1392-1572 |
5.11e-12 |
|
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: 66.61 E-value: 5.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1392 QRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHM 1471
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1472 TGREMLVMYARLRGIPERLInacvENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARR 1551
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180
....*....|....*....|.
gi 569000489 1552 LLWDTVARARESGKAIVITSH 1572
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1402-1550 |
5.59e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 5.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysissdigkvrQRMGYCP----------QFDALLDHM 1471
Cdd:PRK11000 22 INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-----------KRMNDVPpaergvgmvfQSYALYPHL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1472 TGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVAR 1550
Cdd:PRK11000 91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALR 169
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1381-1541 |
6.31e-12 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 69.10 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS------DIGKV 1454
Cdd:PRK11650 4 LKLQAVRKSYDGKTQ--VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQrmGYcpqfdALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:PRK11650 82 FQ--NY-----ALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154
|
....*..
gi 569000489 1535 VIFLDEP 1541
Cdd:PRK11650 155 VFLFDEP 161
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
548-741 |
7.99e-12 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 67.16 E-value: 7.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 548 GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHA-YIHGYEISQDMAQI---------RKSLGLCPQHDVl 617
Cdd:TIGR02323 18 GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerrrlmRTEWGFVHQNPR- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 618 fDNL--------TVAEHLY-----FYAQLKglslqkcpEEVKQMLHILSLEDKR--DLRSKFlSGGMKRKLSIGIALIAG 682
Cdd:TIGR02323 97 -DGLrmrvsagaNIGERLMaigarHYGNIR--------ATAQDWLEEVEIDPTRidDLPRAF-SGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 683 SKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLglAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
530-721 |
8.51e-12 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 67.40 E-value: 8.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGN-----KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQ 603
Cdd:PRK10419 4 LNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 604 IR-----------KSLG-LCPQHDVlfdNLTVAEHLyfyAQLKGLSLQKCPEEVKQMLHILSLEDK-RDLRSKFLSGGMK 670
Cdd:PRK10419 84 RKafrrdiqmvfqDSISaVNPRKTV---REIIREPL---RHLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 671 RKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTH 721
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKklQQQFGTACLFITH 210
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1381-1579 |
9.25e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 66.35 E-value: 9.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSkVYDQRAPLLAvdRISLAVQKGECFGLLGFNGAGKTTTFKMLTG---EETITSGDAFVGGYSISSdiGKVRQR 1457
Cdd:COG4136 2 LSLENLT-ITLGGRPLLA--PLSLTVAPGEILTLMGPSGSGKSTLLAAIAGtlsPAFSASGEVLLNGRRLTA--LPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1458 -MGYCPQFDALLDHMTGREMLvMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:COG4136 77 rIGILFQDDLLFPHLSVGENL-AFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTV-ARARESGKAIVITSHSMEECEA 1579
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEEDAPA 199
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1398-1575 |
9.26e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 67.45 E-value: 9.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-SDIGKVRQRMGYCPQF-DALLDHMTGRE 1475
Cdd:PRK13647 20 ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaENEKWVRSKVGLVFQDpDDQVFSSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1476 MLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWD 1555
Cdd:PRK13647 100 DVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLME 179
|
170 180
....*....|....*....|
gi 569000489 1556 TVARARESGKAIVITSHSME 1575
Cdd:PRK13647 180 ILDRLHNQGKTVIVATHDVD 199
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
551-699 |
9.93e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI----SQDMAQIRKSLGLCPQHDVLFDNLTVAEH 626
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYF----YAQLkglslqkcPEE-----VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA 697
Cdd:PRK11831 105 VAYplreHTQL--------PAPllhstVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
..
gi 569000489 698 VS 699
Cdd:PRK11831 177 IT 178
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1381-1572 |
1.09e-11 |
|
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: 65.03 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03247 1 LSINNVSFSYPEQEQQ-VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDhmtgremlvmyarlrgiperlinacveNTLRglllephaNKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03247 80 LNQRPYLFD---------------------------TTLR--------NNLGRRFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARAREsGKAIVITSH 1572
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLK-DKTLIWITH 155
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
530-740 |
1.17e-11 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 65.57 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF-QVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisqdmaqirkSL 608
Cdd:cd03250 1 ISVEDASFTWdSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 609 GLCPQHDVLFdNLTVAEHLYFYAQLKglslqkcPEEVKQMLHILSLEdkRDL-------------RSKFLSGGMKRKLSI 675
Cdd:cd03250 69 AYVSQEPWIQ-NGTIRENILFGKPFD-------EERYEKVIKACALE--PDLeilpdgdlteigeKGINLSGGQKQRISL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 676 GIALIAGSKVLMLDEPTSGMDAVSRRAIWD--LLQQQKSDRTVLLTTH---FMDEAdllgDRIAILAKGE 740
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNKTRILVTHqlqLLPHA----DQIVVLDNGR 204
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1402-1590 |
1.18e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI-------SSDIGKVRQRMGYCPQFDALLDHMTGR 1474
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMLVMY-ARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLL 1553
Cdd:PRK11124 101 QNLIEApCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQI 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000489 1554 WDTVARARESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:PRK11124 181 VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENG 217
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1376-1590 |
1.32e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYdqRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSdigKVR 1455
Cdd:PRK15056 2 MQQAGIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1456 QRM-GYCPQ-------FDALLDH--MTGREMLVMYARlrgIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLST 1525
Cdd:PRK15056 77 KNLvAYVPQseevdwsFPVLVEDvvMMGRYGHMGWLR---RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1526 GIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTrLAIMVQG 1590
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
550-746 |
1.71e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMA-QIRKSLGLCPQHDVLFDNLTVAEHL- 627
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASkEVARRIGLLAQNATTPGDITVQELVa 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 ---YFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIW 704
Cdd:PRK10253 104 rgrYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569000489 705 DLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK10253 184 ELLSELNREKgyTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1399-1572 |
1.90e-11 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 64.86 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEE--TITSGDAFVGGYSISSDIGKVRQRMGycpqfdalldhmtgreM 1476
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARLG----------------I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARlrgiPERLINACVENTLRGLllephaNklvKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDT 1556
Cdd:cd03217 80 FLAFQY----PPEIPGVKNADFLRYV------N---EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEV 146
|
170
....*....|....*.
gi 569000489 1557 VARARESGKAIVITSH 1572
Cdd:cd03217 147 INKLREEGKSVLIITH 162
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1409-1572 |
3.04e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 68.37 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1409 GECFGLLGFNGAGKTTTFKMLTGEetiTSGDAFVGgySISSDIGK----VRQRMGYCPQFDALLDHMTGREMLVMYARLR 1484
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGR---IQGNNFTG--TILANNRKptkqILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1485 gIPERL-----------------INACvENTLRGlllephaNKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDP 1547
Cdd:PLN03211 169 -LPKSLtkqekilvaesviselgLTKC-ENTIIG-------NSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
|
170 180
....*....|....*....|....*
gi 569000489 1548 VARRLLWDTVARARESGKAIVITSH 1572
Cdd:PLN03211 240 TAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1385-1603 |
3.04e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 3.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI----SSDIGKVRQRMGY 1460
Cdd:PRK11831 9 DMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSM 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMlVMYArLR---GIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRK--LSTGIALigEPAV 1535
Cdd:PRK11831 89 LFQSGALFTDMNVFDN-VAYP-LRehtQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRaaLARAIAL--EPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKS 1603
Cdd:PRK11831 165 IMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1406-1572 |
3.11e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1406 VQKGECFGLLGFNGAGKTTTFKMLTGEETITSGdafvggySISSDIgkvrqRMGYCPQFDALLDHMTGREMlvmyarLRG 1485
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEG-------EVDPEL-----KISYKPQYIKPDYDGTVEDL------LRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1486 IPERLINACVENTL-RGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDpVARRLlwdTVAR----- 1559
Cdd:PRK13409 424 ITDDLGSSYYKSEIiKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRL---AVAKairri 499
|
170
....*....|...
gi 569000489 1560 ARESGKAIVITSH 1572
Cdd:PRK13409 500 AEEREATALVVDH 512
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1378-1598 |
3.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.80 E-value: 3.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1378 DTPLIINELSKVYDQRAP--LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVR 1455
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQEneLVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1456 QRMGYCPQ----FDALldhmtgREMLVMYARLrgiPE-RLINACVEntlRGLLLEP--------HANKLVKTY------- 1515
Cdd:PRK13631 99 LITNPYSKkiknFKEL------RRRVSMVFQF---PEyQLFKDTIE---KDIMFGPvalgvkksEAKKLAKFYlnkmgld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1516 -----------SGGNKRKLS-TGIALIgEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTR 1583
Cdd:PRK13631 167 dsylerspfglSGGQKRRVAiAGILAI-QPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADE 245
|
250
....*....|....*
gi 569000489 1584 LAIMVQGQFKCLGSP 1598
Cdd:PRK13631 246 VIVMDKGKILKTGTP 260
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1402-1573 |
3.55e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 64.51 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIssDIGKVRQRMGYCPQFDALLDHMTGREMLVMYA 1481
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1482 RLRGIPERLINACVENTLRGLLLEPHANKLvktySGGNKRKLStgIA--LIGEPAVIFLDEPSTGMDPVARRLLWDTVAR 1559
Cdd:PRK13539 99 AFLGGEELDIAAALEAVGLAPLAHLPFGYL----SAGQKRRVA--LArlLVSNRPIWILDEPTAALDAAAVALFAELIRA 172
|
170
....*....|....
gi 569000489 1560 ARESGKAIVITSHS 1573
Cdd:PRK13539 173 HLAQGGIVIAATHI 186
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
546-721 |
3.78e-11 |
|
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: 65.65 E-value: 3.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 546 KMGIRDLTLNLYEGQITVL---------------LGHNGAGKTTTMSLLTGLFPpTSGHAYIHGYEI-SQDMAQIRKSLG 609
Cdd:cd03289 2 QMTVKDLTAKYTEGGNAVLenisfsispgqrvglLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWnSVPLQKWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 610 LCPQHDVLFDNlTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLR----SKFLSGGMKRKLSIGIALIAGSKV 685
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVlvdgGCVLSHGHKQLMCLARSVLSKAKI 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 686 LMLDEPTSGMDAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:cd03289 160 LLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEH 195
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
501-739 |
4.64e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 501 VGKEEEGSDPEKalrneyfEAEPEDLVagIKIKHLSKVFQVGnkdkmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLT 580
Cdd:PRK10982 231 VGRSLTQRFPDK-------ENKPGEVI--LEVRNLTSLRQPS------IRDVSFDLHKGEILGIAGLVGAKRTDIVETLF 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 581 GLFPPTSGHAYIHGYEISQDMA------------QIRKSLGLCPQHDVLFDNL--TVAEHLYFYAQLKGLSLQKCPEEVK 646
Cdd:PRK10982 296 GIREKSAGTITLHGKKINNHNAneainhgfalvtEERRSTGIYAYLDIGFNSLisNIRNYKNKVGLLDNSRMKSDTQWVI 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 647 QMLHILSLEDKRDLRSkfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDE 725
Cdd:PRK10982 376 DSMRVKTPGHRTQIGS--LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAElAKKDKGIIIISSEMPE 453
|
250
....*....|....*.
gi 569000489 726 adLLG--DRIAILAKG 739
Cdd:PRK10982 454 --LLGitDRILVMSNG 467
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1389-1599 |
4.70e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.62 E-value: 4.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1389 VYDQRAPLLA--VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIG-----KVRQRMGYC 1461
Cdd:PRK13641 11 IYSPGTPMEKkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlkKLRKKVSLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQF--------DALLDHMTG-----------REMLVMYARLRGIPERLINacventlrglllephanKLVKTYSGGNKRK 1522
Cdd:PRK13641 91 FQFpeaqlfenTVLKDVEFGpknfgfsedeaKEKALKWLKKVGLSEDLIS-----------------KSPFELSGGQMRR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1523 LSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQ 1599
Cdd:PRK13641 154 VAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPK 230
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
543-721 |
5.09e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 63.74 E-value: 5.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 543 NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISqdmaQIRKSLGLCPQHDV-LFDNL 621
Cdd:PRK13541 10 NIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNIN----NIAKPYCTYIGHNLgLKLEM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHLYFYAQLKGLSlqkcpEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:PRK13541 86 TVFENLKFWSEIYNSA-----ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD 160
|
170 180
....*....|....*....|.
gi 569000489 702 AIWDLL-QQQKSDRTVLLTTH 721
Cdd:PRK13541 161 LLNNLIvMKANSGGIVLLSSH 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1376-1601 |
5.73e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 64.99 E-value: 5.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLIINELSKVYDQRAPLLAVdriSLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS------- 1448
Cdd:PRK10619 1 MSENKLNVIDLHKRYGEHEVLKGV---SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1449 -------SDIGKVRQRMGYCPQFDALLDHMTGREMlVMYARLR--GIPERLINACVENTLRGLLLEPHAN-KLVKTYSGG 1518
Cdd:PRK10619 78 qlkvadkNQLRLLRTRLTMVFQHFNLWSHMTVLEN-VMEAPIQvlGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1519 NKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:PRK10619 157 QQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
...
gi 569000489 1599 QHL 1601
Cdd:PRK10619 237 EQL 239
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
534-725 |
5.95e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 64.35 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 534 HLSKV-FQVGnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLC 611
Cdd:PRK10247 9 QLQNVgYLAG--DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 612 PQHDVLFDNlTVAEHLYFYAQLKglslQKCPEEVKQMLHILSLEDKRDLRSK---FLSGGMKRKLSIGIALIAGSKVLML 688
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIR----NQQPDPAIFLDDLERFALPDTILTKniaELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 689 DEPTSGMDAVSRRAIWDLLQQQKSDR--TVLLTTHFMDE 725
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQniAVLWVTHDKDE 200
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
520-746 |
7.76e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 7.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 520 EAEPEDLVAgikIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY-------- 591
Cdd:PRK10261 6 ELDARDVLA---VENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQcdkmllrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 592 -----IHGYEISQ-DMAQIRKS-LGLCPQHDVLFDN--LTVAEHLYFYAQL-KGLSLQKCPEEVKQMLHILSLEDKRDLR 661
Cdd:PRK10261 83 rsrqvIELSEQSAaQMRHVRGAdMAMIFQEPMTSLNpvFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 662 SKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAIL 736
Cdd:PRK10261 163 SRYphqLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKvlQKEMSMGVIFITHDMGVVAEIADRVLVM 242
|
250
....*....|
gi 569000489 737 AKGELQCCGS 746
Cdd:PRK10261 243 YQGEAVETGS 252
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1377-1604 |
8.15e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 64.63 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1377 LDTPLI-INELSKVYDQRAPLlAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD-IGKV 1454
Cdd:PRK13632 3 NKSVMIkVENVSFSYPNSENN-ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYC---P--QFDALL---DHMTGREMlvmyarlRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTG 1526
Cdd:PRK13632 82 RKKIGIIfqnPdnQFIGATvedDIAFGLEN-------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1527 IALIGEPAVIFLDEpSTGM-DPVARRLLWDTVARARESGKAIVIT-SHSMEECeALCTRLAIMVQGQFKCLGSPQH-LKS 1603
Cdd:PRK13632 155 SVLALNPEIIIFDE-STSMlDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKLIAQGKPKEiLNN 232
|
.
gi 569000489 1604 K 1604
Cdd:PRK13632 233 K 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
531-740 |
8.73e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 64.18 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSKVFQVGNkdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHA-YIHGYEISQDMAQI----- 604
Cdd:PRK11701 8 SVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALseaer 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 ----RKSLGLCPQH--DVLFDNLT----VAEHLY-----FYAQLKglslqkcpEEVKQMLHILSLEDKR--DLRSKFlSG 667
Cdd:PRK11701 84 rrllRTEWGFVHQHprDGLRMQVSaggnIGERLMavgarHYGDIR--------ATAGDWLERVEIDAARidDLPTTF-SG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 668 GMKRKLSIGIALIAGSKVLMLDEPTSGMDaVSRRA-IWDLLQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK11701 155 GMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGLVRELglAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
522-742 |
8.89e-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: 66.39 E-value: 8.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 522 EPEDLVAGI-KIKHLSkVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPT-SGHAYIHGYE--- 596
Cdd:TIGR02633 249 EPHEIGDVIlEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPvdi 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 597 ------ISQDMAQI---RKSLGLCPQHDVlFDNLTVA--EHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDkrDLRSKFL 665
Cdd:TIGR02633 328 rnpaqaIRAGIAMVpedRKRHGIVPILGV-GKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKVKTASP--FLPIGRL 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 666 SGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFmdeADLLG--DRIAILAKGEL 741
Cdd:TIGR02633 405 SGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlaQEGVAIIVVSSEL---AEVLGlsDRVLVIGEGKL 481
|
.
gi 569000489 742 Q 742
Cdd:TIGR02633 482 K 482
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
549-776 |
1.08e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.92 E-value: 1.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIhgyeisqdmaqIRKSLGLCPQHDVLFdNLTVAEHLY 628
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIF-NATVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 FYAQLKGLSLQKCPEeVKQMLHILSLEDKRDL-----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA-VSRRA 702
Cdd:PLN03232 701 FGSDFESERYWRAID-VTALQHDLDLLPGRDLteigeRGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhVAHQV 779
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 703 IWDLLQQQKSDRTVLLTT---HFMDeadlLGDRIAILAKGELQCCG--------SSLFLKQKYGAGyHMTLVKEPHCNPE 771
Cdd:PLN03232 780 FDSCMKDELKGKTRVLVTnqlHFLP----LMDRIILVSEGMIKEEGtfaelsksGSLFKKLMENAG-KMDATQEVNTNDE 854
|
....*
gi 569000489 772 GISQL 776
Cdd:PLN03232 855 NILKL 859
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1381-1572 |
1.17e-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: 62.90 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAPLlavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGY 1460
Cdd:cd03231 1 LEADELTCERDGRALF---SGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQFDALLDHMTGREMLVMYARLRGiPERLINACVENTLRGLLLEPhanklVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRFWHADHS-DEQVEEALARVGLNGFEDRP-----VAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVITSH 1572
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1398-1632 |
1.36e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 63.68 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysissDIGKVRQRMGycpqfdaLLDHMTGREML 1477
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAG-------LSGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP-STGMDPVARRLLwDT 1556
Cdd:PRK13546 107 EFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCL-DK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1557 VARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFgSGYSLQAKVRSEGKQdalEEFKAFVD 1632
Cdd:PRK13546 186 IYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKY-EAFLNDFKKKSKAEQ---KEFRNKLD 257
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
530-766 |
1.46e-10 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 65.98 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGL--FPPTSGHAYIH-------GY----- 595
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYHvalcekcGYverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 596 --------------EISQDM--------AQIRKSLGLCPQHD-VLFDNLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHIL 652
Cdd:TIGR03269 77 kvgepcpvcggtlePEEVDFwnlsdklrRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 653 SLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLG 730
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVIEDLS 236
|
250 260 270
....*....|....*....|....*....|....*.
gi 569000489 731 DRIAILAKGELQCCGSSLFLKQKYgagyhMTLVKEP 766
Cdd:TIGR03269 237 DKAIWLENGEIKEEGTPDEVVAVF-----MEGVSEV 267
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1398-1626 |
1.50e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 65.68 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKvrqrmgycpqfdALLDHMTGREML 1477
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP-STGMDPVARRLLwDT 1556
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlSVGDQTFTKKCL-DK 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1557 VARARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAKVRSEGKQDALEE 1626
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFLKKYNQMSVEERKDFREE 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1398-1591 |
1.56e-10 |
|
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: 65.62 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG--EETITSGDAFVGGYSISSD---------IGKVRQRMGYCPQFDA 1466
Cdd:TIGR02633 16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASnirdteragIVIIHQELTLVPELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 LLDHMTGREmLVMYARLRGIPERLINAcvENTLRGLLLEPHANKL-VKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:TIGR02633 96 AENIFLGNE-ITLPGGRMAYNAMYLRA--KNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 1546 DPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:TIGR02633 173 TEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
552-696 |
1.74e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 62.56 E-value: 1.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQhdvLFDNLTVAEHLYFY 630
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLPG---LKADLSTLENLHFL 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 631 AQLKGLSLQKCPEEVkqmLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:PRK13543 107 CGLHGRRAKQMPGSA---LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1379-1591 |
1.93e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 63.16 E-value: 1.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIINELSKVYDQRAPLLAVDrisLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRqrm 1458
Cdd:PRK11247 11 TPLLLNAVSKRYGERTVLNQLD---LHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 gycpqfdalldhmtgreMLVMYARLrgIP-ERLIN-----------ACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTG 1526
Cdd:PRK11247 85 -----------------LMFQDARL--LPwKKVIDnvglglkgqwrDAALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1527 IALIGEPAVIFLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1390-1570 |
2.06e-10 |
|
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: 62.63 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1390 YDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALL 1468
Cdd:cd03253 10 YDPGRPVL--KDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQ-DTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 DHMTGREMlVMYARLRGIPERLINAC--------VEN------TL---RGLLLephanklvktySGGNKRKLSTGIALIG 1531
Cdd:cd03253 87 FNDTIGYN-IRYGRPDATDEEVIEAAkaaqihdkIMRfpdgydTIvgeRGLKL-----------SGGEKQRVAIARAILK 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 1532 EPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVIT 1570
Cdd:cd03253 155 NPPILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA 193
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
553-692 |
2.26e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 65.02 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 553 TLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI-------SQD--MAQIRKSLGLCPQhdvlfdnLTV 623
Cdd:PRK10762 24 ALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpksSQEagIGIIHQELNLIPQ-------LTI 96
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 624 AEHLY----FYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:PRK10762 97 AENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
552-752 |
2.32e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 63.27 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNLTVAEHL--- 627
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVaig 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 -YFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDL 706
Cdd:PRK10575 110 rYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLAL 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 569000489 707 LQQQKSDR--TVLLTTHFMDEADLLGDRIAILAKGELQCCGSSLFLKQ 752
Cdd:PRK10575 190 VHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1397-1612 |
2.32e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 63.23 E-value: 2.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD--------IGKVRQR-----MGYCPQ 1463
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnfeklrkhIGIVFQNpdnqfVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1464 FD---ALLDHMTGREMLVmyarlRGIPERLINAcveNTLRGLLLEPHAnklvktYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:PRK13648 103 YDvafGLENHAVPYDEMH-----RRVSEALKQV---DMLERADYEPNA------LSGGQKQRVAIAGVLALNPSVIILDE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESgKAIVITSHSMEECEAL-CTRLAIMVQGQFKCLGSPQHLkskFGSGYSLQ 1612
Cdd:PRK13648 169 ATSMLDPDARQNLLDLVRKVKSE-HNITIISITHDLSEAMeADHVIVMNKGTVYKEGTPTEI---FDHAEELT 237
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1406-1572 |
2.34e-10 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 65.19 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1406 VQKGECFGLLGFNGAGKTTTFKMLTGEETITSGdafvggySISSDIgkvrqRMGYCPQFDALLDHMTGREMLvmyarLRG 1485
Cdd:COG1245 363 IREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG-------EVDEDL-----KISYKPQYISPDYDGTVEEFL-----RSA 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1486 IPERLINACVENTL-RGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDpVARRLlwdTVAR----- 1559
Cdd:COG1245 426 NTDDFGSSYYKTEIiKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-VEQRL---AVAKairrf 501
|
170
....*....|...
gi 569000489 1560 ARESGKAIVITSH 1572
Cdd:COG1245 502 AENRGKTAMVVDH 514
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
530-742 |
2.70e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.91 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQV--GNKDKM--------------GIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIH 593
Cdd:PRK13546 5 VNIKNVTKEYRIyrTNKERMkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 594 GyeisqDMAQIRKSLGLCPQhdvlfdnLTVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKL 673
Cdd:PRK13546 85 G-----EVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 674 SIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQK-SDRTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:PRK13546 153 GFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
530-740 |
2.78e-10 |
|
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: 64.85 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP--PTSGHAYIHGYEI-SQDMAQI-R 605
Cdd:TIGR02633 2 LEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkASNIRDTeR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSLGLCPQHDVLFDNLTVAEHLYFYAQ--LKGlSLQKCPEEV---KQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIAL 679
Cdd:TIGR02633 78 AGIVIIHQELTLVPELSVAENIFLGNEitLPG-GRMAYNAMYlraKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 569000489 680 IAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTV-LLTTHFMDEADLLGDRIAILAKGE 740
Cdd:TIGR02633 157 NKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVAcVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1390-1606 |
3.16e-10 |
|
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: 62.24 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1390 YDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALL 1468
Cdd:cd03254 12 YDEKKPVL--KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ-DTFL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 DHMTGREMLvMYARLRGIPERLINAC--------VENTLRGllLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:cd03254 89 FSGTIMENI-RLGRPNATDEEVIEAAkeagahdfIMKLPNG--YDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESGKAIVItSHsmeecealctRLA-------IMV--QGQFKCLGSPQHLKSKFG 1606
Cdd:cd03254 166 ATSNIDTETEKLIQEALEKLMKGRTSIII-AH----------RLStiknadkILVldDGKIIEEGTHDELLAKKG 229
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1413-1601 |
3.58e-10 |
|
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: 63.58 E-value: 3.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1413 GLLGFNGAGKTTTFKMLTGEETITSGDAFVGG---YSISSDIG-KVRQR-MGYCPQFDALLDHMTGREMLvMYARLRGIP 1487
Cdd:COG4148 29 ALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGIFlPPHRRrIGYVFQEARLFPHLSVRGNL-LYGRKRAPR 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1488 ER---LINACVEntLRGL--LLEPHANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVAR-AR 1561
Cdd:COG4148 108 AErriSFDEVVE--LLGIghLLDRRPATL----SGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYLERlRD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 1562 ESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:COG4148 182 ELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
532-721 |
4.36e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 63.20 E-value: 4.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPP---TSGHAYIHGYEI----SQDMAQI 604
Cdd:PRK09473 15 VKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSlglcpQHDVLF-DNLT-------VAEHLYFYAQL-KGLSLQKCPEEVKQMLHILSLEDKRDLRSKF---LSGGMKRK 672
Cdd:PRK09473 95 RAE-----QISMIFqDPMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMKMYpheFSGGMRQR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 673 LSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD--RTVLLTTH 721
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfnTAIIMITH 220
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1359-1575 |
4.38e-10 |
|
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: 64.23 E-value: 4.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1359 QDVAEERSRILVPSLDSMLD--TPLIINELSKVYDQRAPllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETIT 1436
Cdd:TIGR02857 298 FAVLDAAPRPLAGKAPVTAApaSSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1437 SGDAFVGGYSISS-DIGKVRQRMGYCPQFDALLDHmTGREMLVMY---ARLRGIPERLINACVENTLRGL------LLEP 1506
Cdd:TIGR02857 376 EGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAENIRLArpdASDAEIREALERAGLDEFVAALpqgldtPIGE 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1507 HANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARAREsGKAIVITSHSME 1575
Cdd:TIGR02857 455 GGAGL----SGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1350-1572 |
4.61e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 64.87 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1350 NRTSVLPEDQDVAEERSRIL--VP---SLDSM---LDTPLIINElSKVYDQRAPLLAvdRISLAVQKGECFGLLGFNGAG 1421
Cdd:PLN03140 842 NRDSSLEAANGVAPKRGMVLpfTPlamSFDDVnyfVDMPAEMKE-QGVTEDRLQLLR--EVTGAFRPGVLTALMGVSGAG 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1422 KTTTFKMLTGEETitsgdafvGGYsISSDI-----GKVRQRM----GYCPQFDALLDHMTGREMLVMYARLR-----GIP 1487
Cdd:PLN03140 919 KTTLMDVLAGRKT--------GGY-IEGDIrisgfPKKQETFarisGYCEQNDIHSPQVTVRESLIYSAFLRlpkevSKE 989
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1488 ERLInaCVENTLRGLLLEPHANKLV-----KTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARE 1562
Cdd:PLN03140 990 EKMM--FVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVD 1067
|
250
....*....|
gi 569000489 1563 SGKAIVITSH 1572
Cdd:PLN03140 1068 TGRTVVCTIH 1077
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
552-742 |
4.75e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 64.22 E-value: 4.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIRKslglcpqhdvLFDNLTVAEHLyFY 630
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRK----------LFSAVFTDFHL-FD 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 631 AQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKF-----LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD 705
Cdd:PRK10522 411 QLLGPEGKPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQ 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 706 LL--QQQKSDRTVLLTTH---FMDEAdllgDRIAILAKGELQ 742
Cdd:PRK10522 491 VLlpLLQEMGKTIFAISHddhYFIHA----DRLLEMRNGQLS 528
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
553-741 |
5.66e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 63.78 E-value: 5.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 553 TLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQ--IRKSLGLCPQhDVLFDNL----TVAEH 626
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdaIRAGIMLCPE-DRKAEGIipvhSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYFYAQLK----GLSLQKCPEEVKQMLHILSLEDK---RDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:PRK11288 352 INISARRHhlraGCLINNRWEAENADRFIRSLNIKtpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGA 431
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 700 RRAIWDLLQQ-QKSDRTVLLTTHfmDEADLLG--DRIAILAKGEL 741
Cdd:PRK11288 432 KHEIYNVIYElAAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1381-1546 |
6.14e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 6.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAfvgGYSISSDIgkvrqrmGY 1460
Cdd:PRK15064 320 LEVENLTKGFDNG-PLF--KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV---KWSENANI-------GY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1461 CPQ-----FD---ALLDHMT------GREMLVmyarlRGIPERLinacventlrgLLLEPHANKLVKTYSGGNKRKLSTG 1526
Cdd:PRK15064 387 YAQdhaydFEndlTLFDWMSqwrqegDDEQAV-----RGTLGRL-----------LFSQDDIKKSVKVLSGGEKGRMLFG 450
|
170 180
....*....|....*....|
gi 569000489 1527 IALIGEPAVIFLDEPSTGMD 1546
Cdd:PRK15064 451 KLMMQKPNVLVMDEPTNHMD 470
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
530-741 |
6.16e-10 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.94 E-value: 6.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKT-TTMSLLtGLFPP----TSGHAYIHGYEISQ----D 600
Cdd:COG4172 7 LSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLLGlserE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQIR-KSLG---------LCPQHdvlfdnlTVAEhlyfyaQL-------KGLSLQKCPEEVKQMLHILSLEDKRDLRSK 663
Cdd:COG4172 86 LRRIRgNRIAmifqepmtsLNPLH-------TIGK------QIaevlrlhRGLSGAAARARALELLERVGIPDPERRLDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 664 F---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHfmdeaDL-----LGDRI 733
Cdd:COG4172 153 YphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKdlQRELGMALLLITH-----DLgvvrrFADRV 227
|
....*...
gi 569000489 734 AILAKGEL 741
Cdd:COG4172 228 AVMRQGEI 235
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
551-721 |
7.14e-10 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 61.67 E-value: 7.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyEISQDmAQIRksLGLCPQHDVLFDN--LTVAEHLY 628
Cdd:PRK09544 22 DVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG-------VIKRN-GKLR--IGYVPQKLYLDTTlpLTVNRFLR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 FYAQLKGLSLQKCPEEVkQMLHILsledkrDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ 708
Cdd:PRK09544 92 LRPGTKKEDILPALKRV-QAGHLI------DAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170
....*....|....*
gi 569000489 709 QQKS--DRTVLLTTH 721
Cdd:PRK09544 165 QLRRelDCAVLMVSH 179
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
545-721 |
8.52e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 63.58 E-value: 8.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 545 DKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTV 623
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TV 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLyfyAQLKGLSLQKCPEEVKQM--LH--ILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGM 695
Cdd:PRK10789 406 ANNI---ALGRPDATQQEIEHVARLasVHddILRLPQGYDTevgeRGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180
....*....|....*....|....*.
gi 569000489 696 DAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGRTVIISAH 508
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1408-1643 |
1.00e-09 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 60.88 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1408 KGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISsdigkvrqrmgYCPQFDALLDHMTGREMlvmyarLRGIP 1487
Cdd:cd03237 24 ESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-----------YKPQYIKADYEGTVRDL------LSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1488 ERLINACVENT--LRGLLLEPHANKLVKTYSGGNKRKLSTGIALiGEPAVIFL-DEPSTGMDpVARRLLWDTVAR--ARE 1562
Cdd:cd03237 87 KDFYTHPYFKTeiAKPLQIEQILDREVPELSGGELQRVAIAACL-SKDADIYLlDEPSAYLD-VEQRLMASKVIRrfAEN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1563 SGKAIVITSHSMEECEALCTRLaIMVQGQfkclgspqhlKSKFGSGYSLQAKVrsegkqDALEEFKAFVDLTF------- 1635
Cdd:cd03237 165 NEKTAFVVEHDIIMIDYLADRL-IVFEGE----------PSVNGVANPPQSLR------SGMNRFLKNLDITFrrdpetg 227
|
250
....*....|....
gi 569000489 1636 ------PGSILEDE 1643
Cdd:cd03237 228 rprinkLGSVKDRE 241
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1399-1591 |
1.07e-09 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 61.24 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-------------------DIGKVRQRMG 1459
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraqrkafrrdiqmvfqdSISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVMYARLRGIperlinacventLRGLLLEP-HANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:PRK10419 108 VREIIREPLRHLLSLDKAERLARASEM------------LRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1539 DEPSTGMDPVARRLLWDTVARARE-SGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQ 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1375-1575 |
1.19e-09 |
|
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: 63.22 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1375 SMLDTPLIINELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGK 1453
Cdd:TIGR01193 468 NNLNGDIVINDVSYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHT 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1454 VRQRMGYCPQfDALLDHMTGREMLVMYARLRGIPERLINAC--------VENTLRGL--LLEPHANKLvktySGGNKRKL 1523
Cdd:TIGR01193 546 LRQFINYLPQ-EPYIFSGSILENLLLGAKENVSQDEIWAACeiaeikddIENMPLGYqtELSEEGSSI----SGGQKQRI 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1524 STGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARAREsgKAIVITSHSME 1575
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLS 670
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
549-760 |
1.34e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.43 E-value: 1.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTttmSLLTGLF---PPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVA 624
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDPVLFSG-SLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHLYFYAQLKGLSLQKCPEEVKQMLHILSLEDKRDLR----SKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR 700
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHEcaegGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLETD 1457
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 701 RAIWDLLQQQKSDRTVLLTTH----FMDEAdllgdRIAILAKGELQCCGSSLFLKQKYGAGYHM 760
Cdd:TIGR00957 1458 NLIQSTIRTQFEDCTVLTIAHrlntIMDYT-----RVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1385-1617 |
1.44e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI---SSDIGKVRQRMGYC 1461
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpGAERGVVFQNEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PQFDALLDHMTGREmlvmyarLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEP 1541
Cdd:PRK11248 83 PWRNVQDNVAFGLQ-------LAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1542 STGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLgspQHLKSKFGSGYSLQAKVRS 1617
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAGESSRS 229
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
561-741 |
1.48e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.88 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 561 ITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY-----IHGYEI--SQDMAQIRKSLGLCPQHDVLF-----DNLTV---AE 625
Cdd:PRK14271 49 VTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIfnYRDVLEFRRRVGMLFQRPNPFpmsimDNVLAgvrAH 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLSLQKCPEevkqmLHILSLEDKRDLRSKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIW 704
Cdd:PRK14271 129 KLVPRKEFRGVAQARLTE-----VGLWDAVKDRLSDSPFrLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIE 203
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000489 705 DLLQQQKSDRTVLLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK14271 204 EFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1402-1608 |
1.53e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 60.63 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTT---TFKMLT--GEETITSGDAFVGG---YSISSDIGKVRQRMGYCPQFDALLDHMTG 1473
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGrniYSPDVDPIEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1474 REMLVMYARLRGI--PERLINACVENTLRGLLLEPHANKLVKTY----SGGNKRKLSTGIALIGEPAVIFLDEPSTGMDP 1547
Cdd:PRK14267 103 YDNVAIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDRLNDYpsnlSGGQRQRLVIARALAMKPKILLMDEPTANIDP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1548 VARRLLWDTVARARESgKAIVITSHSMEECEALCTRLAIMVQGQF-------KCLGSPQH-LKSKFGSG 1608
Cdd:PRK14267 183 VGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLievgptrKVFENPEHeLTEKYVTG 250
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1402-1601 |
1.53e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.45 E-value: 1.53e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLT------GEETITSGDAFVGGYSI-SSDIGKVRQRMGYCPQFDALLDHMTGR 1474
Cdd:PRK14246 29 ITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHLSIY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMLVMYARLRGIPE-RLINACVENTLR--GLLLEPH--ANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVA 1549
Cdd:PRK14246 109 DNIAYPLKSHGIKEkREIKKIVEECLRkvGLWKEVYdrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVN 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1550 RRLLWDTVARARESgKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK14246 189 SQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1398-1592 |
1.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 1.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGeetITSGDA-----------FVG-GYSISSDIGKVRQRMGYCPQFD 1465
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG---IYTRDAgsilylgkevtFNGpKSSQEAGIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 ALLDHMTGREMLvmyARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:PRK10762 96 IAENIFLGREFV---NRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 569000489 1546 DPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:PRK10762 173 TDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
549-741 |
2.00e-09 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 59.35 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHL 627
Cdd:cd03369 24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIPQDPTLFSG-TIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYAQLKGlslqkcpEEVKQMLHILSLEDKrdlrskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL 707
Cdd:cd03369 103 DPFDEYSD-------EEIYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALIQKTI 168
|
170 180 190
....*....|....*....|....*....|....*
gi 569000489 708 QQQKSDRTVLLTTHFMDE-ADLlgDRIAILAKGEL 741
Cdd:cd03369 169 REEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1390-1572 |
2.41e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 62.10 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1390 YDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALL 1468
Cdd:COG1132 349 YPGDRPVL--KDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTFL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 DHMTGREMLvMYARLRGIPERLINAC----VENTLRGL------LLEPHANKLvktySGGNKRKLStgIA--LIGEPAVI 1536
Cdd:COG1132 426 FSGTIRENI-RYGRPDATDEEVEEAAkaaqAHEFIEALpdgydtVVGERGVNL----SGGQRQRIA--IAraLLKDPPIL 498
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARAREsGKAIVITSH 1572
Cdd:COG1132 499 ILDEATSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1376-1600 |
2.65e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 59.94 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLI-INELSKVYdqrAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSG----DAFVGGYSISSD 1450
Cdd:PRK11701 1 MMDQPLLsVRGLTKLY---GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGevhyRMRDGQLRDLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1451 IGKVRQRM------GYCPQfdallDHMTGREMLV-----MYARLRGIPER---LINACVENTLRGLLLEP-HANKLVKTY 1515
Cdd:PRK11701 78 LSEAERRRllrtewGFVHQ-----HPRDGLRMQVsaggnIGERLMAVGARhygDIRATAGDWLERVEIDAaRIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1516 SGGNKRKLSTGIALIGEPAVIFLDEPSTGMD-PVARRLLwDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQF- 1592
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvSVQARLL-DLLRGlVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVv 231
|
250
....*....|....
gi 569000489 1593 ------KCLGSPQH 1600
Cdd:PRK11701 232 esgltdQVLDDPQH 245
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1346-1572 |
2.76e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.87 E-value: 2.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1346 AELQNRTSVLPEDQDVAEERSRILVPSLDSMLDTPLIINELSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTT 1425
Cdd:TIGR03719 288 ARLARYEELLSQEFQKRNETAEIYIPPGPRLGDKVIEAENLTKAFGDK---LLIDDLSFKLPPGGIVGVIGPNGAGKSTL 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1426 FKMLTGEETITSGdAFVGGYSIssdigkvrqRMGYCPQF-DALLDHMT-------GREMLVMYArlRGIPERLInaCVEN 1497
Cdd:TIGR03719 365 FRMITGQEQPDSG-TIEIGETV---------KLAYVDQSrDALDPNKTvweeisgGLDIIKLGK--REIPSRAY--VGRF 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1498 TLRGlllePHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPvarrllwDTVaRARES------GKAIVItS 1571
Cdd:TIGR03719 431 NFKG----SDQQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV-------ETL-RALEEallnfaGCAVVI-S 497
|
.
gi 569000489 1572 H 1572
Cdd:TIGR03719 498 H 498
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
559-721 |
2.78e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 61.82 E-value: 2.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 559 GQITVLLGHNGAGKTTTMSLLTGLFPPTS--GHAYIHGYEISQdmaQIRKSLGLCPQHDVLFDNLTVAEHLYFYAQL--- 633
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLrlp 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 634 KGLSLQ---KCPEEVKQMLHILSLEDKRDLRS--KFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR-RAIWDLL 707
Cdd:PLN03211 171 KSLTKQekiLVAESVISELGLTKCENTIIGNSfiRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLG 250
|
170
....*....|....
gi 569000489 708 QQQKSDRTVLLTTH 721
Cdd:PLN03211 251 SLAQKGKTIVTSMH 264
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1399-1593 |
2.91e-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: 61.76 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGE-ETITSGDAFVGGY---------SISSDIGKV---RQRMGYCPQFD 1465
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKpvdirnpaqAIRAGIAMVpedRKRHGIVPILG 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 -------ALLDHMTGREMLVMYARLRGIPERLINACVENTlrglllepHANKLVKTYSGGNKRKLSTGIALIGEPAVIFL 1538
Cdd:TIGR02633 356 vgknitlSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTA--------SPFLPIGRLSGGNQQKAVLAKMLLTNPRVLIL 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1539 DEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFK 1593
Cdd:TIGR02633 428 DEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1399-1591 |
2.95e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.56 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD------------IGKVRQRmgycpqfDA 1466
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangivyISEDRKR-------DG 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 LLDHMTGREMLVMYA---------RLRGIPERLInacVENTLRGLLLE-PHANKLVKTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:PRK10762 341 LVLGMSVKENMSLTAlryfsraggSLKHADEQQA---VSDFIRLFNIKtPSMEQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
549-739 |
3.12e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 59.20 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTG--LFPPTSGHAYIHGYEISQDmaqirkslglcpqhdvlfdnLTVAEH 626
Cdd:COG2401 46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGRE--------------------ASLIDA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYfyaqlkglsLQKCPEEVKQMLHILSLEDKRDLRSKF--LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIW 704
Cdd:COG2401 106 IG---------RKGDFKDAVELLNAVGLSDAVLWLRRFkeLSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 569000489 705 DLLQQ--QKSDRTVLLTTHFMD-EADLLGDRIAILAKG 739
Cdd:COG2401 177 RNLQKlaRRAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1402-1599 |
3.19e-09 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 59.26 E-value: 3.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-------SDIGKVRQRMGYCPQFDALLDHMTGR 1474
Cdd:COG4161 21 INLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqkpseKAIRLLRQKVGMVFQQYNLWPHLTVM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMLVMY-ARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLL 1553
Cdd:COG4161 101 ENLIEApCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQV 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 1554 WDTVARARESGKAIVITSHSMEECEALCTRLA------IMVQGQFKCLGSPQ 1599
Cdd:COG4161 181 VEIIRELSQTGITQVIVTHEVEFARKVASQVVymekgrIIEQGDASHFTQPQ 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
528-721 |
4.02e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 59.51 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFQVGNKdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQdmaQIRKS 607
Cdd:PRK15056 5 AGIVVNDVTVTWRNGHT---ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 L-GLCPQHD-------VLFDNLTVAEHlyfYAQLKGLSLQKCPEE--VKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGI 677
Cdd:PRK15056 79 LvAYVPQSEevdwsfpVLVEDVVMMGR---YGHMGWLRRAKKRDRqiVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 678 ALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTH 721
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEgKTMLVSTH 200
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1379-1546 |
4.05e-09 |
|
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: 58.43 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIINELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG--EETI-TSGDAFVGGYSISSDIGKVR 1455
Cdd:cd03233 5 SWRNISFTTGKGRSKIPIL--KDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtEGNVsVEGDIHYNGIPYKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1456 QRMGYCPQFDALLDHMTGREMLVMYARLRGiperlinacventlrglllephaNKLVKTYSGGNKRKLSTGIALIGEPAV 1535
Cdd:cd03233 83 GEIIYVSEEDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASV 139
|
170
....*....|.
gi 569000489 1536 IFLDEPSTGMD 1546
Cdd:cd03233 140 LCWDNSTRGLD 150
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1413-1598 |
4.34e-09 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 59.64 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1413 GLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS-SDIG--KVRQRMGYCPQFDALLDHMTGREMLVMYA-RLRGIPE 1488
Cdd:PRK13638 31 GLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDySKRGllALRQQVATVFQDPEQQIFYTDIDSDIAFSlRNLGVPE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1489 RLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIV 1568
Cdd:PRK13638 111 AEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVI 190
|
170 180 190
....*....|....*....|....*....|
gi 569000489 1569 ITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:PRK13638 191 ISSHDIDLIYEISDAVYVLRQGQILTHGAP 220
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
504-747 |
4.50e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 61.72 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 504 EEEGSDPEKALRNEYFEAEPEDLvagikikhlskvfqvgnkdkmgIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLF 583
Cdd:PTZ00243 653 SERSAKTPKMKTDDFFELEPKVL----------------------LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQF 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 584 pptsghayihgyEISQDMAQIRKSLGLCPQHDVLFdNLTVAEHLYFYAQLKGLSLQKCPeEVKQM---LHILS--LEDKR 658
Cdd:PTZ00243 711 ------------EISEGRVWAERSIAYVPQQAWIM-NATVRGNILFFDEEDAARLADAV-RVSQLeadLAQLGggLETEI 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 659 DLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA-VSRRAIWDLLQQQKSDRTVLLTTHfmdEADLL--GDRIAI 735
Cdd:PTZ00243 777 GEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGERVVEECFLGALAGKTRVLATH---QVHVVprADYVVA 853
|
250
....*....|..
gi 569000489 736 LAKGELQCCGSS 747
Cdd:PTZ00243 854 LGDGRVEFSGSS 865
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1390-1601 |
5.33e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 59.34 E-value: 5.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1390 YDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSD-IGKVRQRMGYCPQF-DAL 1467
Cdd:PRK13642 14 YEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNpDNQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1468 LDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDP 1547
Cdd:PRK13642 94 FVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1548 VARRLLWDTVARARESGKAIVIT-SHSMEECeALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK13642 174 TGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEIIKEAAPSEL 227
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1402-1574 |
6.63e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.59 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGeetitsgdafvggySISSDIGKVRQ----RMGYCPQ---FDALLDHMTGR 1474
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLG--------------LVAPDEGVIKRngklRIGYVPQklyLDTTLPLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 EMlvmyaRLR-GIPERLINACVENTLRGLLLEPHANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLL 1553
Cdd:PRK09544 89 FL-----RLRpGTKKEDILPALKRVQAGHLIDAPMQKL----SGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180
....*....|....*....|..
gi 569000489 1554 WDTVARAR-ESGKAIVITSHSM 1574
Cdd:PRK09544 160 YDLIDQLRrELDCAVLMVSHDL 181
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1398-1569 |
8.09e-09 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 58.01 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQfDALLDHMTGREM 1476
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQ-DVFLFNDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 lVMYARLRGIPERLINAC--------VENTLRGL--LLEPHANKLvktySGGNKRKLSTGIALIGEPAVIFLDEPSTGMD 1546
Cdd:cd03251 96 -IAYGRPGATREEVEEAAraanahefIMELPEGYdtVIGERGVKL----SGGQRQRIAIARALLKDPPILILDEATSALD 170
|
170 180
....*....|....*....|...
gi 569000489 1547 PVARRLLWDTVARARESGKAIVI 1569
Cdd:cd03251 171 TESERLVQAALERLMKNRTTFVI 193
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1381-1575 |
8.25e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.94 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRAP--LLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSG-------------------- 1438
Cdd:PRK13651 3 IKVKNIVKIFNKKLPteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtiewifkdeknkkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1439 --DAFVGGYSISSDIGKV---RQRMGYCPQF-DALLDHMTGREMLVMYARLRGIPERlinacventlrglllepHANKLV 1512
Cdd:PRK13651 83 vlEKLVIQKTRFKKIKKIkeiRRRVGVVFQFaEYQLFEQTIEKDIIFGPVSMGVSKE-----------------EAKKRA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1513 KTY------------------SGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSM 1574
Cdd:PRK13651 146 AKYielvgldesylqrspfelSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL 225
|
.
gi 569000489 1575 E 1575
Cdd:PRK13651 226 D 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
511-741 |
8.96e-09 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.04 E-value: 8.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 511 EKALRNEYFEAEPEDLVagIKIKHLSkvfQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHA 590
Cdd:COG3845 241 EVLLRVEKAPAEPGEVV--LEVENLS---VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSI 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 591 YIHGYEIS-QDMAQIRKsLGLC-----PQHDVLFDNLTVAEHL---YFYAQ--LKGLSLQKcpEEVKQM-LHILSLEDKR 658
Cdd:COG3845 316 RLDGEDITgLSPRERRR-LGVAyipedRLGRGLVPDMSVAENLilgRYRRPpfSRGGFLDR--KAIRAFaEELIEEFDVR 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 659 ----DLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWD-LLQQQKSDRTVLLTTHFMDEADLLGDRI 733
Cdd:COG3845 393 tpgpDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQrLLELRDAGAAVLLISEDLDEILALSDRI 472
|
....*...
gi 569000489 734 AILAKGEL 741
Cdd:COG3845 473 AVMYEGRI 480
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1399-1593 |
1.30e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGE-ETITSGDAFVGGY---------SISSDIGKV---RQRMGYCPQFD 1465
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDGKpvkirnpqqAIAQGIAMVpedRKRDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 -------ALLDHMTGREMLVMYARLRgiperlinaCVENTLRGLLLE-PHANKLVKTYSGGNKRKLSTGIALIGEPAVIF 1537
Cdd:PRK13549 358 vgknitlAALDRFTGGSRIDDAAELK---------TILESIQRLKVKtASPELAIARLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1538 LDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQFK 1593
Cdd:PRK13549 429 LDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1402-1610 |
1.42e-08 |
|
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: 59.43 E-value: 1.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEEtitsgdafvggySISSDIGKVRQRMGYCPQ------------------ 1463
Cdd:TIGR03269 19 ISFTIEEGEVLGILGRSGAGKSVLMHVLRGMD------------QYEPTSGRIIYHVALCEKcgyverpskvgepcpvcg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1464 ---------FDALLDHMTG---REMLVMYARLRGIPERliNACVENTLRGL---------------------LLEPHANK 1510
Cdd:TIGR03269 87 gtlepeevdFWNLSDKLRRrirKRIAIMLQRTFALYGD--DTVLDNVLEALeeigyegkeavgravdliemvQLSHRITH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1511 LVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQ 1589
Cdd:TIGR03269 165 IARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKAIWLEN 244
|
250 260
....*....|....*....|.
gi 569000489 1590 GQFKCLGSPQHLKSKFGSGYS 1610
Cdd:TIGR03269 245 GEIKEEGTPDEVVAVFMEGVS 265
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
525-707 |
1.58e-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: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 525 DLVagIKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIhGYEIsqDMAQI 604
Cdd:TIGR03719 320 DKV--IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--KLAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 605 RKSlglcpqHDVLFDNLTVAehlyfyaqlkglslqkcpEEVKQMLHILSLEDK----RDLRSKF-------------LSG 667
Cdd:TIGR03719 391 DQS------RDALDPNKTVW------------------EEISGGLDIIKLGKReipsRAYVGRFnfkgsdqqkkvgqLSG 446
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 668 GMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL 707
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL 486
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1402-1593 |
2.00e-08 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 56.71 E-value: 2.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVR-----QRMGYCPQFDALLDHMTGREM 1476
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARaklraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDpvarRLLWDT 1556
Cdd:PRK10584 109 VELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD----RQTGDK 184
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 569000489 1557 VARA-----RESGKAIVITSHSmEECEALCTRLAIMVQGQFK 1593
Cdd:PRK10584 185 IADLlfslnREHGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
528-739 |
2.29e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 57.93 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 528 AGIKIKHLSKVFQVGNKdkmGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ------DM 601
Cdd:PRK11650 2 AGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNElepadrDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 602 AQIRKSLGLCPqHDVLFDNLTvaehlyfYAqLK--GLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIAL 679
Cdd:PRK11650 79 AMVFQNYALYP-HMSVRENMA-------YG-LKirGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAI 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 680 IAGSKVLMLDEPTSGMDA---VSRRaiwdlLQQQKSDR----TVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11650 150 VREPAVFLFDEPLSNLDAklrVQMR-----LEIQRLHRrlktTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1385-1546 |
2.34e-08 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 56.42 E-value: 2.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1385 ELSKVY-DQRAPLLAVDrisLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSIS----SDIGKVRQRMG 1459
Cdd:PRK10908 6 HVSKAYlGGRQALQGVT---FHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRRQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQFDALLDHMTGREMLVMYARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
....*..
gi 569000489 1540 EPSTGMD 1546
Cdd:PRK10908 163 EPTGNLD 169
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1397-1614 |
3.35e-08 |
|
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: 56.34 E-value: 3.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQFDALL------- 1468
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFnrsirdn 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 ----DHMTGREMLVMYARLRGIPErLINACVE--NTL---RGLLLephanklvktySGGNKRKLSTGIALIGEPAVIFLD 1539
Cdd:cd03252 96 ialaDPGMSMERVIEAAKLAGAHD-FISELPEgyDTIvgeQGAGL-----------SGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1540 EPSTGMDPVARRLLWDTVaRARESGKAIVITSHSMEECEAlCTRLAIMVQGQFKCLGSPQHLKSKFGSGYSLQAK 1614
Cdd:cd03252 164 EATSALDYESEHAIMRNM-HDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
531-742 |
3.78e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 58.02 E-value: 3.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 531 KIKHLSkVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP-PTSGHAYIHGYE---------ISQD 600
Cdd:PRK13549 261 EVRNLT-AWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPvkirnpqqaIAQG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 601 MAQI---RKSLGLCPQHDVLfDNLTVAEhlyfYAQLKGLSLQKCPEEVKQMLH-ILSLEDKR---DLRSKFLSGGMKRKL 673
Cdd:PRK13549 340 IAMVpedRKRDGIVPVMGVG-KNITLAA----LDRFTGGSRIDDAAELKTILEsIQRLKVKTaspELAIARLSGGNQQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 674 SIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEADLLGDRIAILAKGELQ 742
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
552-756 |
4.87e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 58.42 E-value: 4.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGyeisqdmaqirkSLGLCPQHdVLFDNLTVAEHLYFYA 631
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQ-AWIQNDSLRENILFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 632 QLKGLSLQKCPEEVKQM--LHILSLEDKRDLRSK--FLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL 707
Cdd:TIGR00957 724 ALNEKYYQQVLEACALLpdLEILPSGDRTEIGEKgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHV 803
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 708 QQQK---SDRTVLLTTH---FMDEADLlgdrIAILAKGELQCCGSSLFLKQKYGA 756
Cdd:TIGR00957 804 IGPEgvlKNKTRILVTHgisYLPQVDV----IIVMSGGKISEMGSYQELLQRDGA 854
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
559-697 |
5.01e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 58.20 E-value: 5.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 559 GQITVLLGHNGAGKTTTMSLLTGlfpptsghaYIHGYEISQD-------------MAQIRKSLGLCPQHDVLFDNLTVAE 625
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIAS---------NTDGFHIGVEgvitydgitpeeiKKHYRGDVVYNAETDVHFPHLTVGE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLSLQKC----PEEVKQMLH----ILSLEDKRDLRS-----KFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:TIGR00956 158 TLDFAARCKTPQNRPDgvsrEEYAKHIADvymaTYGLSHTRNTKVgndfvRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
....*
gi 569000489 693 SGMDA 697
Cdd:TIGR00956 238 RGLDS 242
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1379-1590 |
5.43e-08 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 57.37 E-value: 5.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1379 TPLIinELSKVYDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRM 1458
Cdd:PRK15439 9 PPLL--CARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1459 G-Y-CPQFDALLDHMTGRE-MLVMYARLRGIPERLinacvENTLRGL--LLEPHAN---------KLVKTYSGgnkrkls 1524
Cdd:PRK15439 87 GiYlVPQEPLLFPNLSVKEnILFGLPKRQASMQKM-----KQLLAALgcQLDLDSSagslevadrQIVEILRG------- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1525 tgiaLIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:PRK15439 155 ----LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1376-1572 |
5.69e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.96 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDtplIINELSKVYDQraPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVR 1455
Cdd:PRK13540 1 MLD---VIELDFDYHDQ--PLL--QQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1456 QRMGYCPQFDALLDHMTGREMLvmyarLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAV 1535
Cdd:PRK13540 74 KQLCFVGHRSGINPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKL 148
|
170 180 190
....*....|....*....|....*....|....*..
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSH 1572
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1402-1601 |
5.76e-08 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 56.15 E-value: 5.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGK-VRQRMGYCPQFDALLDHMTGREMLV-- 1478
Cdd:PRK10253 26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDITVQELVArg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1479 ------MYARLRGIPERLINAcvenTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRL 1552
Cdd:PRK10253 106 ryphqpLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 1553 LWDTVARA-RESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSPQHL 1601
Cdd:PRK10253 182 LLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
551-740 |
5.92e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFP--PTSGHAYIHGYEISqdMAQIR----KSLGLCPQHDVLFDNLTVA 624
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQ--ASNIRdterAGIAIIHQELALVKELSVL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 625 EHLYFYAQL-KG--LSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRR 701
Cdd:PRK13549 101 ENIFLGNEItPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 702 AIWDLLQQQKS-DRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK13549 181 VLLDIIRDLKAhGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
544-721 |
6.73e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 6.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 544 KDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQD--MAQIRKSLGLCPQHDVLFDNL 621
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDinLKWWRSKIGVVSQDPLLFSNS 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 ---TVAEHLYFYAQLKGLSLQ--------------------KCPEEVKQMLH---------------------------- 650
Cdd:PTZ00265 476 iknNIKYSLYSLKDLEALSNYynedgndsqenknkrnscraKCAGDLNDMSNttdsneliemrknyqtikdsevvdvskk 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 651 ------ILSLEDKRDL----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQK--SDRTVLL 718
Cdd:PTZ00265 556 vlihdfVSALPDKYETlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITII 635
|
...
gi 569000489 719 TTH 721
Cdd:PTZ00265 636 IAH 638
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
559-742 |
7.09e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.83 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 559 GQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIhgyeisqdmaqIRKSLGLCPQHDVLFdNLTVAEHLYFYAQLKGLSL 638
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIF-NATVRDNILFGSPFDPERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 639 QKCPEeVKQMLHILSLEDKRDL-----RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDA-VSRRAIWDLLQQQKS 712
Cdd:PLN03130 711 ERAID-VTALQHDLDLLPGGDLteigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAhVGRQVFDKCIKDELR 789
|
170 180 190
....*....|....*....|....*....|...
gi 569000489 713 DRTVLLTT---HFMDEAdllgDRIAILAKGELQ 742
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMIK 818
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1398-1591 |
7.21e-08 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 57.25 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG--------EETITSGDAFVgGYSIS----SDIGKVRQRMgycpqfd 1465
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyeGEIIFEGEELQ-ASNIRdterAGIAIIHQEL------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1466 ALLDHMT-------GREML--------VMYARlrgiperlinacVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALI 1530
Cdd:PRK13549 92 ALVKELSvleniflGNEITpggimdydAMYLR------------AQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1531 GEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
549-727 |
7.41e-08 |
|
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: 55.03 E-value: 7.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQI-----RKSLGLCPQHDVLFdNLTV 623
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLL-NATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 624 AEHLYF---------YAQLKGLSLQkcPEevkqmLHILSLEDKRDL--RSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:cd03290 96 EENITFgspfnkqryKAVTDACSLQ--PD-----IDLLPFGDQTEIgeRGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000489 693 SGMDA-----VSRRAIWDLLQQQKsdRTVLLTTH---FMDEAD 727
Cdd:cd03290 169 SALDIhlsdhLMQEGILKFLQDDK--RTLVLVTHklqYLPHAD 209
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
561-739 |
9.78e-08 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 56.04 E-value: 9.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 561 ITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQI-----RKSLGLCPQHDVLFDNLTVAEHLYFyaqlkG 635
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQDARLFPHYKVRGNLRY-----G 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 636 LSlQKCPEEVKQMLHILSLEDkrdLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--Q 710
Cdd:PRK11144 101 MA-KSMVAQFDKIVALLGIEP---LLDRYpgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERlaR 176
|
170 180
....*....|....*....|....*....
gi 569000489 711 KSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK11144 177 EINIPILYVSHSLDEILRLADRVVVLEQG 205
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1390-1611 |
1.10e-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: 54.85 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1390 YDQRAPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQFDALL 1468
Cdd:cd03249 10 YPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1469 DhMTGREMLVmYARLRGIPERLINACVE--------------NTLRGlllePHANKLvktySGGNKRKLSTGIALIGEPA 1534
Cdd:cd03249 90 D-GTIAENIR-YGKPDATDEEVEEAAKKanihdfimslpdgyDTLVG----ERGSQL----SGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARESGKAIVItSHSmeeceaLCT-----RLAIMVQGQFKCLGSPQHLKSKFGSGY 1609
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVI-AHR------LSTirnadLIAVLQNGQVVEQGTHDELMAQKGVYA 232
|
..
gi 569000489 1610 SL 1611
Cdd:cd03249 233 KL 234
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
550-721 |
1.51e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 56.58 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 550 RDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQDMAQIRKSLGLCPQH--------------- 614
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQGDEEQNvgmknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 615 -------------DVLFDNLTVAEH--------------------LYFYAQLKGLSLQKCPEEVKQMLH-------ILSL 654
Cdd:PTZ00265 1265 gsgedstvfknsgKILLDGVDICDYnlkdlrnlfsivsqepmlfnMSIYENIKFGKEDATREDVKRACKfaaidefIESL 1344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 655 EDKRDLR----SKFLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTH 721
Cdd:PTZ00265 1345 PNKYDTNvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVdiKDKADKTIITIAH 1417
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
548-740 |
1.61e-07 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 55.39 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 548 GIRDLTLNLyEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAY-----------------IHGY--------------- 595
Cdd:COG3593 13 SIKDLSIEL-SDDLTVLVGENNSGKSSILEALRLLLGPSSSRKFdeedfylgddpdlpeieIELTfgsllsrllrlllke 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 596 ----EISQDMAQIRKSLglcpqhDVLFDNLT--VAEHLYFYAQLKGLSLQKCPEEVKQMLHILSL--EDKRDLRSKFLSG 667
Cdd:COG3593 92 edkeELEEALEELNEEL------KEALKALNelLSEYLKELLDGLDLELELSLDELEDLLKSLSLriEDGKELPLDRLGS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 668 GMKRKLSIGIALI-------AGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRT-VLLTTH---FMDEADLlgDRIAIL 736
Cdd:COG3593 166 GFQRLILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNqVIITTHsphLLSEVPL--ENIRRL 243
|
....
gi 569000489 737 AKGE 740
Cdd:COG3593 244 RRDS 247
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1398-1572 |
2.10e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDigkvrQRMGYCPQFDA------LLDHM 1471
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE-----QPEDYRKLFSAvftdfhLFDQL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1472 TGREmlvmyarlrGIPERliNACVENTLRGL----LLEPHANKLVKT-YSGGNKRKLSTGIALIGEPAVIFLDEPSTGMD 1546
Cdd:PRK10522 413 LGPE---------GKPAN--PALVEKWLERLkmahKLELEDGRISNLkLSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
170 180
....*....|....*....|....*..
gi 569000489 1547 PVARRLLW-DTVARARESGKAIVITSH 1572
Cdd:PRK10522 482 PHFRREFYqVLLPLLQEMGKTIFAISH 508
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1399-1619 |
2.31e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 54.33 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG-EETIT----SGDAFVGGYSISS--DIGKVRQRMGYC-----PQFDA 1466
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVSgyrySGDVLLGGRSIFNyrDVLEFRRRVGMLfqrpnPFPMS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 LLDHMTG---REMLVMYARLRGIPE-RLINACVENTLRGLLLEPHANklvktYSGGNKRKLSTGIALIGEPAVIFLDEPS 1542
Cdd:PRK14271 117 IMDNVLAgvrAHKLVPRKEFRGVAQaRLTEVGLWDAVKDRLSDSPFR-----LSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1543 TGMDPVARRLLWDTVaRARESGKAIVITSHSMEECEALCTRLAIMVQGQF-------KCLGSPQHLKS-KFGSGYSLQAK 1614
Cdd:PRK14271 192 SALDPTTTEKIEEFI-RSLADRLTVIIVTHNLAQAARISDRAALFFDGRLveegpteQLFSSPKHAETaRYVAGLSGDVK 270
|
....*
gi 569000489 1615 VRSEG 1619
Cdd:PRK14271 271 DAKRG 275
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1377-1613 |
3.00e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1377 LDTPLIINELSKVYDQRAPLL------AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFV-------G 1443
Cdd:PRK15112 1 VETLLEVRNLSKTFRYRTGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIddhplhfG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1444 GYSISSDIGKV-----------RQRMGYCPQFDALLD-HMTGREMlvmyarlrgipERLINAcvenTLRGL-LLEPHANK 1510
Cdd:PRK15112 81 DYSYRSQRIRMifqdpstslnpRQRISQILDFPLRLNtDLEPEQR-----------EKQIIE----TLRQVgLLPDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1511 LVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARES-GKAIVITSHSMEECEALCTRLAIMVQ 1589
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQ 225
|
250 260 270
....*....|....*....|....*....|....*..
gi 569000489 1590 GQF-------KCLGSPQH------LKSKFGSGYSLQA 1613
Cdd:PRK15112 226 GEVvergstaDVLASPLHeltkrlIAGHFGEALTADA 262
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1383-1576 |
3.14e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 53.50 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRApllAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLT------GEETITSGDAFVGG--YSISSDIGKV 1454
Cdd:PRK14258 10 VNNLSFYYDTQK---ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQniYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYC-PQFDalLDHMTGREMLVMYARLRGI-PERLINACVENTLRGL-LLEPHANKLVKT---YSGGNKRKLSTGIA 1528
Cdd:PRK14258 87 RRQVSMVhPKPN--LFPMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDAdLWDEIKHKIHKSaldLSGGQQQRLCIARA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 1529 LIGEPAVIFLDEPSTGMDPVARRLLWDTVARAR-ESGKAIVITSHSMEE 1576
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQ 213
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
552-785 |
3.69e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 55.37 E-value: 3.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVLFDNlTVAEHLYFY 630
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRFNIDPF 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 631 AQLKGLSLQKCpeevkqmLHILSLEDKRDlRSKF------------LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAV 698
Cdd:PLN03232 1334 SEHNDADLWEA-------LERAHIKDVID-RNPFgldaevseggenFSVGQRQLLSLARALLRRSKILVLDEATASVDVR 1405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 699 SRRAIWDLLQQQKSDRTVLLTTHFMDEAdLLGDRIAILAKGE-LQCCGSSLFLKQKYGAGYHMTLVKEPHcNPEGISQLV 777
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQvLEYDSPQELLSRDTSAFFRMVHSTGPA-NAQYLSNLV 1483
|
....*...
gi 569000489 778 HHHVPNAM 785
Cdd:PLN03232 1484 FERRENGM 1491
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
539-741 |
4.09e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 539 FQVGNKDKMGIRDLTLNlyEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIH-------GYEISQDMA----QIRKS 607
Cdd:PRK10938 11 FRLSDTKTLQLPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshitrlSFEQLQKLVsdewQRNNT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 608 LGLCPQHDvlfD-NLTVAEHLyfyaQLKGLSLQKCpEEVKQMLHILSLEDKRdlrSKFLSGGMKRKLSIGIALIAGSKVL 686
Cdd:PRK10938 89 DMLSPGED---DtGRTTAEII----QDEVKDPARC-EQLAQQFGITALLDRR---FKYLSTGETRKTLLCQALMSEPDLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTHFMDEADLLgDRIAILAKGEL 741
Cdd:PRK10938 158 ILDEPFDGLDVASRQQLAELLASlhQSGITLVLVLNRFDEIPDFV-QFAGVLADCTL 213
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1381-1611 |
5.14e-07 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 54.45 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 LIINELSKVYDQRaPLLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMG 1459
Cdd:PRK11160 339 LTLNNVSFTYPDQ-PQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADySEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1460 YCPQ----FDALLdhmtgREMLVMyARLRGIPERLINACVENTLRGLLLEPHANKLV-----KTYSGGNKRKLSTGIALI 1530
Cdd:PRK11160 418 VVSQrvhlFSATL-----RDNLLL-AAPNASDEALIEVLQQVGLEKLLEDDKGLNAWlgeggRQLSGGEQRRLGIARALL 491
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1531 GEPAVIFLDEPSTGMDPVA-RRLLwdTVARARESGKAIVITSH---SMEECEALCtrlaIMVQGQFKCLGSPQHLKSKFG 1606
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETeRQIL--ELLAEHAQNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQELLAQQG 565
|
....*
gi 569000489 1607 SGYSL 1611
Cdd:PRK11160 566 RYYQL 570
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
551-690 |
5.17e-07 |
|
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: 54.42 E-value: 5.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNlyEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS-QDMAQIRkslglcpQH------DV-LFDnlt 622
Cdd:COG4615 352 DLTIR--RGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYR-------QLfsavfsDFhLFD--- 419
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 623 vaeHLYfyaqlkGLSLQKCPEEVKQMLHILSLEDKRDLRS-KF----LSGGMKRKLSIGIALIAGSKVLMLDE 690
Cdd:COG4615 420 ---RLL------GLDGEADPARARELLERLELDHKVSVEDgRFsttdLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
549-721 |
5.51e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 54.43 E-value: 5.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHayihgyeisqdmaqirksLGLCPQHDVLFdnltVAEHLY 628
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGR------------------IARPAGARVLF----LPQRPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 F----------YAQLkglSLQKCPEEVKQMLHILSLE------DKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:COG4178 437 LplgtlreallYPAT---AEAFSDAELREALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180
....*....|....*....|....*....
gi 569000489 693 SGMDAVSRRAIWDLLQQQKSDRTVLLTTH 721
Cdd:COG4178 514 SALDEENEAALYQLLREELPGTTVISVGH 542
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1402-1591 |
5.97e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 52.09 E-value: 5.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGysissdigkvrqRMGYCPQFdALLDHMTGREMLVMYA 1481
Cdd:cd03250 24 INLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SIAYVSQE-PWIQNGTIRENILFGK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1482 RLRgiPERL---INACventlrglLLEPHANKLVK-----------TYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDP 1547
Cdd:cd03250 91 PFD--EERYekvIKAC--------ALEPDLEILPDgdlteigekgiNLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 569000489 1548 -VARRLLWDTVARARESGKAIVITSHSMEECEAlCTRLAIMVQGQ 1591
Cdd:cd03250 161 hVGRHIFENCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1386-1572 |
7.82e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 53.97 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1386 LSKVYDQRaplLAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGdafvggysiSSDIGKVRQrMGYCPQF- 1464
Cdd:PRK11819 330 LSKSFGDR---LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG---------TIKIGETVK-LAYVDQSr 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DAL-------------LDHMT--GREMlvmyarlrgiPERlinACVE--NtLRGlllePHANKLVKTYSGGNKRKLSTGI 1527
Cdd:PRK11819 397 DALdpnktvweeisggLDIIKvgNREI----------PSR---AYVGrfN-FKG----GDQQKKVGVLSGGERNRLHLAK 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 569000489 1528 ALIGEPAVIFLDEPSTGMDpVarrllwDTVaRARES------GKAIVItSH 1572
Cdd:PRK11819 459 TLKQGGNVLLLDEPTNDLD-V------ETL-RALEEallefpGCAVVI-SH 500
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
549-721 |
8.86e-07 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 50.62 E-value: 8.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHayihgyeisqdmaqirksLGLCPQHDVLFdnltVAEHLY 628
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR------------------IGMPEGEDLLF----LPQRPY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 629 FYAqlkgLSLqkcpeevKQMLhILSLEDKrdlrskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ 708
Cdd:cd03223 75 LPL----GTL-------REQL-IYPWDDV-------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLK 135
|
170
....*....|...
gi 569000489 709 QQKSdrTVLLTTH 721
Cdd:cd03223 136 ELGI--TVISVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-43 |
9.69e-07 |
|
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: 54.25 E-value: 9.69e-07
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 569000489 1 MAVLRQLTLLLWKNYTLKKRKVLVTVLELFLPLLFSGILIWLR 43
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLR 43
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
551-740 |
1.14e-06 |
|
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: 53.15 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTT-MSLLtGLFPpTSGHAYIHGYEISQ----DMAQIRKSL---------GLCPQHDV 616
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTLgLALL-RLIP-SEGEIRFDGQDLDGlsrrALRPLRRRMqvvfqdpfgSLSPRMTV 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 617 LfdnLTVAEHLYFYAqlKGLSLQKCPEEVKQMLHILSLEdkRDLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:COG4172 382 G---QIIAEGLRVHG--PGLSAAERRARVAEALEEVGLD--PAARHRYpheFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 694 GMDaVSRRA-IWDLLQ--QQKSDRTVLLTTHfmdeaDL-----LGDRIAILAKGE 740
Cdd:COG4172 455 ALD-VSVQAqILDLLRdlQREHGLAYLFISH-----DLavvraLAHRVMVMKDGK 503
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1399-1576 |
1.19e-06 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 51.25 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGEcFGLL-GFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQFDALLDHmTGREM 1476
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 LVMYARLRGI-PERliNACVENTLRGLLLEPHANKLVKTYSGGNKRKlstgIALIGE----PAVIFLDEPSTGMDPVARR 1551
Cdd:PRK10247 101 LIFPWQIRNQqPDP--AIFLDDLERFALPDTILTKNIAELSGGEKQR----ISLIRNlqfmPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
gi 569000489 1552 LLWDTVAR-ARESGKAIVITSHSMEE 1576
Cdd:PRK10247 175 NVNEIIHRyVREQNIAVLWVTHDKDE 200
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
532-739 |
1.30e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.17 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKT-TTMSLLTGL-FPP---TSGHAYIHGYEI----SQDMA 602
Cdd:PRK15134 8 IENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 603 QIRKS----------LGLCPQHdvlfdnlTVAEHLYFYAQL-KGLSLQKCPEEVKQMLHILSLEDKRDLRSKF---LSGG 668
Cdd:PRK15134 88 GVRGNkiamifqepmVSLNPLH-------TLEKQLYEVLSLhRGMRREAARGEILNCLDRVGIRQAAKRLTDYphqLSGG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 669 MKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1406-1584 |
1.35e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.00 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1406 VQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSdiGKVRQRMGYCPQFDALLDHMTGREMLVMYARLRG 1485
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR--GDRSRFMAYLGHLPGLKADLSTLENLHFLCGLHG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1486 I-PERLINacveNTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESG 1564
Cdd:PRK13543 112 RrAKQMPG----SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 569000489 1565 KAIVITSHSMEECEALCTRL 1584
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
522-711 |
1.52e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 1.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 522 EPEDLVAGIKIKHLSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-- 599
Cdd:PRK15079 10 EVADLKVHFDIKDGKQWFWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmk 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 600 --DMAQIRKSLGLCPQHDV--LFDNLTV----AEHLY-FYAQlkgLSLQKCPEEVKQMLhilsleDKRDLRSKFL----- 665
Cdd:PRK15079 90 ddEWRAVRSDIQMIFQDPLasLNPRMTIgeiiAEPLRtYHPK---LSRQEVKDRVKAMM------LKVGLLPNLInryph 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 666 --SGGMKRKLSIGIALIAGSKVLMLDEPTSGMDaVSRRA-IWDLLQQ-QK 711
Cdd:PRK15079 161 efSGGQCQRIGIARALILEPKLIICDEPVSALD-VSIQAqVVNLLQQlQR 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
647-740 |
1.53e-06 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.11 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 647 QMLHILSLEDKRDLRSKF---LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ--QKSDRTVLLTTH 721
Cdd:PRK15093 138 ELLHRVGIKDHKDAMRSFpyeLTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISH 217
|
90
....*....|....*....
gi 569000489 722 FMDEADLLGDRIAILAKGE 740
Cdd:PRK15093 218 DLQMLSQWADKINVLYCGQ 236
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1398-1600 |
1.53e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSI----SSDIGKVRQRMGYCPQfD--ALLD-- 1469
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQ-DpyASLDpr 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1470 HMTG---REMLVMYARLRGIPERlinACVENTLRGLLLEP-HANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:PRK10261 418 QTVGdsiMEPLRVHGLLPGKAAA---ARVAWLLERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1546 DPVAR----RLLWDTvarARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLG-------SPQH 1600
Cdd:PRK10261 495 DVSIRgqiiNLLLDL---QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGprravfeNPQH 557
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
549-746 |
2.34e-06 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 50.98 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPptsGHAYIHGYEISQD---------------MAQIRKSLGLCPQ 613
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDvtlngeplaaidaprLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 614 HDVLF--DNLtVAEHLYFYAQLKGLSLQKCPEEVKQMLHILSLE--DKRDLRSkfLSGGMKRKLSIGIAL---------I 680
Cdd:PRK13547 94 PAFAFsaREI-VLLGRYPHARRAGALTHRDGEIAWQALALAGATalVGRDVTT--LSGGELARVQFARVLaqlwpphdaA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 681 AGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRT--VLLTTHFMDEADLLGDRIAILAKGELQCCGS 746
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNlgVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
530-741 |
2.39e-06 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 50.94 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVF--QVG---NKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEI------- 597
Cdd:PRK15112 5 LEVRNLSKTFryRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLhfgdysy 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 598 -SQDMAQIRK--SLGLCPQHdvlfdnlTVAEHLYFYAQLK-GLSLQKCPEEVKQMLHILSL-EDKRDLRSKFLSGGMKRK 672
Cdd:PRK15112 85 rSQRIRMIFQdpSTSLNPRQ-------RISQILDFPLRLNtDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 673 LSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDL---LQQQKSDRTVLLTTHF--MDEadlLGDRIAILAKGEL 741
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLmleLQEKQGISYIYVTQHLgmMKH---ISDQVLVMHQGEV 228
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
561-727 |
2.71e-06 |
|
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: 49.91 E-value: 2.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 561 ITVLLGHNGAGKTTTMSL----LTGLFPPTS--GH------------AYI---------HGYEISQDMAQIRKSLgLCPQ 613
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNSkgGAhdpkliregevrAQVklafenangKKYTITRSLAILENVI-FCHQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 614 hdvlfdnltvaehlyfyaqlkglslqkcpEEVKQMLhilslEDKRDlrskFLSGGMKRKLSIGIAL-IA---GSK--VLM 687
Cdd:cd03240 103 -----------------------------GESNWPL-----LDMRG----RCSGGEKVLASLIIRLaLAetfGSNcgILA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 688 LDEPTSGMDAVSRR-AIWDLL--QQQKSDRTVLLTTH---FMDEAD 727
Cdd:cd03240 145 LDEPTTNLDEENIEeSLAEIIeeRKSQKNFQLIVITHdeeLVDAAD 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
532-696 |
2.94e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 51.82 E-value: 2.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 532 IKHLSKVFQvgnkDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyEIS-QDMAQIrkslGL 610
Cdd:PRK15064 322 VENLTKGFD----NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG-------TVKwSENANI----GY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 611 CPQ-HDVLFDN-LTVAEHLYFYAQLKGLSLQkcpeeVKQML-HILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLM 687
Cdd:PRK15064 387 YAQdHAYDFENdLTLFDWMSQWRQEGDDEQA-----VRGTLgRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
....*....
gi 569000489 688 LDEPTSGMD 696
Cdd:PRK15064 462 MDEPTNHMD 470
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
554-696 |
3.23e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 3.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 554 LNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHayihgYEISQDMAQIRksLGLCPQHDV---LFDNLT-----VAE 625
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-----IIYEQDLIVAR--LQQDPPRNVegtVYDFVAegieeQAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 626 HLYFYAQLKGLSLQKCPEE-----------------------VKQMLHILSLEDKRDLRSkfLSGGMKRKLSIGIALIAG 682
Cdd:PRK11147 97 YLKRYHDISHLVETDPSEKnlnelaklqeqldhhnlwqlenrINEVLAQLGLDPDAALSS--LSGGWLRKAALGRALVSN 174
|
170
....*....|....
gi 569000489 683 SKVLMLDEPTSGMD 696
Cdd:PRK11147 175 PDVLLLDEPTNHLD 188
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1400-1572 |
3.90e-06 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 49.42 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1400 DRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKVRQRMGYCPQFDALLDHMTGREMLVM 1479
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1480 YARLRGIP--ERLINAcventLRGLLLEPHANKLVKTYSGGNKRKlstgIAL----IGEPAVIFLDEPSTGMDPVARRLL 1553
Cdd:PRK13538 98 YQRLHGPGddEALWEA-----LAQVGLAGFEDVPVRQLSAGQQRR----VALarlwLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*....
gi 569000489 1554 WDTVARARESGKAIVITSH 1572
Cdd:PRK13538 169 EALLAQHAEQGGMVILTTH 187
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
552-746 |
5.37e-06 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 49.55 E-value: 5.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 552 LTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFpPTSGHAYIHGYEISQ----DMAQIRKSlgLCPQHDVLFdNLTVAEHL 627
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAY--LSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 628 YFYaQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRK-------LSIGIALIAGSKVLMLDEPTSGMDaVSR 700
Cdd:PRK03695 91 TLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMNSLD-VAQ 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 569000489 701 RAIWDLLQQQ--KSDRTVLLTTHfmdeaDL-----LGDRIAILAKGELQCCGS 746
Cdd:PRK03695 169 QAALDRLLSElcQQGIAVVMSSH-----DLnhtlrHADRVWLLKQGKLLASGR 216
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1516-1591 |
5.59e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.88 E-value: 5.59e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1516 SGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQ 1591
Cdd:PRK10982 393 SGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1394-1590 |
5.64e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 49.70 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1394 APLLAVDRISLAVQKGECFGLLGFNGAGKTTT----FKMLTGEETITSGDAFVGGYSISSD------IGKVRQ--RMGYC 1461
Cdd:PRK10418 14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgrkIATIMQnpRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1462 PqFDALLDHmtGREMLvmyaRLRGIP--ERLINACVENTlrGLllePHANKLVKTY----SGGNKRKLSTGIALIGEPAV 1535
Cdd:PRK10418 94 P-LHTMHTH--ARETC----LALGKPadDATLTAALEAV--GL---ENAARVLKLYpfemSGGMLQRMMIALALLCEAPF 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1536 IFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQG 1590
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHG 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
542-707 |
6.86e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 6.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 542 GNKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyEISqdMAQIRKsLGLCPQHDVLF--D 619
Cdd:PRK10636 321 GYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIG--LAKGIK-LGYFAQHQLEFlrA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 620 NLTVAEHLYFYAqlkglslqkcPEEVKQMLhilsledkRDLRSKF-------------LSGGMKRKLSIGIALIAGSKVL 686
Cdd:PRK10636 391 DESPLQHLARLA----------PQELEQKL--------RDYLGGFgfqgdkvteetrrFSGGEKARLVLALIVWQRPNLL 452
|
170 180
....*....|....*....|.
gi 569000489 687 MLDEPTSGMDAVSRRAIWDLL 707
Cdd:PRK10636 453 LLDEPTNHLDLDMRQALTEAL 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
530-696 |
7.05e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.89 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFqvgnKDKMGIRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyEI----SQDMAQIR 605
Cdd:PRK11819 325 IEAENLSKSF----GDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSG-------TIkigeTVKLAYVD 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 606 KSlglcpqHDVLFDNLTVAehlyfyaqlkglslqkcpEEVKQMLHILSLEDK----RDLRSKF-------------LSGG 668
Cdd:PRK11819 394 QS------RDALDPNKTVW------------------EEISGGLDIIKVGNReipsRAYVGRFnfkggdqqkkvgvLSGG 449
|
170 180
....*....|....*....|....*...
gi 569000489 669 MKRKLSIGIALIAGSKVLMLDEPTSGMD 696
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
558-736 |
7.54e-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: 50.55 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 558 EGQITVLLGHNGAGKTTTMSLLTGLFPPTSGH-----------AYIHGYEIS---QDMAQIRKSLGLCPQH-DVL---FD 619
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDydeepswdevlKRFRGTELQdyfKKLANGEIKVAHKPQYvDLIpkvFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 620 NlTVAEHLYFYAQLKGLslqkcpEEVKQMLHILSLEDkRDLRSkfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:COG1245 178 G-TVRELLEKVDERGKL------DELAEKLGLENILD-RDISE--LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQ 247
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 569000489 700 R----RAIWDLLqqqKSDRTVLLTTHfmDEA--DLLGDRIAIL 736
Cdd:COG1245 248 RlnvaRLIRELA---EEGKYVLVVEH--DLAilDYLADYVHIL 285
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
558-736 |
1.11e-05 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 48.90 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 558 EGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHayiHGYEisqdmaqirkslglcPQHDVLFDNLTVAE-HLYFYAQLKG- 635
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGK---FDDP---------------PDWDEILDEFRGSElQNYFTKLLEGd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 636 LSLQKCPEEVKQML-----HILSLEDKRDLRSKF-------------------LSGGMKRKLSIGIALIAGSKVLMLDEP 691
Cdd:cd03236 87 VKVIVKPQYVDLIPkavkgKVGELLKKKDERGKLdelvdqlelrhvldrnidqLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 692 TSGMDAVSR----RAIWDLLQQqksDRTVLLTTHFMDEADLLGDRIAIL 736
Cdd:cd03236 167 SSYLDIKQRlnaaRLIRELAED---DNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
551-740 |
1.30e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEIS---------QDMAQIRKSLGLCPQHDVLfDNL 621
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfksskealeNGISMVHQELNLVLQRSVM-DNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 622 TVAEHlyfyaQLKGLSL--QKCPEEVKQMLHILSLE-DKRDLRSKfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAV 698
Cdd:PRK10982 95 WLGRY-----PTKGMFVdqDKMYRDTKAIFDELDIDiDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569000489 699 SRRAIWDLLQQQKsDR--TVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK10982 169 EVNHLFTIIRKLK-ERgcGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1332-1572 |
1.75e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.40 E-value: 1.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1332 LRTFICAFRRRWTLA-ELQNRTSVLpedqdvaeERSRILVPSL------------DSMLDTPLIINELSKVYDQRaplLA 1398
Cdd:PRK10636 259 LQSYIDRFRAKATKAkQAQSRIKML--------ERMELIAPAHvdnpfhfsfrapESLPNPLLKMEKVSAGYGDR---II 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAfvggySISSDIgkvrqRMGYCPQF--------DALLDH 1470
Cdd:PRK10636 328 LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGI-----KLGYFAQHqleflradESPLQH 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1471 MTgremlvmyarlrgipeRLINACVENTLRGLL--LEPHANKLVKT---YSGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:PRK10636 398 LA----------------RLAPQELEQKLRDYLggFGFQGDKVTEEtrrFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
250 260
....*....|....*....|....*..
gi 569000489 1546 DPVARRLLwdTVARARESGkAIVITSH 1572
Cdd:PRK10636 462 DLDMRQAL--TEALIDFEG-ALVVVSH 485
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1399-1592 |
3.46e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 3.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTtFKM-LTGEE--TITSGDAFVGGYSIssDIGKVRQ------------RMGYcpq 1463
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTE-LAMsVFGRSygRNISGTVFKDGKEV--DVSTVSDaidaglayvtedRKGY--- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1464 fdALLDHMTGREMLVMyARLRGIPER-LINACVE--------NTLRglLLEPHANKLVKTYSGGNKRKLSTGIALIGEPA 1534
Cdd:NF040905 350 --GLNLIDDIKRNITL-ANLGKVSRRgVIDENEEikvaeeyrKKMN--IKTPSVFQKVGNLSGGNQQKVVLSKWLFTDPD 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1535 VIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSMEECEALCTRLAIMVQGQF 1592
Cdd:NF040905 425 VLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
558-736 |
3.87e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.27 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 558 EGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHA-----------YIHGYEIS---QDMAQIRKSLGLCPQH-DVL---FD 619
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELQnyfKKLYNGEIKVVHKPQYvDLIpkvFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 620 NlTVAEhlyfyaQLKGLSLQKCPEEVKQMLHILSLEDkRDLRSkfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVS 699
Cdd:PRK13409 178 G-KVRE------LLKKVDERGKLDEVVERLGLENILD-RDISE--LSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQ 247
|
170 180 190
....*....|....*....|....*....|....*....
gi 569000489 700 RRAIWDLLQQQKSDRTVLLTTHfmDEA--DLLGDRIAIL 736
Cdd:PRK13409 248 RLNVARLIRELAEGKYVLVVEH--DLAvlDYLADNVHIA 284
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1398-1574 |
5.03e-05 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 46.95 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTT---TF-KMLtgeETI----TSGDAFVGG---YSISSDIGKVRQRMGYCPQ--- 1463
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTllrCLnRMN---DLIpgarVEGEILLDGediYDPDVDVVELRRRVGMVFQkpn 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1464 -FdalldHMTGREMLVMYARLRGI-PERLINACVENTLRGLLL---------EPhANKLvktySGGNKRKLStgIA--LI 1530
Cdd:COG1117 103 pF-----PKSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevkdrlkKS-ALGL----SGGQQQRLC--IAraLA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 569000489 1531 GEPAVIFLDEPSTGMDPVARRLLWDTVARARESgKAIVITSHSM 1574
Cdd:COG1117 171 VEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNM 213
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1516-1575 |
5.23e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 47.38 E-value: 5.23e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 1516 SGGNKRKLSTGIALI---GEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVITSHSME 1575
Cdd:pfam13304 238 SDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
549-740 |
6.12e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTT-MSLLTGLfpPTSGHAYIHGYEISQ----DMAQIRKSL---------GLCPQH 614
Cdd:PRK15134 302 VKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNlnrrQLLPVRHRIqvvfqdpnsSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 615 DVLfdnLTVAEHLYFYAqlKGLSLQKCPEEVKQMLHILSLEDKRDLR--SKFlSGGMKRKLSIGIALIAGSKVLMLDEPT 692
Cdd:PRK15134 380 NVL---QIIEEGLRVHQ--PTLSAAQREQQVIAVMEEVGLDPETRHRypAEF-SGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 569000489 693 SGMDAVSRRAIWDLLQ--QQKSDRTVLLTTHFMDEADLLGDRIAILAKGE 740
Cdd:PRK15134 454 SSLDKTVQAQILALLKslQQKHQLAYLFISHDLHVVRALCHQVIVLRQGE 503
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
665-722 |
6.22e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 45.04 E-value: 6.22e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 569000489 665 LSGGMKRKLSI----GIALIAGSKVLMLDEPTSGMDAVSRRAI-WDLLQQQKSDRTVLLTTHF 722
Cdd:cd03227 78 LSGGEKELSALalilALASLKPRPLYILDEIDRGLDPRDGQALaEAILEHLVKGAQVIVITHL 140
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1398-1591 |
6.70e-05 |
|
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: 47.79 E-value: 6.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1398 AVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS-DIGKVRQRMGYCPQFDALLDHMTGREm 1476
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDVVLFNDTIANN- 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1477 lVMYARLRGIPErlinACVENTLRGLLLEPHANKLVKTY-----------SGGNKRKLSTGIALIGEPAVIFLDEPSTGM 1545
Cdd:TIGR02203 426 -IAYGRTEQADR----AEIERALAAAYAQDFVDKLPLGLdtpigengvllSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 569000489 1546 DPVARRLLWDTVARARESGKAIVItSHSMEECEAlCTRLAIMVQGQ 1591
Cdd:TIGR02203 501 DNESERLVQAALERLMQGRTTLVI-AHRLSTIEK-ADRIVVMDDGR 544
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1414-1597 |
7.19e-05 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 47.18 E-value: 7.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1414 LLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISSDIGKV-----RQRMGYCPQfDA-LLDHMTGREMLvMYARLRGIP 1487
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ-DArLFPHYKVRGNL-RYGMAKSMV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1488 ERLinacveNTLRGLL-LEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMD-PVARRLLWDTVARARESGK 1565
Cdd:PRK11144 107 AQF------DKIVALLgIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRELLPYLERLAREINI 180
|
170 180 190
....*....|....*....|....*....|..
gi 569000489 1566 AIVITSHSMEECEALCTRLAIMVQGQFKCLGS 1597
Cdd:PRK11144 181 PILYVSHSLDEILRLADRVVVLEQGKVKAFGP 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
497-741 |
7.32e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 47.54 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 497 PR--TVVGKEEEGSDPEKALRNEYFEAEP----EDLVAGIKIKhlSKVFQVGNKDKMGIRDLTLNLYEGQITVLLGHNGA 570
Cdd:PRK10261 284 PRrfPLISLEHPAKQEPPIEQDTVVDGEPilqvRNLVTRFPLR--SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGS 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 571 GKTTTMSLLTGLFPPTSGHAYIHGYEI----SQDMAQIRKSL---------GLCPQHDVLFdnlTVAEHLYFYAQLKGLS 637
Cdd:PRK10261 362 GKSTTGRALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIqfifqdpyaSLDPRQTVGD---SIMEPLRVHGLLPGKA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 638 LQKcpeEVKQMLHILSLEDKRDLRSKF-LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSDRTV 716
Cdd:PRK10261 439 AAA---RVAWLLERVGLLPEHAWRYPHeFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGI 515
|
250 260
....*....|....*....|....*..
gi 569000489 717 --LLTTHFMDEADLLGDRIAILAKGEL 741
Cdd:PRK10261 516 ayLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1400-1572 |
8.51e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 8.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1400 DRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVGGYSISS----DIGKV-RQRMGYCPQFDALLDHMTGR 1474
Cdd:PRK10535 25 KGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLrREHFGFIFQRYHLLSHLTAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1475 ---EMLVMYArlrGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARR 1551
Cdd:PRK10535 105 qnvEVPAVYA---GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|.
gi 569000489 1552 LLWDTVARARESGKAIVITSH 1572
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTH 202
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
665-721 |
9.34e-05 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 46.66 E-value: 9.34e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 665 LSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLL--QQQKSDRTVLLTTH 721
Cdd:PRK11022 154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLleLQQKENMALVLITH 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1315-1606 |
9.64e-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: 47.60 E-value: 9.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1315 GIYLTLLFLIETNLLWRLRTFIcafrrrwTLAELQNRTSV------LPEDQDVAEERSRILVPSLDSMLDTP-------- 1380
Cdd:TIGR01271 1142 GIILTLAMNILSTLQWAVNSSI-------DVDGLMRSVSRvfkfidLPQEEPRPSGGGGKYQLSTVLVIENPhaqkcwps 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1381 ---LIINELSKVY--DQRAPLlavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETiTSGDAFVGGYSISS-DIGKV 1454
Cdd:TIGR01271 1215 ggqMDVQGLTAKYteAGRAVL---QDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTW 1290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1455 RQRMGYCPQfDALLDHMTGREMLVMYARLRGipERLINACVENTLRGlLLEPHANKLV-------KTYSGGNKRKLSTGI 1527
Cdd:TIGR01271 1291 RKAFGVIPQ-KVFIFSGTFRKNLDPYEQWSD--EEIWKVAEEVGLKS-VIEQFPDKLDfvlvdggYVLSNGHKQLMCLAR 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1528 ALIGEPAVIFLDEPSTGMDPVARRLLWDTVARAReSGKAIVITSHSME---ECEALctrlaIMVQG----QF----KCLG 1596
Cdd:TIGR01271 1367 SILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSF-SNCTVILSEHRVEallECQQF-----LVIEGssvkQYdsiqKLLN 1440
|
330
....*....|
gi 569000489 1597 SPQHLKSKFG 1606
Cdd:TIGR01271 1441 ETSLFKQAMS 1450
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1399-1598 |
1.07e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 45.97 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETitsGDAFVGGYSISSDIG------------KVRQRMGYCPQFDA 1466
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDVTlngeplaaidapRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1467 LLDHMTGREMLVM----YARLRGIPERLINACVENTLRGLLLEPHANKLVKTYSGGNKRKLSTGIAL---------IGEP 1533
Cdd:PRK13547 94 PAFAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPP 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 1534 AVIFLDEPSTGMDPVARRLLWDTVAR-ARESGKAIVITSHSMEECEALCTRLAIMVQGQFKCLGSP 1598
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRlARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
539-742 |
1.14e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 47.43 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 539 FQVGNKDKMGIrdltlnlyegqitvlLGHNGAGKTTTMSLLTGLFPPTSGHAYIHGYEISQ-DMAQIRKSLGLCPQHDVL 617
Cdd:PLN03130 1260 FEISPSEKVGI---------------VGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVL 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 618 FDNlTVAEHLYFYAQLKGLSLQKCPE--EVKQML--HILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLMLDEPTS 693
Cdd:PLN03130 1325 FSG-TVRFNLDPFNEHNDADLWESLEraHLKDVIrrNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 569000489 694 GMDAVSRRAIWDLLQQQKSDRTVLLTTHFMDEAdLLGDRIAILAKGELQ 742
Cdd:PLN03130 1404 AVDVRTDALIQKTIREEFKSCTMLIIAHRLNTI-IDCDRILVLDAGRVV 1451
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1397-1547 |
1.35e-04 |
|
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: 45.18 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTT----FKMLtgeeTITSGDAFVGGYSISSdIG--KVRQRMGYCPQfDALLDH 1470
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISK-IGlhDLRSRISIIPQ-DPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1471 MTGREMLVMYARLRgiPERLINA--------CVENTLRGLLLEPHANKlvKTYSGGNKRKLSTGIALIGEPAVIFLDEPS 1542
Cdd:cd03244 92 GTIRSNLDPFGEYS--DEELWQAlervglkeFVESLPGGLDTVVEEGG--ENLSVGQRQLLCLARALLRKSKILVLDEAT 167
|
....*
gi 569000489 1543 TGMDP 1547
Cdd:cd03244 168 ASVDP 172
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
549-740 |
1.47e-04 |
|
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: 45.62 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyeisqdmaQIRKS--LGLCPQHDVLFDNlTVAEH 626
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEG--------------KIKHSgrISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYF---YAQLKGLS-LQKCpeEVKQMLHILSLEDKRDLRSK--FLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR 700
Cdd:cd03291 118 IIFgvsYDEYRYKSvVKAC--QLEEDITKFPEKDNTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 569000489 701 RAIWD-LLQQQKSDRTVLLTTHFMDEADlLGDRIAILAKGE 740
Cdd:cd03291 196 KEIFEsCVCKLMANKTRILVTSKMEHLK-KADKILILHEGS 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1409-1546 |
1.76e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1409 GECFGLLGFNGAGKTTTFKMLTGEetiTSGDAFVGGYSISSD-IGK---VRQRMG---YCPQFDALLDHMTGREMLVMYA 1481
Cdd:TIGR00956 87 GELTVVLGRPGSGCSTLLKTIASN---TDGFHIGVEGVITYDgITPeeiKKHYRGdvvYNAETDVHFPHLTVGETLDFAA 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 569000489 1482 RLRGIPERL--------INACVENTLRGLLLEpH------ANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMD 1546
Cdd:TIGR00956 164 RCKTPQNRPdgvsreeyAKHIADVYMATYGLS-HtrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
551-739 |
1.83e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 551 DLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPptsghayiHG-YE--------------ISQDMAQ----IRKSLGLC 611
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP--------HGsYEgeilfdgevcrfkdIRDSEALgiviIHQELALI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 612 PQhdvlfdnLTVAEHLYF---YAQLKGLSLQKCPEEVKQMLHILSLEDKRDLRSKFLSGGMKRKLSIGIALIAGSKVLML 688
Cdd:NF040905 91 PY-------LSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLIL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 569000489 689 DEPTSGMDAVSRRAIWDLLQQQKS-DRTVLLTTHFMDEADLLGDRIAILAKG 739
Cdd:NF040905 164 DEPTAALNEEDSAALLDLLLELKAqGITSIIISHKLNEIRRVADSITVLRDG 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1397-1576 |
2.03e-04 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 45.16 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1397 LAVDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG-EETITS----GDAFVGGYSISS---DIGKVRQRMGYCPQ----F 1464
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRlNDLIPGfrveGKVTFHGKNLYApdvDPVEVRRRIGMVFQkpnpF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1465 DALLdhmtgREMLVMYARLRGIPERLiNACVENTLR-GLLLEPHANKLVKT---YSGGNKRKLSTGIALIGEPAVIFLDE 1540
Cdd:PRK14243 104 PKSI-----YDNIAYGARINGYKGDM-DELVERSLRqAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1541 PSTGMDPVARRLLWDTVARARESgKAIVITSHSMEE 1576
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQ 212
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
530-721 |
2.17e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 46.04 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 530 IKIKHLSKVFQVGNKDKMGIRDL----------------TLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGHAYIH 593
Cdd:PRK13545 5 VKFEHVTKKYKMYNKPFDKLKDLffrskdgeyhyalnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 594 GyeisqDMAQIRKSLGLCPQhdvlfdnLTVAEHLyfyaQLKGLSLQKCPEEVKQML-HILSLEDKrdlrSKFL------- 665
Cdd:PRK13545 85 G-----SAALIAISSGLNGQ-------LTGIENI----ELKGLMMGLTKEKIKEIIpEIIEFADI----GKFIyqpvkty 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 666 SGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQQKSD-RTVLLTTH 721
Cdd:PRK13545 145 SSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQgKTIFFISH 201
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1383-1570 |
2.38e-04 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 45.70 E-value: 2.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1383 INELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVG-GYSIS------------- 1448
Cdd:TIGR03719 7 MNRVSKVVPPKKEIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKVGylpqepqldptkt 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1449 ---------SDIGKVRQR-----MGYC---PQFDALLDHMtgremlvmyARLrgipERLINAC----VENTLR----GLL 1503
Cdd:TIGR03719 85 vrenveegvAEIKDALDRfneisAKYAepdADFDKLAAEQ---------AEL----QEIIDAAdawdLDSQLEiamdALR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 569000489 1504 LePHANKLVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDpvARRLLWDTVARARESGKAIVIT 1570
Cdd:TIGR03719 152 C-PPWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD--AESVAWLERHLQEYPGTVVAVT 215
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
558-736 |
2.48e-04 |
|
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: 43.71 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 558 EGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyeisqdmaqirkslglcpqhDVLFDNLTVAEHlyfyaqlkgls 637
Cdd:cd03222 24 EGEVIGIVGPNGTGKTTAVKILAGQLIPNGD--------------------------NDEWDGITPVYK----------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 638 lqkcPEEVKqmlhilsledkrdlrskfLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR----RAIWDLLqqQKSD 713
Cdd:cd03222 67 ----PQYID------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRlnaaRAIRRLS--EEGK 122
|
170 180
....*....|....*....|...
gi 569000489 714 RTVLLTTHFMDEADLLGDRIAIL 736
Cdd:cd03222 123 KTALVVEHDLAVLDYLSDRIHVF 145
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
549-741 |
2.90e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.55 E-value: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKT-TTMSLLT---GLFppTSGHAYIHGYE---------ISQDMAQI---RKSLGLcp 612
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyGRN--ISGTVFKDGKEvdvstvsdaIDAGLAYVtedRKGYGL-- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 613 qhdVLFD----NLTVAEhlyfyaqLKGLSLQKCPEEVKQmlhILSLED-KRDLRSKF---------LSGGMKRKLSIGIA 678
Cdd:NF040905 352 ---NLIDdikrNITLAN-------LGKVSRRGVIDENEE---IKVAEEyRKKMNIKTpsvfqkvgnLSGGNQQKVVLSKW 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 569000489 679 LIAGSKVLMLDEPTSGMDAVSRRAIWDLLQQ-QKSDRTVLLTTHFMDEadLLG--DRIAILAKGEL 741
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPE--LLGmcDRIYVMNEGRI 482
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1376-1591 |
3.86e-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: 45.06 E-value: 3.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1376 MLDTPLI-INELSKVYDQRAPL-LAVDRISLAVQKGECFGLLGFNGAGKTTTF----KMLTGEETITSGDAFVGGYSISS 1449
Cdd:COG4172 1 MMSMPLLsVEDLSVAFGQGGGTvEAVKGVSFDIAAGETLALVGESGSGKSVTAlsilRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1450 ----DIGKVR-QRMGYCPQfdallDHMT--------GR---EMLVMYARLRGIPERliNACVEntlrglLLE----PHAN 1509
Cdd:COG4172 81 lserELRRIRgNRIAMIFQ-----EPMTslnplhtiGKqiaEVLRLHRGLSGAAAR--ARALE------LLErvgiPDPE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1510 KLVKTY----SGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARR----LLWDTVaraRESGKAIVITSHSMEECEALC 1581
Cdd:COG4172 148 RRLDAYphqlSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAqildLLKDLQ---RELGMALLLITHDLGVVRRFA 224
|
250
....*....|
gi 569000489 1582 TRLAIMVQGQ 1591
Cdd:COG4172 225 DRVAVMRQGE 234
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
549-739 |
4.25e-04 |
|
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: 45.29 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 549 IRDLTLNLYEGQITVLLGHNGAGKTTTMSLLTGLFPPTSGhayihgyeisqdmaQIRKS--LGLCPQHDVLFDNlTVAEH 626
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEG--------------KIKHSgrISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 627 LYF---YAQLKGLSLQK-CpeEVKQMLHILSLEDKRDLRSK--FLSGGMKRKLSIGIALIAGSKVLMLDEPTSGMDAVSR 700
Cdd:TIGR01271 507 IIFglsYDEYRYTSVIKaC--QLEEDIALFPEKDKTVLGEGgiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 569000489 701 RAIWD-LLQQQKSDRTVLLTTHFMDEADlLGDRIAILAKG 739
Cdd:TIGR01271 585 KEIFEsCLCKLMSNKTRILVTSKLEHLK-KADKILLLHEG 623
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1402-1571 |
4.58e-04 |
|
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: 45.29 E-value: 4.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEetitsgdafvggysISSDIGKVRQ--RMGYCPQFDALLDHMTGREML-- 1477
Cdd:TIGR01271 445 ISFKLEKGQLLAVAGSTGSGKSSLLMMIMGE--------------LEPSEGKIKHsgRISFSPQTSWIMPGTIKDNIIfg 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1478 VMYARLRgiPERLINAC-VENTLRGLllePHANKLVK-----TYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARR 1551
Cdd:TIGR01271 511 LSYDEYR--YTSVIKACqLEEDIALF---PEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEK 585
|
170 180
....*....|....*....|.
gi 569000489 1552 LLWDT-VARARESGKAIVITS 1571
Cdd:TIGR01271 586 EIFEScLCKLMSNKTRILVTS 606
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1414-1546 |
5.72e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 5.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1414 LLGFNGAGKTTTFKMLTGEETITSGDAFVGgysissdiGKVRQRMGYCPQFDALldHMTGREMLVMYARLRGIPERLINA 1493
Cdd:PLN03073 540 MVGPNGIGKSTILKLISGELQPSSGTVFRS--------AKVRMAVFSQHHVDGL--DLSSNPLLYMMRCFPGVPEQKLRA 609
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 569000489 1494 CVEN-TLRG-LLLEPhanklVKTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMD 1546
Cdd:PLN03073 610 HLGSfGVTGnLALQP-----MYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD 659
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
534-605 |
7.71e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 7.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 534 HLSKVFQVGNKDKmgirDLTLNLYEGQITVLLGHNGAGKTTTMSLL----TGLFPP-TSGHAYIHGYEISQDM---AQIR 605
Cdd:TIGR00606 7 SILGVRSFGIEDK----DKQIIDFFSPLTILVGPNGAGKTTIIECLkyicTGDFPPgTKGNTFVHDPKVAQETdvrAQIR 82
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1402-1572 |
8.45e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.09 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1402 ISLAVQKGECFGLLGFNGAGKTTTFKMLTGEE--TITSGDAFVGGYSISSDIGKVRQRMGYCPQF------------DAL 1467
Cdd:CHL00131 26 LNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLGIFLAFqypieipgvsnaDFL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1468 ldhmtgreMLVMYARL--RGIPE-------RLINacveNTLRGLLLEPH-ANKLV-KTYSGGNKRKLSTGIALIGEPAVI 1536
Cdd:CHL00131 106 --------RLAYNSKRkfQGLPEldpleflEIIN----EKLKLVGMDPSfLSRNVnEGFSGGEKKRNEILQMALLDSELA 173
|
170 180 190
....*....|....*....|....*....|....*.
gi 569000489 1537 FLDEPSTGMDPVARRLLWDTVARARESGKAIVITSH 1572
Cdd:CHL00131 174 ILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1384-1463 |
9.33e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 43.95 E-value: 9.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1384 NELSKVYDQRAPLLavDRISLAVQKGECFGLLGFNGAGKTTTFKMLTGEETITSGDAFVG-GYSIssdigkvrqrmGYCP 1462
Cdd:PRK11819 10 NRVSKVVPPKKQIL--KDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-----------GYLP 76
|
.
gi 569000489 1463 Q 1463
Cdd:PRK11819 77 Q 77
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1381-1423 |
1.61e-03 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 42.81 E-value: 1.61e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 569000489 1381 LIINELSKVY-DQRAPLLAVDRISLAVQKGECFGLLGFNGAGKT 1423
Cdd:PRK11022 4 LNVDKLSVHFgDESAPFRAVDRISYSVKQGEVVGIVGESGSGKS 47
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1399-1608 |
2.38e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 41.82 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1399 VDRISLAVQKGECFGLLGFNGAGKTTTFKMLTG-----EETITSGDAFVGGYSI-SSDIGKVRQRMGYCPQFDALLDHMT 1472
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 1473 GREMLVMYARLrgipERLINACVENTLR-------GLLLEPHANKL---VKTYSGGNKRKLSTGIALIGEPAVIFLDEPS 1542
Cdd:PRK14247 99 IFENVALGLKL----NRLVKSKKELQERvrwalekAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 569000489 1543 TGMDPVARRLLWDTVARARESgKAIVITSHSMEECEALCTRLAIMVQGQFKCLG-------SPQH-LKSKFGSG 1608
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGptrevftNPRHeLTEKYVTG 247
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1513-1570 |
2.81e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.71 E-value: 2.81e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 569000489 1513 KTYSGGNKRKLSTGIALIGEPAVIFLDEPSTGMDPVARRLLWDTVARARESGKAIVIT 1570
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| RsgA_GTPase |
pfam03193 |
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ... |
537-581 |
3.30e-03 |
|
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.
Pssm-ID: 427191 [Multi-domain] Cd Length: 174 Bit Score: 40.22 E-value: 3.30e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 569000489 537 KVFQVGNKDKMGIRDLtLNLYEGQITVLLGHNGAGKTTTMSLLTG 581
Cdd:pfam03193 85 PVLFVSAKTGEGIEAL-KELLKGKTTVLAGQSGVGKSTLLNALLP 128
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
547-605 |
3.56e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 40.56 E-value: 3.56e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 569000489 547 MGIRDLTLNLYEGqITVLLGHNGAGKTTTMS----LLTGLFPPTS----GHAYIHGYEIS---QDMAQIR 605
Cdd:pfam13476 7 RSFRDQTIDFSKG-LTLITGPNGSGKTTILDaiklALYGKTSRLKrksgGGFVKGDIRIGlegKGKAYVE 75
|
|
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