|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2176 |
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: 2383.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1 MPSAGTLPWVQGIICNANNPCFRYPTPGEAPGVVGNFNKSIVARLFSDARRLLLYSQKDTSMKDMRKVLRTLQQI----- 75
Cdd:TIGR01257 61 MPSAGMLPWLQGIFCNVNNPCFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFmdtlr 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 76 ----KKSSSNLKLQDFLVDNETFSGFLYHNLSLPKSTVDKMLRADVILHKvFLQGY-QLHLTSL-CNGSKSEEMI----Q 145
Cdd:TIGR01257 141 thpeRIAGRGIRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQ-FAYGVpDLELKDIaCSEALLERFIifsqR 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 146 LGDQEVSE-LCGLPREKLAAAERVLRSNMDILKpILRTLNSTSPFPSKEL-AEATKTLLHSLGTLAQELFSMRSWSDMRQ 223
Cdd:TIGR01257 220 RGAQTVRDaLCSLSQGTLQWIEDTLYANVDFFK-LFHVLPTLLDSRSQGInLRSWGGILSDMSPRIQEFIHRPSVQDLLW 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 224 EVMFLTNVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAETFYDNSTTPYCNDLMKNLE 303
Cdd:TIGR01257 299 VTRPLLQNGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDKRTTSFCNALIQSLE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 304 SSPLSRIIWKALKPLLVGKILYTPDTPATRQVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMENSQEMDLVRMLLDSR 383
Cdd:TIGR01257 379 SNPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNP 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 384 DNDHFWEQQLDGLDWTAQDIVAFLAKHPEDVQSSNGSVYTWREAFNETNQAIRTISRFMECVNLNKLEPIATEVWLINKS 463
Cdd:TIGR01257 459 TVKDFINRQLGEEGITAEAVLNFLYNGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 464 MELLDERKFWAGIVFTGITPGSIELPHHVKYKIRMDIDNVERTNKIKDGYWDPGPRADPFEDMRYVWGGFAYLQDVVEQA 543
Cdd:TIGR01257 539 LSLLEENRFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQG 618
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 544 IIRVLTGTEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWF 623
Cdd:TIGR01257 619 ITRSQMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWC 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 624 SWFISSLIPLLVSAGLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVL 703
Cdd:TIGR01257 699 TWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHIL 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 704 CVAWQDYVGFTLKIFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESPVEEDGFNLTTSVSMMLFDTFLYGVMTWYIE 783
Cdd:TIGR01257 779 CFAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLD 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 784 AVFPGQYGIPRPWYFPCTKSYWFG--------EESDEKSHPGSNQKR-------ISEICMEEEPTHLKLGVSIQNLVKVY 848
Cdd:TIGR01257 859 QVFPGDYGTPLPWYFLLQESYWLGgegcstreERALEKTEPLTEEMEdpehpegINDSFFERELPGLVPGVCVKNLVKIF 938
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 928
Cdd:TIGR01257 939 EPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHL 1018
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR 1008
Cdd:TIGR01257 1019 TVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR 1097
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1009 RGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKdVESSLSSCRNSSST 1088
Cdd:TIGR01257 1098 RSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRK-MKNIQSQRGGCEGT 1176
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1089 VSYLKKEDSVsqsSSDAGLGSDHESDTLTIDVSAISNLIRKHVSEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDDR 1168
Cdd:TIGR01257 1177 CSCTSKGFST---RCPARVDEITPEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEET 1253
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1169 LSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGtlpARRNRRAFGDKQSCLRPfTEDDAADPNDSDIDPESRETDLL 1248
Cdd:TIGR01257 1254 LADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGG---AQQKRENANLRHPCSGP-TEKAGQTPQASHTCSPGQPAAHP 1329
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1249 SGM-----DGKGSYQVKGWKLTQQQFVALLWKRLLIARRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPSLELQPWM 1323
Cdd:TIGR01257 1330 EGQpppepEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWM 1409
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1324 YNEQYTFVSNDAPEDTGTLELLNALTKDPGFGTRCMEGNPIPDTPCqAGEEEWTTAPVPQTIMDLFQNGNWTMQNPSPAC 1403
Cdd:TIGR01257 1410 YGQQYTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEEWLPEYPC-GNSTPWKTPSVSPNITHLFQKQKWTAAHPSPSC 1488
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1404 QCSSDKIKKMLPVCPPGAGGLPPPQRKQNTADILQDLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGvSNTQ 1483
Cdd:TIGR01257 1489 RCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIG-GKLP 1567
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1484 ALPPSQE-----VNDATKQMKKHLKLAKDSSADRFLNslgrFMTGLDTRNNVKVWFNNKGWHAISSFLNVINNAILRANL 1558
Cdd:TIGR01257 1568 AIPITGEalvgfLSDLGQMMNVSGGPVTREASKEMPD----FLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASL 1643
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1559 QKGENPSHYGITAFNHPLNLTKQQLSEVAPMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIY 1638
Cdd:TIGR01257 1644 PKDRDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTY 1723
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1639 WLSNFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIG 1718
Cdd:TIGR01257 1724 WLTNFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIG 1803
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1719 INGSVATFVLELFTDNK-LNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFVSPLSWDLVGRNLFAMA 1797
Cdd:TIGR01257 1804 INSSAITFVLELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMA 1883
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1798 VEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIP 1877
Cdd:TIGR01257 1884 VEGVVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVR 1963
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1878 PGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVP 1957
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVP 2043
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1958 EKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSV 2037
Cdd:TIGR01257 2044 AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAV 2123
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2038 VLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSN----PDLKPVQDFFGLAFPGSVPKEKHR 2113
Cdd:TIGR01257 2124 VLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHY 2203
|
2170 2180 2190 2200 2210 2220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2114 NMLQYQLPSslSSLARIFSILSQSKKRLHIEDYSVSQTTLDQVFVNFAKDQSDDdhlKDLSLH 2176
Cdd:TIGR01257 2204 NMLQFQVSS--SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTET---YDLPLH 2261
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
839-1059 |
3.38e-116 |
|
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: 366.83 E-value: 3.38e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGL-TDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLK 1059
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1852-2072 |
3.49e-115 |
|
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: 364.13 E-value: 3.49e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2072
Cdd:cd03263 161 TSGLDPASRRAIWD-LILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
839-1076 |
1.64e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 276.94 E-value: 1.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 999 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVE 1076
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEAR 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1852-2075 |
3.50e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 249.98 E-value: 3.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRF 2075
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
839-1049 |
1.10e-65 |
|
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: 220.35 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03230 79 PEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 999 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
841-1049 |
4.10e-63 |
|
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: 215.88 E-value: 4.10e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQ 920
Cdd:COG4555 4 VENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1000
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGL-EEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 1001 AGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
839-1059 |
1.90e-61 |
|
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: 209.92 E-value: 1.90e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 999 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLK 1059
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
846-1063 |
1.22e-59 |
|
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: 208.01 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 846 KVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLF 925
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 DMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFEL-GEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 1006 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLG 1063
Cdd:TIGR01188 158 RTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1867-2160 |
1.66e-57 |
|
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: 201.85 E-value: 1.66e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAITELLTGREH 1946
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1947 VEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNC 2026
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2027 ALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSnpDLKPVQDFFGLAFPGS 2106
Cdd:TIGR01188 167 IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ--SLKVEVSMLIAELGET 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2107 V--PKEKHRNMLQYQLPSSLSS--LARIFSILsqSKKRLHIEDYSVSQTTLDQVFVNF 2160
Cdd:TIGR01188 245 GlgLLAVTVDSDRIKILVPDGDetVPEIVEAA--IRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1852-2072 |
5.34e-57 |
|
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: 197.21 E-value: 5.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2072
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
839-1049 |
3.67e-55 |
|
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: 191.64 E-value: 3.67e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMkvAVDGLALNFYEGqITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1852-2062 |
1.73e-54 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 188.38 E-value: 1.73e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEffallrgvpekevgkvgewairklglvkygekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1852-2077 |
1.76e-52 |
|
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: 185.06 E-value: 1.76e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2077
Cdd:COG4555 160 TNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
840-1048 |
4.76e-49 |
|
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: 174.19 E-value: 4.76e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVC 918
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 998 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
839-1048 |
1.40e-48 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 176.07 E-value: 1.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 918
Cdd:COG4152 2 LELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
839-1054 |
1.24e-47 |
|
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: 170.98 E-value: 1.24e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 917
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQH--NVLFdMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:COG1122 80 VFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
839-1053 |
1.14e-46 |
|
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: 167.54 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 916
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGM-EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1852-2063 |
9.60e-46 |
|
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: 164.67 E-value: 9.60e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGeCFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2012 TTGMDPKAR-RF--LwncaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2063
Cdd:cd03264 158 TAGLDPEERiRFrnL----LSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
839-1049 |
1.07e-45 |
|
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: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQnLGVC 918
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVkaemEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 999 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
839-1054 |
1.67e-44 |
|
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: 162.07 E-value: 1.67e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 914
Cdd:COG1127 6 IEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMLTVEEHIWFYAR-LKGLSEkhvkAEMEQMALD----VGLPSSKLKsKTSQLSGGMQRKLSVALAFVG 989
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLReHTDLSE----AEIRELVLEklelVGLPGAADK-MPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 990 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:COG1127 159 DPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
839-1049 |
1.73e-44 |
|
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: 161.15 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 918
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 999 PTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03259 157 PLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
856-1001 |
5.16e-44 |
|
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: 157.42 E-value: 5.16e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-RQNLGVCPQHNVLFDMLTVEEHI 934
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 935 WFYARLKGLSEKHVKAEMEQMALDVGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
839-1054 |
1.00e-43 |
|
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: 159.59 E-value: 1.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 914
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEaVGLRGAEDL-YPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
839-1054 |
1.24e-43 |
|
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: 159.77 E-value: 1.24e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 917
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
839-1045 |
4.50e-43 |
|
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: 157.25 E-value: 4.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDG--MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstIRQNLG 916
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 997 DEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEADVLGDRIAIIS 1045
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
839-1048 |
6.78e-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: 156.29 E-value: 6.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 918
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1851-2066 |
1.76e-42 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 155.60 E-value: 1.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNM 1928
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
839-1049 |
1.33e-41 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 153.03 E-value: 1.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 -QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPsSKLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADvLGDRIAIISHGKL 1049
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1852-2061 |
1.74e-41 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 152.37 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNiHEVHQNMGYC 1931
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
839-1048 |
3.88e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 154.96 E-value: 3.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMeQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAARALV-PPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
828-1047 |
4.03e-41 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 153.32 E-value: 4.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 828 MEEEPTHLklgvSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 905
Cdd:COG1116 1 MSAAAPAL----ELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 906 SemstIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVAL 985
Cdd:COG1116 77 G----PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGL-AGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 986 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
837-1048 |
4.93e-41 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 155.76 E-value: 4.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 916
Cdd:PRK13536 40 VAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMaLDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSL-LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 997 DEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
839-1041 |
6.51e-41 |
|
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: 150.71 E-value: 6.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGL--SEKHVKAEMEQMALDvGLpsskLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLraDREAIDEALEAVGLA-GL----ADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHhmDEADVLGDRI 1041
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
839-1049 |
2.02e-39 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 2.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 -QNLGVCPQ-HNvLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:COG1136 85 rRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADvLGDRIAIISHGKL 1049
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
840-1048 |
2.66e-39 |
|
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: 143.92 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVC 918
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQhnvlfdmltveehiwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1851-2061 |
6.90e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.41 E-value: 6.90e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGY 1930
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVEFFALLRGVP----EKEVGKVGEWAirklGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSaaaaRALVPPLLEFA----KLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
839-1055 |
8.45e-39 |
|
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: 153.52 E-value: 8.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTI 911
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 912 RQNLGVCPQH--NVLFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1055
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1851-2166 |
1.27e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 147.18 E-value: 1.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNrNSILSniHEVHQNMGY 1930
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-GEPLD--PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPqfdaitE---L---LTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:COG4152 76 LP------EergLypkMKVGEQLVYLARLKGLSKAEAKRrADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGdGYTIVV 2083
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2084 RIAGSNPDLKpvqdffglAFPGSVPKEKHRNMLQYQLPSSLSSlARIFSILSQskkRLHIEDYSVSQTTLDQVFVNFAKD 2163
Cdd:COG4152 228 EADGDAGWLR--------ALPGVTVVEEDGDGAELKLEDGADA-QELLRALLA---RGPVREFEEVRPSLNEIFIEVVGE 295
|
...
gi 5734101 2164 QSD 2166
Cdd:COG4152 296 KAE 298
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1852-2042 |
4.75e-38 |
|
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: 142.23 E-value: 4.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEvGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR-EAIDE-ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2042
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
839-1049 |
2.25e-37 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 141.56 E-value: 2.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
840-1054 |
5.51e-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: 140.26 E-value: 5.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP 919
Cdd:cd03219 2 EVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 920 --QHNVLFDMLTVEE------------HIWFYARLKGLSEKHVKAEmeqMALD-VGLpSSKLKSKTSQLSGGMQRKLSVA 984
Cdd:cd03219 80 tfQIPRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAE---ELLErVGL-ADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 985 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
839-1049 |
6.39e-37 |
|
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: 139.95 E-value: 6.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 QNLGVCPQH--NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD--VGLPSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLvgVGLPEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1852-2066 |
8.90e-37 |
|
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: 138.95 E-value: 8.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSnihEVHQNMGYC 1931
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2010
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRrIDEW-LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2011 PTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
839-1048 |
1.85e-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: 136.36 E-value: 1.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:cd03228 81 VPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGK 1048
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
839-1049 |
3.97e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 137.49 E-value: 3.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQ 913
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 914 NLGVCPQ-HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:COG2884 80 RIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVRE-VLDlVGL-SDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
841-1048 |
7.08e-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: 135.01 E-value: 7.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGV 917
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIwfyarlkglsekhvkaemeqmaldvGLPssklksktsqLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:cd03229 81 VFQDFALFPHLTVLENI-------------------------ALG----------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 998 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd03229 126 EPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
854-1048 |
1.13e-35 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 148.35 E-value: 1.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 854 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTiRQNLGVCPQHNVLFDMLTVEE 932
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIAT-RRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 933 HIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1012
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDL-ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190
....*....|....*....|....*....|....*...
gi 5734101 1013 ELL--LKYRQGRTIILSTHHMDEADvLGDRIAIISHGK 1048
Cdd:NF033858 438 RLLieLSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1852-2091 |
2.58e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.81 E-value: 2.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL-KNRFGdgyTIVVRIAGSNP 2090
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALiDEHIG---CQVIEIYGGDP 276
|
.
gi 5734101 2091 D 2091
Cdd:PRK13536 277 H 277
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
839-1051 |
3.16e-35 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.60 E-value: 3.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 918
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQH-NVLFDM-LTVEE--------HIWFYARLKGLSEKHVKAEMEQmaldVGLpsSKLKSKT-SQLSGGMQRKLSVALAF 987
Cdd:COG1121 81 PQRaEVDWDFpITVRDvvlmgrygRRGLFRRPSRADREAVDEALER----VGL--EDLADRPiGELSGGQQQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCC 1051
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
839-1054 |
3.58e-35 |
|
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: 135.06 E-value: 3.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 918
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 999 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
840-1050 |
4.19e-35 |
|
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: 134.20 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVCP 919
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 920 QH-NVLFDM-LTVEE--------HIWFYARLKglseKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:cd03235 75 QRrSIDRDFpISVRDvvlmglygHKGLFRRLS----KADKAKVDE-ALErVGL-SELADRQIGELSGGQQQRVLLARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLC 1050
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
839-1054 |
5.66e-35 |
|
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: 135.17 E-value: 5.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLG 916
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRreLARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEE--------HIWFYARLKGLSEKHVKAEMEQMALdvglpsSKLKSKT-SQLSGGMQRKLSVALAF 987
Cdd:COG1120 79 YVPQEPPAPFGLTVRElvalgrypHLGLFGRPSAEDREAVEEALERTGL------EHLADRPvDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1496-1809 |
9.45e-35 |
|
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: 137.52 E-value: 9.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1496 KQMKKHLKLAKDSSADRFLNSLGRfMTGLDTRNNVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPSHYGITAFNHP 1575
Cdd:pfam12698 68 EEAKEALKNGKIDGLLVIPKGFSK-DLLKGESATVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIP 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1576 LNLTkqQLSEvaPMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPat 1655
Cdd:pfam12698 147 VEST--PLFN--PQSGYAYYLVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ-- 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1656 LVIIIFICFQQksYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGInGSVATFVlelftdnk 1735
Cdd:pfam12698 221 LLIILLLLFGI--GIPFGNLGLLLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFP-------- 289
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 1736 LNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADalerfgenrfvsplswdlVGRNLFAMAVEGVVFFLITVL 1809
Cdd:pfam12698 290 LEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSLWE------------------IAPSLIILLLFAVVLLLLALL 345
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
839-1054 |
3.23e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 134.02 E-value: 3.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE---MSTIR 912
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 QNLGVC---PQHNvLFDMlTVEEHIWFYARLKGLSE----KHVKAEMEQmaldVGLPSSKLKSKTS-QLSGGMQRKLSVA 984
Cdd:PRK13637 83 KKVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEeeieNRVKRAMNI----VGLDYEDYKDKSPfELSGGQKRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 985 LAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13637 157 GVVAMEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1853-2061 |
3.84e-34 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 131.44 E-value: 3.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYC 1931
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2009
Cdd:cd03225 81 FQ-NPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2010 EPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
840-1049 |
6.65e-34 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 130.71 E-value: 6.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGV 917
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHI--WFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:COG4619 79 VPQEPALWGG-TVRDNLpfPFQLRERKFDRERALELLER----LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
839-1049 |
7.90e-34 |
|
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: 131.15 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-----PTSGTAYILGKDIRSEMSTI-- 911
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 912 -RQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSS-KLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:cd03260 79 lRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRkAALWDEvKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
840-1048 |
9.03e-34 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 130.63 E-value: 9.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 916
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIWFYARLkgLSEKHVKAEMEQM-----ALDvglpsSKLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERVyelfpRLK-----ERRKQLAGTLSGGEQQMLAIARALMSRP 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd03224 152 KLLLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
839-1049 |
1.55e-33 |
|
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: 137.73 E-value: 1.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYILGKDIRSEMSTIR-QN 914
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSsKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLER-RLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 994 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
839-1068 |
2.23e-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: 129.97 E-value: 2.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTiRQNLGV 917
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 C--PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:cd03218 78 GylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHI-THLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEADVLGDRIAIISHGKLCCVGSS-LFLKNQLGTGYYL 1068
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD-RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPeEIAANELVRKVYL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
854-1049 |
4.15e-33 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 129.77 E-value: 4.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 854 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFDMLTVE 931
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 932 EHI-----------WFYARLKGLSEKHVKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:COG0411 98 ENVlvaaharlgrgLLAALLRLPRARREEREARERAEEllerVGL-ADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYR--QGRTIILSTHHMDEadVLG--DRIAIISHGKL 1049
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDL--VMGlaDRIVVLDFGRV 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
837-1068 |
4.92e-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: 137.20 E-value: 4.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEmSTIRQN 914
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDE-DDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMlTVEEHIwfyaRL--KGLSEkhvkAEMEQMALDVGLPS----------SKLKSKTSQLSGGMQRKLS 982
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENL----RLarPDATD----EELWAALERVGLGDwlaalpdgldTWLGEGGRRLSGGERRRLA 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 983 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSSLFLKNQL 1062
Cdd:COG4987 482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQN 560
|
....*.
gi 5734101 1063 GTGYYL 1068
Cdd:COG4987 561 GRYRQL 566
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1853-2061 |
5.08e-33 |
|
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: 126.21 E-value: 5.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSN-IHEVHQNMGYC 1931
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFdaitelltgrehveffallrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
839-1054 |
6.79e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 129.73 E-value: 6.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 917
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
841-1048 |
6.92e-33 |
|
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: 128.84 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----------RSEMS 909
Cdd:cd03256 3 VENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQNLGVCPQHNVLFDMLT--VEEHIWFYARLKGLSEKHVKAEMEqmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALA 986
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrLGRRSTWRSLFGLFPKEEKQRALA--ALErVGL-LDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1852-2061 |
7.75e-33 |
|
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: 128.22 E-value: 7.75e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL-SNIHEVHQNMGY 1930
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQF--DAITELlTGREHVEFfALL-RGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2007
Cdd:COG1122 80 VFQNpdDQLFAP-TVEEDVAF-GPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2008 LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
835-1053 |
1.25e-32 |
|
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: 128.92 E-value: 1.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 835 LKLGVSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMST 910
Cdd:cd03294 21 LAKGKSKEEILK--KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 IRQN-LGVCPQHNVLFDMLTVEEHIWFYARLKGLS--EKHVKAeMEQMALdVGLPSSKlKSKTSQLSGGMQRKLSVALAF 987
Cdd:cd03294 99 LRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPraEREERA-AEALEL-VGLEGWE-HKYPDELSGGMQQRVGLARAL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03294 176 AVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
841-1053 |
3.38e-32 |
|
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: 126.68 E-value: 3.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYRDgmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 920
Cdd:cd03299 3 VENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1000
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGI-DHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1001 AGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
837-1049 |
4.14e-32 |
|
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: 126.29 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVK-VYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNL 915
Cdd:cd03267 19 LIGSLKSLFKrKYRE--VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 G-VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:cd03267 97 GvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSelLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
839-1054 |
4.08e-31 |
|
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: 131.03 E-value: 4.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:COG4988 337 IELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIWFYARlkGLSEKHVKAEMEQ-------MALDVGLpSSKLKSKTSQLSGG-MQRkLSVALAFVG 989
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRP--DASDEELEAALEAagldefvAALPDGL-DTPLGEGGRGLSGGqAQR-LALARALLR 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 990 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1054
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGT 554
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
840-1055 |
1.11e-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: 122.38 E-value: 1.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV-- 917
Cdd:TIGR04406 3 VAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIwfYARL---KGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVV 994
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI--MAVLeirKDLDRAEREERLEALLEEFQISHLR-DNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 995 ILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1055
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
842-1049 |
1.67e-30 |
|
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: 120.98 E-value: 1.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 842 QNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGV 917
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVkAEMEQMALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 996
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREI-RKRVPAALElVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 997 DEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
839-1049 |
2.11e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 124.04 E-value: 2.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYR-----DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI 899
Cdd:COG4586 2 IEVENLSKTYRvyekePGLKgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 900 LGKDIRSEMSTIRQNLGVcpqhnV-------LFDmLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKT 970
Cdd:COG4586 82 LGYVPFKRRKEFARRIGV-----VfgqrsqlWWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVelLDLG---ELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 971 SQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:COG4586 153 RQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHG 231
|
..
gi 5734101 1048 KL 1049
Cdd:COG4586 232 RI 233
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
839-1053 |
2.66e-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: 120.44 E-value: 2.66e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 918
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQI-EHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 999 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03301 157 PLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
839-1054 |
3.33e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 3.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 918
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVAL--AFVGGSKVVI 995
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGL-EDLLDRKPKQLSGGqRQR---VALgrALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 996 LDEPTAGVDPYSR---RGiwEL--LLKyRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:COG3839 157 LDEPLSNLDAKLRvemRA--EIkrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1851-2156 |
3.88e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 123.27 E-value: 3.88e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP-------------------AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA- 1910
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1911 ------FLNRNSILSNIHEVhqnMGycpQ-----FDaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLvkyGE 1979
Cdd:COG4586 81 vlgyvpFKRRKEFARRIGVV---FG---QrsqlwWD-----LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDL---GE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1980 KYagnysggNK--RKLS--------TAMALIGGPPVVFLDEPTTGMDPKA----RRFLwncaLSVVKE-GRSVVLTSHSM 2044
Cdd:COG4586 147 LL-------DTpvRQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSkeaiREFL----KEYNRErGTTILLTSHDM 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2045 EECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKpvqdffgLAFPGSVpKEKHRNMLQYQLPSSL 2124
Cdd:COG4586 216 DDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLE-------LPRGGEV-IEREGNRVRLEVDPRE 287
|
330 340 350
....*....|....*....|....*....|..
gi 5734101 2125 sSLARIFSILSQskkRLHIEDYSVSQTTLDQV 2156
Cdd:COG4586 288 -SLAEVLARLLA---RYPVRDLTIEEPPIEEV 315
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
839-1049 |
1.69e-29 |
|
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: 116.37 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 918
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 pqhnvlfdmLTVeehiwfyarlkglsekhvkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03216 78 ---------AMV----------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 999 PTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03216 109 PTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
839-1054 |
2.01e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.14 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLG 916
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIW--------FYARLKGLSEKhVKAEMEQMALDVglpssKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVlgleptkgGRLDRKAARAR-IRELSERYGLDV-----DPDAKVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLccVGS 1054
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
840-1053 |
2.44e-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: 2.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLGV 917
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPkeLARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLtveehiwfyarlkGLSEKHVkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:cd03214 78 VPQALELLGLA-------------HLADRPF----------------------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 998 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03214 123 EPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
840-1055 |
4.80e-29 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 117.44 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSemstiR 912
Cdd:COG1137 5 EAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkRA-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKL-KSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEAdvLG--DRIAIISHGKLCCVGSS 1055
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
837-1054 |
1.21e-28 |
|
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: 116.28 E-value: 1.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLG 916
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALD----VGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGS 991
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGLRVKPRSERPPEAEIRAKVHEllklVQL--DWLADRyPAQLSGGQRQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 992 KVVILDEPTAGVDPYSRRGI--WELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:cd03296 156 KVLLLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
839-1049 |
1.80e-28 |
|
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: 116.06 E-value: 1.80e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGM--KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNL 915
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQH--NVLFDMLTVEEHIwfyAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGG-MQRklsVAL--AFVG 989
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGqRQR---VAIarALIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 990 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
848-1034 |
2.20e-28 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 114.06 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 922
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 923 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGA--SGLRERpTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 5734101 1002 GVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEA 1034
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1852-2061 |
2.59e-28 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 114.54 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNihEVHQ-NMGY 1930
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERrNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVEFfAL-LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2009
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 2010 EPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03259 156 EPLSALDAKLREEL----REELKElqrelGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
839-1061 |
2.95e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.37 E-value: 2.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGV 917
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpsSKLKSKTS-QLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK13647 84 VFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEE-ALKaVRM--WDFRDKPPyHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQ 1061
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1851-2069 |
3.08e-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: 115.53 E-value: 3.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMG 1929
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDAITELLTGREHVE-----FFALLRGVPEKEVGKVgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2004
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEDREAV-EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2005 VVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2069
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEV----LELLRRlarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
821-1068 |
3.18e-28 |
|
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: 123.79 E-value: 3.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 821 KRISEIcMEEEP-----------THLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL 889
Cdd:COG2274 446 ERLDDI-LDLPPereegrsklslPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGL 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 890 FPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIWFYArlKGLSEKHVKAEMEQMALD---VGLPS-- 963
Cdd:COG2274 525 YEPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITLGD--PDATDEEIIEAARLAGLHdfiEALPMgy 601
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 964 -SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAdvlgD 1039
Cdd:COG2274 602 dTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----D 677
|
250 260
....*....|....*....|....*....
gi 5734101 1040 RIAIISHGKLCCVGSSLFLKNQLGTGYYL 1068
Cdd:COG2274 678 RIIVLDKGRIVEDGTHEELLARKGLYAEL 706
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
837-1049 |
6.74e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 115.70 E-value: 6.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--- 910
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 --IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALA 986
Cdd:PRK13641 81 kkLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
848-1054 |
1.92e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 114.35 E-value: 1.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLAL-----NFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-----MSTIRQNLGV 917
Cdd:PRK13634 10 HRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkkLKPLRKKVGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 C---PQHNvLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 994
Cdd:PRK13634 90 VfqfPEHQ-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 995 ILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1852-2061 |
2.00e-27 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 112.20 E-value: 2.00e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRR--KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIHEV----- 1924
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 -HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEEcEALCTRMAIMVNGR 2061
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
839-1076 |
2.26e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.11 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMST 910
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--SLFLKNQLGT 1064
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkELFKDKKKLA 241
|
250
....*....|....*..
gi 5734101 1065 GYYLTL-----VKKDVE 1076
Cdd:PRK13646 242 DWHIGLpeivqLQYDFE 258
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
839-1049 |
2.47e-27 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 115.56 E-value: 2.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 QNLGVCPQH-NvLFDMLTVEEHIWFYARLKGLSekhvKAEMEQMA---LD-VGLpSSKLKSKTSQLSGGMQRKLSVALAF 987
Cdd:COG1135 82 RKIGMIFQHfN-LLSSRTVAENVALPLEIAGVP----KAEIRKRVaelLElVGL-SDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMdeaDV---LGDRIAIISHGKL 1049
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEM---DVvrrICDRVAVLENGRI 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1851-2071 |
3.23e-27 |
|
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: 118.47 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNRNSIL-SNIHEVHQ 1926
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLeLSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQfDAITEL--LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2004
Cdd:COG1123 84 RIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2005 VVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1851-2070 |
4.09e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.10 E-value: 4.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRnsilSNIHEVHQNMGY 1930
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITEL--LTGREHVEF-----FALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMgrygrRGLFRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLGSVQH 2070
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
837-1073 |
5.48e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 112.92 E-value: 5.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EM 908
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 STIRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLS-EKHVKAEMEQMALdVGLPSSKLKSKTSQLSGGMQRKLSVAL 985
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSqEEAEALAREKLAL-VGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 986 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--------SL 1056
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdifqdvDF 238
|
250 260
....*....|....*....|.
gi 5734101 1057 FLKNQLG----TGYYLTLVKK 1073
Cdd:PRK13649 239 LEEKQLGvpkiTKFAQRLADR 259
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
858-1049 |
5.92e-27 |
|
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: 111.21 E-value: 5.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 858 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEmsTIRQNLGVCPQHNVLFDMLTVEEHI 934
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 935 WFYARLKgLSEKHVKAEMEQMALDVGLPSSKLK----SKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1010
Cdd:cd03234 103 TYTAILR-LPRKSSDAIRKKRVEDVLLRDLALTriggNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5734101 1011 IWELLLKY-RQGRTIILSTHHmDEADV--LGDRIAIISHGKL 1049
Cdd:cd03234 182 LVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1869-2013 |
8.98e-27 |
|
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: 108.12 E-value: 8.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1869 VDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQFDAITELLTGREHV 1947
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1948 EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2013
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
843-1049 |
1.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 843 NLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCP 919
Cdd:PRK13639 6 DLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 920 QH--NVLFdMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKtSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:PRK13639 85 QNpdDQLF-APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPP-HHLSGGQKKRVAIAGILAMKPEIIVLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 998 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK13639 163 EPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
840-1049 |
1.96e-26 |
|
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: 108.88 E-value: 1.96e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----RSEMSTIRQN 914
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 lgvcPQHNVLFDmlTVEEHIwfYARLKGLSEKHVKAE--MEQMALdvglpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGS 991
Cdd:cd03226 80 ----VDYQLFTD--SVREEL--LLGLKELDAGNEQAEtvLKDLDL------YALKERHPLsLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
848-1049 |
2.22e-26 |
|
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: 109.22 E-value: 2.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF- 925
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 ----DMLTV------EEHIWFYARLKGLSE---KHVKAemeqMALDVGlpssklkSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAELAGVTDfvnKHPNG----LDLQIG-------ERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKL 1049
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRP-SLLDLVDRIIVMDSGRI 216
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1852-2073 |
4.12e-26 |
|
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: 109.06 E-value: 4.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEV------ 1924
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 --HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWA---IRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
840-1048 |
5.64e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 108.53 E-value: 5.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 916
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-LPPhriARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEH--IWFYARLKGLSEKHVKAEMEQMaldvgLPssKLKSKTSQ----LSGGMQRKLSVALAFVGG 990
Cdd:COG0410 82 YVPEGRRIFPSLTVEENllLGAYARRDRAEVRADLERVYEL-----FP--RLKERRRQragtLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
855-1049 |
2.17e-25 |
|
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: 105.21 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC-----PQHNVLFDMLT 929
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 930 VEEHIwfyarlkglsekhvkaemeqmALdvglpssklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1009
Cdd:cd03215 95 VAENI---------------------AL------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5734101 1010 GIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03215 142 EIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1852-2073 |
4.55e-25 |
|
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: 105.70 E-value: 4.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHE-VHQNMG 1929
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2009
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2010 EPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
839-1048 |
6.30e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.32 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEM 908
Cdd:COG1101 2 LELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 -STIRQN--LGVCPQhnvlfdmLTVEEHIWF-YARLK------GLSEKHVKAEMEQMA-LDVGLPSsKLKSKTSQLSGGm 977
Cdd:COG1101 82 iGRVFQDpmMGTAPS-------MTIEENLALaYRRGKrrglrrGLTKKRRELFRELLAtLGLGLEN-RLDTKVGLLSGG- 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 978 QRK-LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:COG1101 153 QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
841-1049 |
6.64e-25 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 108.35 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 914
Cdd:PRK11153 4 LKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHnvlFDML---TVEEHIWFYARLKGLSEKHVKAEMEQMaLD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:PRK11153 84 IGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKARVTEL-LElVGL-SDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
839-1049 |
6.99e-25 |
|
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: 104.53 E-value: 6.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNL 915
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQHNVLFDMLTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 994
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVM 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 995 ILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03262 158 LFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
863-1049 |
7.78e-25 |
|
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: 103.78 E-value: 7.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 863 FYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTAYILGKDirSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 940
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP--LDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 KGLSekhvkaemeqmaldvglpssklksktsqlsGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ 1020
Cdd:cd03213 110 RGLS------------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
170 180 190
....*....|....*....|....*....|.
gi 5734101 1021 -GRTIILSTHH-MDEADVLGDRIAIISHGKL 1049
Cdd:cd03213 160 tGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
839-1033 |
1.43e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.78 E-value: 1.43e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNlVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSG-TAYILGKDIRSE-MSTIRQNLG 916
Cdd:COG1119 4 LELRN-VTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCpqHNVLFDMLTVEEHIW------FYARLkGLSeKHVKAEMEQMALD----VGLpsSKLKSKT-SQLSGGMQRKLSVAL 985
Cdd:COG1119 82 LV--SPALQLRFPRDETVLdvvlsgFFDSI-GLY-REPTDEQRERAREllelLGL--AHLADRPfGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 986 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDE 1033
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
848-1070 |
2.73e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 105.31 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 922
Cdd:PRK13636 15 YSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 923 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:PRK13636 94 QLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGI--EHLKDKpTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1002 GVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG--SSLFLKNQLGTGYYLTL 1070
Cdd:PRK13636 171 GLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRL 243
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1852-2061 |
6.06e-24 |
|
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: 102.80 E-value: 6.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRK-------------------PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA-- 1910
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1911 -----FLNRNSILSNIHEVhqnmgycpqFDAITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYA 1982
Cdd:cd03267 81 aglvpWKRRKKFLRRIGVV---------FGQKTQLWWDLPVIDSFYLLAaiyDLPPARFKKRLDELSELLDLEELLDTPV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1983 GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03267 152 RQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGR 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1851-2080 |
6.13e-24 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 108.45 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIY---RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL----SNIHE 1923
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VHQNMGYCPQ--FDAITELLTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDG 2078
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
..
gi 5734101 2079 YT 2080
Cdd:COG1123 500 YT 501
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1851-2071 |
6.95e-24 |
|
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: 102.66 E-value: 6.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIY--RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--RNSILSN--IHEV 1924
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDgtDLTLLSGkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQ-FDaiteLLTGR---EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2000
Cdd:cd03258 81 RRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2001 GGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
839-1035 |
8.02e-24 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 108.14 E-value: 8.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIWFYARlkGLSEKHVKAEMEQMALD---VGLPS---SKLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARP--DASDAEIREALERAGLDefvAALPQgldTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAD 1035
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1851-2061 |
8.60e-24 |
|
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: 102.81 E-value: 8.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIY---RrkrkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEV-- 1924
Cdd:COG0411 4 LLEVRGLTKRFgglV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 ------HQNMGYCPQFDAITELLTG---REHVEFFALLRGVP-----EKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNK 1990
Cdd:COG0411 79 lgiartFQNPRLFPELTVLENVLVAahaRLGRGLLAALLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1991 RKLSTAMALIGGPPVVFLDEPTTGMDP-----------KARRflwncalsvvKEGRSVVLTSHSMEECEALCTRMAIMVN 2059
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPeeteelaelirRLRD----------ERGITILLIEHDMDLVMGLADRIVVLDF 228
|
..
gi 5734101 2060 GR 2061
Cdd:COG0411 229 GR 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
839-1065 |
9.96e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 109.83 E-value: 9.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 918
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA----RHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQ---------HNvLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGL------PSSKLksktsqlSGGMQRKLSV 983
Cdd:NF033858 76 PRiaympqglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLapfadrPAGKL-------SGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 984 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR---TIILSTHHMDEADVLgDRIAIISHGKLCCVGSSLFLKN 1060
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
....*
gi 5734101 1061 QLGTG 1065
Cdd:NF033858 227 RTGAD 231
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
839-1054 |
1.35e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 107.03 E-value: 1.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRseMSTIR--QNLG 916
Cdd:COG1129 5 LEMRGISKSF-GGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VC--PQHNVLFDMLTVEEHIWF---YARLKGLSEKHVKAEMEQMALDVGLPSSkLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:COG1129 81 IAiiHQELNLVPNLSVAENIFLgrePRRGGLIDWRAMRRRARELLARLGLDID-PDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 992 KVVILDEPTAgvdPYSRRGIWELL-----LKyRQGRTIILSTHHMDEADVLGDRIAIISHGKLccVGS 1054
Cdd:COG1129 160 RVLILDEPTA---SLTEREVERLFriirrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
841-1054 |
1.69e-23 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 104.92 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYrDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 920
Cdd:PRK11607 22 IRNLTKSF-DG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1000
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1001 AGVDPYSR-RGIWELL-LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK11607 178 GALDKKLRdRMQLEVVdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1852-2057 |
1.84e-23 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 101.01 E-value: 1.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYR--RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnrnSILSN---IHEVHQ 1926
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSG-------EVLVDgepVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVV-KEGRSVVLTSHSMEECEALCTRMAIM 2057
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
859-1053 |
2.14e-23 |
|
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: 100.26 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 859 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWF-- 936
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLgl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 937 --YARLKGLSEKHVKAEMEQMALDvglpsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1014
Cdd:cd03298 96 spGLKLTAEDRQAIEVALARVGLA-----GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5734101 1015 LLKYRQGR--TIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
842-1049 |
3.66e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 101.70 E-value: 3.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 842 QNLVKVYRDG----MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNL 915
Cdd:PRK13633 8 KNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQH--NVLFDMLtVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK13633 88 GMVFQNpdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 994 VILDEPTAGVDPYSRR----GIWELLLKYrqGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK13633 166 IIFDEPTAMLDPSGRRevvnTIKELNKKY--GITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
839-1043 |
3.80e-23 |
|
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: 102.82 E-value: 3.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMS 909
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQN-LGVCPQhnvlfD-------MLTVEEHIW-FYARLKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQ 978
Cdd:COG0444 82 KIRGReIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 979 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAI 1043
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAV 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
840-1054 |
4.95e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 100.62 E-value: 4.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS----EMSTIRqnl 915
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQHNVL-FDmLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSKT-SQLSGG-MQRklsVALAFV---- 988
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDL--AHLAGRDyPQLSGGeQQR---VQLARVlaql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 989 ----GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
839-1050 |
5.58e-23 |
|
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: 99.49 E-value: 5.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTV-----------EEHIWfyarlKGLSEKHVKAEMEQMA--LDvglpsSKLKSKTSQLSGGmQRKL-SV 983
Cdd:cd03244 83 IPQDPVLFSG-TIrsnldpfgeysDEELW-----QALERVGLKEFVESLPggLD-----TVVEEGGENLSVG-QRQLlCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 984 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKLC 1050
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVV 216
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1840-2086 |
5.62e-23 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 102.89 E-value: 5.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1840 QRILDGGGQNDIlEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAG--KSSTFKMLTGDTTVTRGDAFLnrnSI 1917
Cdd:NF000106 3 RKTISNGARNAV-EVRGLVKHFGEVK--AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*---TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1918 LSNIHEVHQNMG-YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTA 1996
Cdd:NF000106 77 CANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFG 2076
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
250
....*....|
gi 5734101 2077 dGYTIVVRIA 2086
Cdd:NF000106 237 -GRTLQIRPA 245
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
856-1056 |
7.50e-23 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 99.46 E-value: 7.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQnlgVCPQHNVLFDMLTVEEHIW 935
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 936 FYAR--LKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWE 1013
Cdd:TIGR01184 77 LAVDrvLPDLSKSERRAIVEEHIALVGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5734101 1014 LLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSL 1056
Cdd:TIGR01184 156 ELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIL 200
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
866-1048 |
9.02e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 99.06 E-value: 9.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE------MSTIRQnlgvcpQHNvLFDMLTVEEHIWF--Y 937
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaerpVSMLFQ------ENN-LFPHLTVAQNIGLglR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 938 ARLKgLSEKHvKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRRGIWEL 1014
Cdd:COG3840 98 PGLK-LTAEQ-RAQVEQALERVGL-AGLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQEMLDL 171
|
170 180 190
....*....|....*....|....*....|....*.
gi 5734101 1015 L--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:COG3840 172 VdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1853-2066 |
1.34e-22 |
|
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: 97.99 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNsilsNIHEVHQNMGYCP 1932
Cdd:cd03235 1 EVEDLT--VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1933 QFDAI--TELLTGREHVE-----FFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:cd03235 75 QRRSIdrDFPISVRDVVLmglygHKGLFRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2006 VFLDEPTTGMDPKARRFLwncaLSVVK----EGRSVVLTSHSMEECEALCTRmAIMVNGRFRCLG 2066
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDI----YELLRelrrEGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
839-1049 |
1.40e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 100.55 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST----- 910
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 --------------------IRQNLGVCPQ--HNVLFDMlTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLPSS 964
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVS----KEEAKKRAAKyielVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 965 KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAI 1043
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*.
gi 5734101 1044 ISHGKL 1049
Cdd:PRK13651 238 FKDGKI 243
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1853-2066 |
2.10e-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: 96.35 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYC 1931
Cdd:cd03214 1 EVENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQfdaitelltgrehveffallrgvpekevgkvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:cd03214 125 TSHLDIAHQIEL----LELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1851-2061 |
2.13e-22 |
|
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: 97.96 E-value: 2.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEV---- 1924
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQfDAITEL---LTGREHVE--FFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:cd03257 81 RKEIQMVFQ-DPMSSLnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQI----LDLLKKlqeelGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1868-2061 |
2.69e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 105.21 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQ-FDAITElLTGREH 1946
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaFSLYGE-LTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1947 VEFFALLRGVPEKEV-GKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2025
Cdd:NF033858 360 LELHARLFHLPAAEIaARVAE-MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 5734101 2026 --CALSvVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2061
Cdd:NF033858 439 llIELS-REDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
851-1055 |
2.94e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 98.31 E-value: 2.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPPTSGTAYIL--GKDI---RSEMSTIRQNLGVCPQHN 922
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPEVTITGSIVynGHNIyspRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 923 VLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMAL-------DVglpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:PRK14239 96 NPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLkgasiwdEV---KDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1055
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
849-1073 |
3.28e-22 |
|
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: 97.61 E-value: 3.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDM 927
Cdd:cd03249 13 RPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 928 lTVEEHIwFYARLKGLSEKHVKAEMEQMALD--VGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1002
Cdd:cd03249 92 -TIAENI-RYGKPDATDEEVEEAAKKANIHDfiMSLPdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1003 VDPYSRRGIWELLLKYRQGRTIILSTHHMdeADVLG-DRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLVKK 1073
Cdd:cd03249 170 LDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRNaDLIAVLQNGQVVEQGTHDELMAQ--KGVYAKLVKA 237
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
821-1054 |
4.33e-22 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.32 E-value: 4.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 821 KRISEIcMEEEP-----------THLKLGVSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL 889
Cdd:COG1132 312 ERIFEL-LDEPPeipdppgavplPPVRGEIEFENVSFSYPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRF 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 890 FPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwFYARlKGLSEKHVKAEMEQMALD---VGLPS-- 963
Cdd:COG1132 390 YDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFSG-TIRENI-RYGR-PDATDEEVEEAAKAAQAHefiEALPDgy 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 964 -SKLKSKTSQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH------HMdead 1035
Cdd:COG1132 467 dTVVGERGVNLSGG-QRqRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA---- 541
|
250
....*....|....*....
gi 5734101 1036 vlgDRIAIISHGKLCCVGS 1054
Cdd:COG1132 542 ---DRILVLDDGRIVEQGT 557
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1852-2075 |
4.50e-22 |
|
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: 97.31 E-value: 4.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS------NIHEVH 1925
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:cd03300 79 QNYALFPH-------LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRF 2075
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1851-2057 |
5.45e-22 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 97.85 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlsniHEVHQNM 1928
Cdd:COG1116 7 ALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAiteLL---TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:COG1116 83 GVVFQEPA---LLpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIM 2057
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
850-1047 |
5.91e-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: 96.91 E-value: 5.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 850 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 928
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIwFYARLKGLSEKHVKAEMEQMALDVG--LPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1003
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEAAKEAGAHDFImkLPNgydTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNI 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 1004 DPYSRRGIWELLLKYRQGRTIILSTHHM------DEADVLgDRIAIISHG 1047
Cdd:cd03254 171 DTETEKLIQEALEKLMKGRTSIIIAHRLstiknaDKILVL-DDGKIIEEG 219
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
839-1049 |
1.04e-21 |
|
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: 94.30 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 918
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMlTVEEhiwfyarlkglsekhvkaemeqmalDVGLpssklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03247 81 NQRPYLFDT-TLRN-------------------------NLGR----------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLgDRIAIISHGKL 1049
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
840-1045 |
1.05e-21 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 96.85 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTiRqnlGV 917
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVP----KAERRARAEEllalVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIIS 1045
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
855-1049 |
1.34e-21 |
|
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: 95.90 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGKD-----IRS-EMSTIRQNlgvcPQhNVL 924
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPllplsIRGrHIATIMQN----PR-TAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 925 FDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1002
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 5734101 1003 VDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
842-1054 |
1.46e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 842 QNLVKVYRdGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCP 919
Cdd:PRK10895 7 KNLAKAYK-GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 920 QHNVLFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHI--EHLRDSMGQsLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1852-2061 |
1.54e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 96.56 E-value: 1.54e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVG----------------------IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGD 1909
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGkskeeilkktgqtvgvndvsldVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1910 AFLNRNSILS------------NIHEVHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKY 1977
Cdd:cd03294 81 VLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1978 GEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAI 2056
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
....*
gi 5734101 2057 MVNGR 2061
Cdd:cd03294 234 MKDGR 238
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1852-2080 |
3.26e-21 |
|
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: 95.26 E-value: 3.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYR--RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnrnSILSNIHEVHQ--- 1926
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSG-------EVTFDGRPVTRrrr 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 -----NMGYCPQfDAITEL---LTGREHVEFFALLRGVPEKEVgKVGEwAIRKLGLvkyGEKYAGNY----SGGNKRKLS 1994
Cdd:COG1124 75 kafrrRVQMVFQ-DPYASLhprHTVDRILAEPLRIHGLPDREE-RIAE-LLEQVGL---PPSFLDRYphqlSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKE--GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLK 2072
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILN-LLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLL 227
|
....*...
gi 5734101 2073 NRFGDGYT 2080
Cdd:COG1124 228 AGPKHPYT 235
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1852-2066 |
3.36e-21 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 94.24 E-value: 3.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS------NIHEVH 1925
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:cd03301 79 QNYALYPH-------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1855-2061 |
3.84e-21 |
|
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: 93.38 E-value: 3.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1855 KELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTV--TRGDAFLN-RNSILSNIHEVhqnMGYC 1931
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgRPLDKRSFRKI---IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHS-MEECEALCTRMAIMVNGR 2061
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGR 189
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
828-1054 |
5.50e-21 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 97.33 E-value: 5.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 828 MEEEPTHLKLGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSE 907
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 MSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAE-MEQMALdVGLpSSKLKSKTSQLSGGMQRKLSVALA 986
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRvMEALRM-VQL-EEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 987 FVGGSKVVILDEPTAGVDpYSRRGIWELLLKYRQ---GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK09452 159 VVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1852-2071 |
6.85e-21 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 93.90 E-value: 6.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL--VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
845-1030 |
7.87e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 7.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 845 VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNV 923
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 924 LFDMlTVEEHIWFyARlKGLSEkhvkAEMEQMALDVGLP----------SSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:TIGR02868 420 LFDT-TVRENLRL-AR-PDATD----EELWAALERVGLAdwlralpdglDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHH 1030
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
839-1070 |
8.26e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 8.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRdGMKVAVDGLalNFYEGQIT--SFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNL 915
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNI--NFIAPRNSriAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQH--NVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpsSKLKSKTSQ-LSGGMQRKLSVALAFVGGSK 992
Cdd:PRK13652 81 GLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHhLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS--SLFLKNQLGTGYYL 1068
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHL 237
|
..
gi 5734101 1069 TL 1070
Cdd:PRK13652 238 DL 239
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
861-1054 |
8.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 95.19 E-value: 8.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 861 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-----YILGKDIRSEMSTIRQNLGVCPQ--HNVLFDMlTVEEH 933
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 934 IWFYARLKGLSekhvKAEMEQMALD----VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1009
Cdd:PRK13643 106 VAFGPQNFGIP----KEKAEKIAAEklemVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 1010 GIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13643 182 EMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
854-1034 |
1.11e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.91 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 854 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDirsemstirqNLGVCPQHNVLFDML--TVE 931
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 932 E--------HIWFYARLKGLSEKHVKAEMEQMALDvGLpsskLKSKTSQLSGG-MQRKLsVALAFVGGSKVVILDEPTAG 1002
Cdd:NF040873 76 DlvamgrwaRRGLWRRLTRDDRAAVDDALERVGLA-DL----AGRQLGELSGGqRQRAL-LAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 5734101 1003 VDPYSRRGIWELLLKY-RQGRTIILSTHHMDEA 1034
Cdd:NF040873 150 LDAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
839-1053 |
1.38e-20 |
|
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: 97.95 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL-----------GKDI 904
Cdd:TIGR03269 280 IKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtkpGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 905 RSE----MSTIRQNLGVCPQHNVLfDMLTVEEHIWF---YARLK--------GLSEKHVKAEMEQMaldvglpssklksk 969
Cdd:TIGR03269 360 RGRakryIGILHQEYDLYPHRTVL-DNLTEAIGLELpdeLARMKavitlkmvGFDEEKAEEILDKY-------------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 970 TSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:TIGR03269 425 PDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDG 504
|
....*.
gi 5734101 1048 KLCCVG 1053
Cdd:TIGR03269 505 KIVKIG 510
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1876-2042 |
1.66e-20 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 92.33 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNrnSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFAL 1952
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFN--GQPRKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1953 LR-------GVPEKEVGKVGewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPkarrFLwn 2025
Cdd:cd03234 108 LRlprkssdAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FT-- 178
|
170 180
....*....|....*....|....
gi 5734101 2026 cALSVV-------KEGRSVVLTSH 2042
Cdd:cd03234 179 -ALNLVstlsqlaRRNRIVILTIH 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
849-1049 |
2.03e-20 |
|
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: 92.21 E-value: 2.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsemSTIRQNLGVCPqhnvlfdML 928
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----SLLGLGGGFNP-------EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSkLKSKTSQLSGGMQRKL--SVALAFvgGSKVVILDEPTAGVDPY 1006
Cdd:cd03220 100 TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDF-IDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5734101 1007 SRRGIWELLL-KYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03220 177 FQEKCQRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1853-2060 |
2.47e-20 |
|
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: 91.16 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-----LSNIHEVHQN 1927
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYcpQFdaitelltGREHVeFFALLRGVPEK-EVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:cd03226 80 VDY--QL--------FTDSV-REELLLGLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2060
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1833-2062 |
2.67e-20 |
|
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: 97.18 E-value: 2.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1833 EDVRRERQRILdgggQNDILEIKELTKIY---RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGD 1909
Cdd:TIGR03269 265 SEVEKECEVEV----GEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1910 ---------------AFLNRNSILSNIHEVHQNMGYCPQFDaITELLTGREHVEF---FALLRGVPE-KEVGKVGEWAIR 1970
Cdd:TIGR03269 341 vnvrvgdewvdmtkpGPDGRGRAKRYIGILHQEYDLYPHRT-VLDNLTEAIGLELpdeLARMKAVITlKMVGFDEEKAEE 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1971 KLglvkygEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEA 2049
Cdd:TIGR03269 420 IL------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLD 493
|
250
....*....|...
gi 5734101 2050 LCTRMAIMVNGRF 2062
Cdd:TIGR03269 494 VCDRAALMRDGKI 506
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1852-2061 |
3.00e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 92.25 E-value: 3.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHE-------- 1923
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 ---VHQNMGYCPQFDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:cd03256 80 igmIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARR-----FLWNCAlsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRqvmdlLKRINR----EEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
849-1048 |
3.97e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 3.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFD 926
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 927 MLTVEE------HIWFYAR-LKGL--SEKHVKAEMEQMA-----LD-VGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGS 991
Cdd:PRK11300 94 EMTVIEnllvaqHQQLKTGlFSGLlkTPAFRRAESEALDraatwLErVGLLEHANRQ-AGNLAYGQQRRLEIARCMVTQP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK11300 173 EILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1851-2061 |
4.01e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 91.63 E-value: 4.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSN--IHE-VHQN 1927
Cdd:COG1137 3 TLEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2007
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2008 LDEPTTGMDPKAR-------RFLwncalsvvKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG1137 160 LDEPFAGVDPIAVadiqkiiRHL--------KErGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1852-2062 |
4.14e-20 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 90.65 E-value: 4.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQ----FDAitellTGREHVEFFALLRGVPEKEvGKVGEWaIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:COG4619 79 VPQepalWGG-----TVRDNLPFPFQLRERKFDR-ERALEL-LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
855-1054 |
4.56e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.76 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA----YILGKDIRS--EMSTIRQNLGVC---PQHNVLF 925
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 DmlTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 1006 YSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13645 184 KGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
852-1037 |
8.32e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.93 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 852 MKVAVDGLA-----------LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTIRQNLGv 917
Cdd:PRK13539 1 MMLEGEDLAcvrggrvlfsgLSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 cpQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDvglPSSKLKSKTsqLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:PRK13539 80 --HRNAMKPALTVAENLEFWAAFLGGEELDIAAALEAVGLA---PLAHLPFGY--LSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHH---MDEADVL 1037
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAHLaQGGIVIAATHIplgLPGAREL 196
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
855-1049 |
8.63e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 95.47 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCP---QHNVLFDMLT 929
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 930 VEEHIWF-----YARLKGLSEKHVKAEMEQM--ALDVGLPSskLKSKTSQLSGGMQRKlsVALA--FVGGSKVVILDEPT 1000
Cdd:COG1129 347 IRENITLasldrLSRGGLLDRRRERALAEEYikRLRIKTPS--PEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1001 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1049
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
839-1049 |
8.73e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 8.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRsemstirqnLGVC 918
Cdd:COG0488 316 LELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETVK---------IGYF 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDM-LTVEEHIWFYARlkGLSEKHVKAEMEQMaldvGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:COG0488 384 DQHQEELDPdKTVLDELRDGAP--GGTEQEVRGYLGRF----LFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYrQGrTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG0488 458 EPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
849-1072 |
1.91e-19 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.17 E-value: 1.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIR-QNLGVCPQHNV 923
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 924 LFDMLTVEEHIWFYARLKGLSekhvKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 999
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGIN----AEERREKALDalrqVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1000 TAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVK 1072
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1876-2073 |
2.28e-19 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 89.48 E-value: 2.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNI----HEVHQNMGYCPQFDAITELLTGREHVEFFa 1951
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMGMLFQSGALFDSLTVFENVAFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1952 lLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2028
Cdd:cd03261 102 -LRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 2029 SVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:cd03261 181 SLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1843-2066 |
3.00e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 88.74 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1843 LDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDafLNRNSILSNIH 1922
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGT--VTVRGRVSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 EVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2002
Cdd:cd03220 90 GL--GGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2003 PPVVFLDEPTTGMDP----KARRFLwncaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:cd03220 161 PDILLIDEVLAVGDAafqeKCQRRL----RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
849-1030 |
3.02e-19 |
|
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: 88.18 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 928
Cdd:TIGR01189 10 RGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFYARLKGLSEKHVKAEMEQMALD--VGLPSsklksktSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1006
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAVGLTgfEDLPA-------AQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*
gi 5734101 1007 SRRGIWELLLKY-RQGRTIILSTHH 1030
Cdd:TIGR01189 162 GVALLAGLLRAHlARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
839-1054 |
3.03e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 90.24 E-value: 3.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS---GTAYILGKDIRSE-MSTIRQN 914
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 994 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGS 226
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
840-1054 |
3.13e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 89.41 E-value: 3.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC- 918
Cdd:COG4674 12 YVEDLTVSF-DGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 ----PqhNVlFDMLTVEEH----------IW--FYARLKGlsekHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLS 982
Cdd:COG4674 90 kfqkP--TV-FEELTVFENlelalkgdrgVFasLFARLTA----EERDRIEEVLETIGL-TDKADRLAGLLSHGQKQWLE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 983 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:COG4674 162 IGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
839-1049 |
4.08e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 4.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMST 910
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 IRQNlgvcPQHNvlFDMLTVEEHIWFyarlkGLSEKHVkaEMEQM------ALD-VGLpSSKLKSKTSQLSGGmqRKLSV 983
Cdd:PRK13635 86 VFQN----PDNQ--FVGATVQDDVAF-----GLENIGV--PREEMvervdqALRqVGM-EDFLNREPHRLSGG--QKQRV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 984 ALAFVGGS--KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK13635 150 AIAGVLALqpDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
853-1047 |
4.49e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 88.99 E-value: 4.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 853 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCPQHNVLfdmlt 929
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 930 veEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1009
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 5734101 1010 GIWELLLK--YRQGRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:PRK11248 166 QMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1852-2061 |
4.80e-19 |
|
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: 88.03 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIH--EVHQNMG 1929
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDpaDLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQ-----FDAITELLT-GREHVEFFALLRGVpekEVGKVGEWAIR-KLGL-VKYGEKYAGnYSGGNKRKLSTAMALIG 2001
Cdd:cd03245 82 YVPQdvtlfYGTLRDNITlGAPLADDERILRAA---ELAGVTDFVNKhPNGLdLQIGERGRG-LSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2002 GPPVVFLDEPTTGMDPKA-RRFLWNcaLSVVKEGRSVVLTSH--SMEEceaLCTRMAIMVNGR 2061
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
848-1049 |
5.90e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.06 E-value: 5.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 926
Cdd:cd03253 10 YDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 927 MlTVEEHIwFYARLKGLSEKHVKAEMEQMALD--VGLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:cd03253 89 D-TIGYNI-RYGRPDATDEEVIEAAKAAQIHDkiMRFPdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEATS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5734101 1002 GVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:cd03253 167 ALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1849-2061 |
6.45e-19 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 87.79 E-value: 6.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-------LS 1919
Cdd:COG1136 2 SPLLELRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1920 NIHevHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:COG1136 82 RLR--RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSmEECEALCTRMAIMVNGR 2061
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
839-1054 |
7.25e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 89.91 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMK---VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI----LGKDIRSEMSTI 911
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 912 -------------RQNLGVC---PQHNVLFDmlTVEEHIWFYARLKGLS--EKHVKAE--MEQMaldvGLPSSKLKSKTS 971
Cdd:PRK13631 102 npyskkiknfkelRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKksEAKKLAKfyLNKM----GLDDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 972 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKLC 1050
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....
gi 5734101 1051 CVGS 1054
Cdd:PRK13631 256 KTGT 259
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
839-1053 |
7.57e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 7.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG-- 916
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFDMLTVEEHIwFYARLK-----GL-----SEKHVKAEMeqMALDVGLPSSkLKSKTSQLSGGMQRKLSVALA 986
Cdd:PRK09700 84 IIYQELSVIDELTVLENL-YIGRHLtkkvcGVniidwREMRVRAAM--MLLRVGLKVD-LDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 987 FVGGSKVVILDEPTAGVdpySRRGIWELLLKYRQ----GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1849-2061 |
7.66e-19 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 88.22 E-value: 7.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFlnrnSIL------SNIH 1922
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFgerrggEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 EVHQNMGYC-PQF-DAITELLTGREHVE--FFA---LLRGVPEKEVGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLST 1995
Cdd:COG1119 75 ELRKRIGLVsPALqLRFPRDETVLDVVLsgFFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVV-----KEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELL----LALLdklaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1851-2073 |
8.48e-19 |
|
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: 87.73 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL----SNIHEVHQ 1926
Cdd:COG1127 5 MIEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQ----FDAitelLTGREHVEFFalLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:COG1127 83 RIGMLFQggalFDS----LTVFENVAFP--LRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
839-1049 |
8.88e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 89.02 E-value: 8.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNL-VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMS 909
Cdd:PRK13650 5 IEVKNLtFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQNlgvcPQHNvlFDMLTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLPSSKLKsKTSQLSGGMQRKLSVALAFV 988
Cdd:PRK13650 85 MVFQN----PDNQ--FVGATVEDDVAFGLENKGIPHEEMKERVNE-ALElVGMQDFKER-EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1852-2063 |
8.93e-19 |
|
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: 87.49 E-value: 8.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHE-VHQNMG 1929
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDAITELLTGREHVEFFALLRGvpekevGKVGEWAIRKLglvkYG---------EKYAGNYSGGNKRKLSTAMALI 2000
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYARR------RAKRKARLERV----YElfprlkerrKQLAGTLSGGEQQMLAIARALM 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2001 GGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2063
Cdd:cd03224 149 SRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
868-1068 |
9.93e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.18 E-value: 9.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 868 ITSFLGHNGAGKTTTMSILTGLFP------PTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 940
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 KGLSEK-HVKAEMEQMALDVGL---PSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLL 1016
Cdd:PRK14246 118 HGIKEKrEIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1017 KYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS--LFL--KNQLGTGYYL 1068
Cdd:PRK14246 198 ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSneIFTspKNELTEKYVI 253
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
857-1030 |
1.04e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 86.78 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 857 DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWF 936
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 937 YARLKGLsekhVKAEMEQMALD-VGL------PssklkskTSQLSGGMQRKlsVALA--FVGGSKVVILDEP-----TAG 1002
Cdd:PRK13538 98 YQRLHGP----GDDEALWEALAqVGLagfedvP-------VRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQG 164
|
170 180
....*....|....*....|....*...
gi 5734101 1003 VDPYSRRgiweLLLKYRQGRTIILSTHH 1030
Cdd:PRK13538 165 VARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
832-1049 |
1.09e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 87.14 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 832 PTHLKLGVSIQNLVKVYRDGMKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMS 909
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQNLGVCPQHNVLFDMlTVEEHIWF------YARLKGLSEK-HVKAEMEQMALDvglPSSKLKSKTSQLSGGMQRKLS 982
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYglqscsFECVKEAAQKaHAHSFISELASG---YDTEVGEKGSQLSGGQKQRVA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 983 VALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKL 1049
Cdd:cd03248 161 IARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
865-1049 |
1.14e-18 |
|
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: 86.97 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 865 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK-----DIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFyaR 939
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 940 LKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LK 1017
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGL-DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqIK 178
|
170 180 190
....*....|....*....|....*....|..
gi 5734101 1018 YRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
841-1054 |
1.29e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 87.76 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsEMSTIRQ---NLGV 917
Cdd:PRK11231 5 TENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSRQlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEE--------HIWFYARLKGLSEKHVKAEMEQMALDvGLPSSKLksktSQLSGGMQRKLSVALAFVG 989
Cdd:PRK11231 81 LPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRIN-HLADRRL----TDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 990 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1851-2107 |
1.38e-18 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 89.77 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIhEVHQ-NMG 1929
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGL-PPEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDAiteL---LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:COG3842 81 MVFQDYA---LfphLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2007 FLDEPTTGMDPKARRflwncalSVVKE--------GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNR 2074
Cdd:COG3842 158 LLDEPLSALDAKLRE-------EMREElrrlqrelGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATR 230
|
250 260 270
....*....|....*....|....*....|....*
gi 5734101 2075 FgdgytivvriagsnpdlkpVQDFFGLA--FPGSV 2107
Cdd:COG3842 231 F-------------------VADFIGEAnlLPGTV 246
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1849-2068 |
1.42e-18 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYR--------------------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRG 1908
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1909 DafLNRNSILSNIHEVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGK----VGEWAirklGLVKYGEKYAGN 1984
Cdd:COG1134 82 R--VEVNGRVSALLEL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeIVEFA----ELGDFIDQPVKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1985 YSGGNKRKL--STAMALigGPPVVFLDEPTTGMDP----KARRFLwncaLSVVKEGRSVVLTSHSMEECEALCTRMAIMV 2058
Cdd:COG1134 147 YSSGMRARLafAVATAV--DPDILLVDEVLAVGDAafqkKCLARI----RELRESGRTVIFVSHSMGAVRRLCDRAIWLE 220
|
250
....*....|
gi 5734101 2059 NGRFRCLGSV 2068
Cdd:COG1134 221 KGRLVMDGDP 230
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1852-2076 |
1.58e-18 |
|
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: 91.75 E-value: 1.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQ----FDA-ITE-LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL---VkyGEkYAGNYSGGNKRKLSTA 1996
Cdd:COG4987 414 VPQrphlFDTtLREnLRLARPDAtdeELWAALERV------GLGDW-LAALpdGLdtwL--GE-GGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFG 2076
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLA-DLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
839-1049 |
1.87e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 1.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 914
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQ-HNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:PRK10908 81 IGMIFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSA-ALDkVGL-LDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
839-1049 |
2.14e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 86.69 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG---KDIRSEMSTIRQNL 915
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQHNVLFDMLTVEEHIWFYA-RLKGLSekhvKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPlRVRGAS----KEEAEKQAREllakVGL-AERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 991 SKVVILDEPTAGVDPYSRRgiwELLLKYR----QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRH---EVLKVMQdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
838-1063 |
2.34e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 89.02 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAgktttmSILTGLFPptsgtAYILGKDIR----------SE 907
Cdd:NF000106 13 AVEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GPDAGrrpwrf*twcAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 MSTIRQNLGVC-PQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSkTSQLSGGMQRKLSVALA 986
Cdd:NF000106 80 RRALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIW-ELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKNQLG 1063
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWdEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
841-1049 |
2.64e-18 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 91.71 E-value: 2.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYRDG-MKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR-Q 913
Cdd:PRK10535 7 LKDIRRSYPSGeEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQLRrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 914 NLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
839-1049 |
3.53e-18 |
|
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: 86.78 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGM-------KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSE 907
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 MSTIRQNLGVCPQ--HNVLFDMLTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVA 984
Cdd:TIGR02769 83 RRAFRRDVQLVFQdsPSAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 985 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
839-1048 |
3.93e-18 |
|
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: 85.75 E-value: 3.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIwFYARLkGLSEKHVKAEMEQ-------MALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:cd03251 81 VSQDVFLFND-TVAENI-AYGRP-GATREEVEEAARAanahefiMELPEGY-DTVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTII-----LSThhMDEAdvlgDRIAIISHGK 1048
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1851-2071 |
5.49e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL-SNIHEVHQNMG 1929
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQF--DAITELlTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2007
Cdd:PRK13652 82 LVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2008 LDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
821-1067 |
5.74e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 90.27 E-value: 5.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 821 KRISEIcMEEEP------THL----KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF 890
Cdd:PRK11160 312 RRINEI-TEQKPevtfptTSTaaadQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAW 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 891 PPTSGTAYILGKDIR--SEmSTIRQNLGVCPQHNVLFDMlTVEEHiwfyarLKGLSEKHVKAEMEQMALDVGLpsSKLKS 968
Cdd:PRK11160 391 DPQQGEILLNGQPIAdySE-AALRQAISVVSQRVHLFSA-TLRDN------LLLAAPNASDEALIEVLQQVGL--EKLLE 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 969 KTS-----------QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH------HM 1031
Cdd:PRK11160 461 DDKglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF 540
|
250 260 270
....*....|....*....|....*....|....*.
gi 5734101 1032 deadvlgDRIAIISHGKLCCVGSSLFLKNQLGtGYY 1067
Cdd:PRK11160 541 -------DRICVMDNGQIIEQGTHQELLAQQG-RYY 568
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
855-1071 |
7.55e-18 |
|
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: 90.18 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEH 933
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 934 IWFYAR--------LKGLSEKHVKAEMEQMALDVGlpsSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:TIGR01193 568 LLLGAKenvsqdeiWAACEIAEIKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDT 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1006 YSRRGIWELLLKYrQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1071
Cdd:TIGR01193 645 ITEKKIVNNLLNL-QDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1852-2061 |
8.11e-18 |
|
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: 83.39 E-value: 8.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---RNSILSNIHEVHQNM 1928
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAITELLTGREHVEFfallrgvpekevgkvgewairklGLvkygekyagnySGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL-----------------------GL-----------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03229 125 DEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
839-1049 |
8.31e-18 |
|
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: 89.78 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIwFYARLKGLSEKHVKAEMEQM-ALDV--GLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGS 991
Cdd:TIGR02203 411 VSQDVVLFND-TIANNI-AYGRTEQADRAEIERALAAAyAQDFvdKLPlglDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKL 1049
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGRI 545
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1848-2061 |
8.38e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.05 E-value: 8.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI---LSNIHEV 1924
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2002
Cdd:PRK13636 81 RESVGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2003 PPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
849-1030 |
9.12e-18 |
|
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: 83.70 E-value: 9.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 928
Cdd:cd03231 10 RDG-RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFYARLkglsekHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR 1008
Cdd:cd03231 89 SVLENLRFWHAD------HSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 5734101 1009 RGIWELLLKY-RQGRTIILSTHH 1030
Cdd:cd03231 162 ARFAEAMAGHcARGGMVVLTTHQ 184
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
858-1029 |
1.03e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.45 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 858 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMSTirQNLGVCPQHNVLFDMLTV 930
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeeaRAKLRA--KHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 931 EEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1010
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGL-GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|.
gi 5734101 1011 IWELL--LKYRQGRTIILSTH 1029
Cdd:PRK10584 185 IADLLfsLNREHGTTLILVTH 205
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1851-2062 |
1.28e-17 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 82.87 E-value: 1.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTkiyrrkRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-LSNIHEVHQN-M 1928
Cdd:cd03215 4 VLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYcpqfdaitelltgrehveffallrgVPE--KEVGKVGEWAIRK-LGLVKYgekyagnYSGGNKRKLSTAMALIGGPPV 2005
Cdd:cd03215 78 AY-------------------------VPEdrKREGLVLDLSVAEnIALSSL-------LSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1852-2061 |
1.82e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 82.05 E-value: 1.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQfDAIteLLTG--REHveffaLLrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03228 81 VPQ-DPF--LFSGtiREN-----IL--------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2009 DEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEaLCTRMAIMVNGR 2061
Cdd:cd03228 121 DEATSALDPETEALILE-ALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
828-1049 |
2.19e-17 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 84.32 E-value: 2.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 828 MEEEPTHLKLGVSIQNLvKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPP--TSGTAYILGK 902
Cdd:COG1117 1 MTAPASTLEPKIEVRNL-NVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 903 DIRS---EMSTIRQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLSEKHVKAEMEQMAL-DVGLP---SSKLKSKTSQLSG 975
Cdd:COG1117 79 DIYDpdvDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLrKAALWdevKDRLKKSALGLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 976 GMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
839-1063 |
2.46e-17 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 85.93 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemSTIrQNLGVC 918
Cdd:PRK11432 7 VVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSI-QQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 P--QHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEM-EQMALdVGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:PRK11432 82 MvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVkEALEL-VDLAGFEDRY-VDQISGGQQQRVALARALILKPKVLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 996 LDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS---------SLFLKNQLG 1063
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMASFMG 238
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
839-1054 |
2.71e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 2.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYR------DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY 898
Cdd:COG1134 5 IEVENVSKSYRlyhepsRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 899 ILGKdirseMSTIrqnLGVcpqhNVLFDM-LTVEEHIWFYARLKGLSEKHVK---------AEMEQmALDvgLPsskLKS 968
Cdd:COG1134 85 VNGR-----VSAL---LEL----GAGFHPeLTGRENIYLNGRLLGLSRKEIDekfdeivefAELGD-FID--QP---VKT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 969 ktsqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY----SRRGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAII 1044
Cdd:COG1134 147 ----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRAIWL 219
|
250
....*....|
gi 5734101 1045 SHGKLCCVGS 1054
Cdd:COG1134 220 EKGRLVMDGD 229
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
839-1049 |
2.72e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 84.37 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLG 916
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-EPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 996 LDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
856-1055 |
4.62e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.04 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLT 929
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 930 VEEHIWFYARLKGLS------EKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLwdEV---KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 1002 GVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1055
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
851-1049 |
4.81e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCPQHNVLFDML 928
Cdd:PRK11288 16 GVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIW---FYARL----KGLSEKHVKAEMEQMALDVGlPSSKLKSktsqLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:PRK11288 95 TVAENLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDID-PDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1002 GVdpySRRGIwELLLKY-----RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK11288 170 SL---SAREI-EQLFRVirelrAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
840-1049 |
4.84e-17 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 80.72 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVC 918
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMlTVEEHIwfyarlkglsekhvkaemeqmaldvglpssklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03246 82 PQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 999 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMdEADVLGDRIAIISHGKL 1049
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1852-2042 |
4.98e-17 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 81.64 E-value: 4.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2042
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
856-1050 |
8.50e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.21 E-value: 8.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstirqnlgVCPQ--------------- 920
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQdglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDMLTVEEHIWFYArLKGLSEK--HVKAEMEQMALD--VGLPSSKLKSKTSQ---LSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK10762 338 RDGLVLGMSVKENMSLTA-LRYFSRAggSLKHADEQQAVSdfIRLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEadVLG--DRIAIISHGKLC 1050
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRIS 474
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
852-1053 |
8.80e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.20 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 852 MKVAVDGLALNFYEGQ---------------ITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDIRSEMST- 910
Cdd:PRK14267 1 MKFAIETVNLRVYYGSnhvikgvdlkipqngVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 --IRQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLS------EKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRK 980
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALwdEV---KDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 981 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
858-1054 |
9.75e-17 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 9.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 858 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----------RSEMSTIRQNlgvcPQHNVLFDm 927
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalRQQVATVFQD----PEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 928 lTVEEHIWFYARLKGLSEKHVKAEMEQmALDVgLPSSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1006
Cdd:PRK13638 94 -DIDSDIAFSLRNLGVPEAEITRRVDE-ALTL-VDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 5734101 1007 SRRGIWELLLK-YRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK13638 171 GRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
848-1068 |
1.22e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 81.38 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 926
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 927 MLTVE-----------EHIWFYARLKGLSE--KHVKAEMEQMALDVGlpssklksktSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:cd03252 90 RSIRDnialadpgmsmERVIEAAKLAGAHDfiSELPEGYDTIVGEQG----------AGLSGGQRQRIAIARALIHNPRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKLCCVGSSLFLKNQLGTGYYL 1068
Cdd:cd03252 160 LIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1852-2068 |
1.43e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 82.40 E-value: 1.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRK---RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS---NIHEVH 1925
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNMG----YcPQFDAITEllTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLV--KYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:PRK13637 83 KKVGlvfqY-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2068
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1852-2069 |
1.47e-16 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 81.74 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:PRK13548 3 LEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI------GGPP 2004
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2005 VVFLDEPTTGMDPK--------ARRFLWNCALSVVkegrsVVLtsHSMEECEALCTRMAIMVNGRFRCLGSVQ 2069
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvlrlARQLAHERGLAVI-----VVL--HDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1879-2069 |
1.71e-16 |
|
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: 81.23 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1879 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPE 1958
Cdd:cd03299 25 GDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1959 KEVG-KVGEWAiRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSV 2037
Cdd:cd03299 104 KEIErKVLEIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVT 182
|
170 180 190
....*....|....*....|....*....|...
gi 5734101 2038 VL-TSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2069
Cdd:cd03299 183 VLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
863-1054 |
1.78e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 85.48 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 863 FYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEMstIRQNLGVCPQHNVLFDMLTVEEHIWFYAR 939
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 940 LK---GLSEKHVKAEMEQMALDVGLPSSKlKSKTSQ------LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1010
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLRKCA-NTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 1011 IWELLLKYRQGRTIILSTHHMDEADV--LGDRIAIISHGKLCCVGS 1054
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
855-1049 |
2.06e-16 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 80.69 E-value: 2.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNLGVCPQHNVLFDMLTVEE 932
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 933 HI---WFYARlkglsekhvKAEMEQMALDVGLPSSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:PRK11614 100 NLamgGFFAE---------RDQFQERIKWVYELFPRLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5734101 1006 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK11614 171 IIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1851-2075 |
2.26e-16 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSiLSNIHEVHQNMGY 1930
Cdd:PRK11607 19 LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVEFFALLRGVPEKEV-GKVGEwairKLGLV---KYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIaSRVNE----MLGLVhmqEFAKRKPHQLSGGQRQRVALARSLAKRPKLL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 2007 FLDEPTTGMDPKARRFLwncALSVV----KEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS----VQHLKNRF 2075
Cdd:PRK11607 172 LLDEPMGALDKKLRDRM---QLEVVdileRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRY 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1824-2082 |
2.31e-16 |
|
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: 85.27 E-value: 2.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1824 KLSPLNDEDEDVRRERQRILDGGGQNDIlEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDT 1903
Cdd:COG2274 447 RLDDILDLPPEREEGRSKLSLPRLKGDI-ELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1904 TVTRGDAFLNRNSILS-NIHEVHQNMGYCPQfDaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGLVKY--- 1977
Cdd:COG2274 526 EPTSGRILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEI----IEAARLAGLHDFiea 596
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1978 ---------GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMeECE 2048
Cdd:COG2274 597 lpmgydtvvGEG-GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE-NLRRLLKGRTVIIIAHRL-STI 673
|
250 260 270
....*....|....*....|....*....|....
gi 5734101 2049 ALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIV 2082
Cdd:COG2274 674 RLADRIIVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
851-1048 |
2.46e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 84.67 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---------SEMSTIRQNLGVCPQh 921
Cdd:PRK10762 16 GVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeAGIGIIHQELNLIPQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 922 nvlfdmLTVEEHIW----FYARLKGLSEKHVKAEMEQMALDVGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:PRK10762 94 ------LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 998 EPT-AGVDPYSR---RGIWELllkYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK10762 167 EPTdALTDTETEslfRVIREL---KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
856-1050 |
2.62e-16 |
|
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: 84.49 E-value: 2.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT-SGTAYILGK--DIRSEMSTIRQNLGVCPQ----HNVLFDMl 928
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFyARLKGLSEK-HVKAEMEQMALDVGLpsSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEPT 1000
Cdd:TIGR02633 355 GVGKNITL-SVLKSFCFKmRIDAAAELQIIGSAI--QRLKVKTAspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 1001 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLC 1050
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
843-1038 |
2.94e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.24 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 843 NLVKVYRDGmKVAVDGL---ALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIR-----QN 914
Cdd:PRK11629 10 NLCKRYQEG-SVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQ-HNVLFDmLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK11629 89 LGFIYQfHHLLPD-FTALENVAMPLLIGKKKPAEINSRALEMLAAVGL-EHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 994 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLG 1038
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1851-2045 |
3.66e-16 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 79.71 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkPAVDRICVGIPPGE-CFgLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-RNsiLSNI--HEVH- 1925
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNgQD--LSRLkrREIPy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 --QNMGYCPQ-FdaitELLTGR---EHVEFFALLRGVPEKEVGK-VGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:COG2884 77 lrRRIGVVFQdF----RLLPDRtvyENVALPLRVTGKSRKEIRRrVRE-VLDLVGLSDKAKALPHELSGGEQQRVAIARA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2045
Cdd:COG2884 152 LVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1851-2061 |
4.69e-16 |
|
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: 79.64 E-value: 4.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHE-VHQNM 1928
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRiARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAITELLTGREHVEFFALLRGVPEKevgkvGEWAIRKLG-----LVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAE-----VRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG0410 156 KLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
839-1049 |
5.57e-16 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 79.40 E-value: 5.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 912
Cdd:COG4181 9 IELRGLTKTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 -QNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEqmaLD-VGLpSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL---LErVGL-GHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDEADVL-GDRIAIISHGKL 1049
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1851-2061 |
5.82e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 80.51 E-value: 5.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI---LSNIHEVHQN 1927
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYCPQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:PRK13639 80 VGIVFQ-NPDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
842-1042 |
6.65e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.21 E-value: 6.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 842 QNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSI---LTGLFPP--TSGTAYILGKDI---RSEMSTIRQ 913
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 914 NLGVCPQHNVLFDMlTVEEHIWFYARL---KGLSEKHVKAEMEQMAL--DVglpSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELVERSLRQAALwdEV---KDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIA 1042
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1851-2061 |
7.36e-16 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 79.02 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYR-----RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNI---- 1921
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1922 -HEVH----QNMGYCPQFdaiteL-----LTGREHVEFFALLRGVPEKE-VGKVGEWaIRKLGLvkyGEK----YAGNYS 1986
Cdd:COG4778 84 pREILalrrRTIGYVSQF-----LrviprVSALDVVAEPLLERGVDREEaRARAREL-LARLNL---PERlwdlPPATFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1987 GGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRflwncalsVVKE--------GRSVVLTSHSMEECEALCTRMAIMV 2058
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA--------VVVElieeakarGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 5734101 2059 NGR 2061
Cdd:COG4778 227 PFS 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1852-2061 |
7.70e-16 |
|
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: 77.08 E-value: 7.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnrnSILSNIHEVHqnmgyc 1931
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG-------EILVDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 pqFDAITElltgrehveffALLRGVpekevgkvgeWAIRKLglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03216 66 --FASPRD-----------ARRAGI----------AMVYQL-------------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1852-2067 |
8.01e-16 |
|
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: 79.31 E-value: 8.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIHEVHQNMGYC 1931
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGV----PEKEV-GKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIrAKVHE-LLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2067
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1849-2074 |
9.04e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 79.78 E-value: 9.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA-FLNRNSILSNIHEVHQN 1927
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVkVMGREVNAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:PRK13647 81 VGLVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR 2074
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1852-2061 |
1.01e-15 |
|
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: 78.22 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSiLSNIHE-----VHQ 1926
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGraipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
839-1049 |
1.25e-15 |
|
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: 79.10 E-value: 1.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-YILGKDIRSEMSTI------ 911
Cdd:TIGR02323 4 LQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 912 ---RQNLGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKH---VKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVAL 985
Cdd:TIGR02323 82 rlmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHygnIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 986 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
839-1054 |
1.36e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLG 916
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQH-NVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVI 995
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGS 1054
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1874-2079 |
1.43e-15 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 81.23 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1874 VGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL----SNIHEVH-QNMGYCPQFDAITELLTGREHVE 1948
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1949 FFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2028
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2029 SV-VKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGY 2079
Cdd:PRK10070 209 KLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
839-1054 |
1.65e-15 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 1.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 918
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQHNVLFDMLTVEEHIWF----YARLKGLSEKHVKAEMEQMALDVGLpsSKLKSK-TSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQL--AHLADRyPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 994 VILDEPTAGVDPYSRRGIWELL------LKYrqgrTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
840-1049 |
2.12e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.61 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVkVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---------RSEMST 910
Cdd:COG3845 259 EVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 I---RQNLGVCPqhnvlfDMlTVEEHIWF-------YARLKGLSEKHVKAEMEQM--ALDVGLPSskLKSKTSQLSGGMQ 978
Cdd:COG3845 338 IpedRLGRGLVP------DM-SVAENLILgryrrppFSRGGFLDRKAIRAFAEELieEFDVRTPG--PDTPARSLSGGNQ 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 979 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG3845 409 QKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
839-1049 |
2.40e-15 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 77.87 E-value: 2.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI------LGKDIRSEMSTIR 912
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 913 ---QNLGVCPQHNVLFDMLTVEEHIwfyarLKG--LSEKHVKAEMEQMALD----VGLpSSKLKSKTSQLSGGMQRKLSV 983
Cdd:PRK11264 82 qlrQHVGFVFQNFNLFPHRTVLENI-----IEGpvIVKGEPKEEATARAREllakVGL-AGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 984 ALAFVGGSKVVILDEPTAGVDPysrRGIWELLLKYRQ----GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
838-1057 |
2.50e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 78.20 E-value: 2.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLVkVYRDGmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGK-----DIRSEM 908
Cdd:PRK10418 4 QIELRNIA-LQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 -STIRQNlgvcPQH--NVLFDMLTveehiwfYAR--LKGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGGMQRKL 981
Cdd:PRK10418 81 iATIMQN----PRSafNPLHTMHT-------HARetCLALGKPADDATLTAALEAVGLENAArvLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 982 SVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL--CCVGSSLF 1057
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveQGDVETLF 229
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1876-2042 |
2.52e-15 |
|
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: 76.51 E-value: 2.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTT--VTRGDAFLNRNSILSNIHEVhqnMGYCPQFDAITELLTGREHVEFFALL 1953
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1954 RGVpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCALS 2029
Cdd:cd03232 107 RGL-----------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAynivRFLKKLADS 157
|
170
....*....|...
gi 5734101 2030 vvkeGRSVVLTSH 2042
Cdd:cd03232 158 ----GQAILCTIH 166
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1852-2061 |
3.03e-15 |
|
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: 77.22 E-value: 3.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFL---NRNSILSNIHE 1923
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VHQNMGYCPQ----FDAitellTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGLVKYGEK--YAGNYSGGNKRKLSTA 1996
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEE-LIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
843-1060 |
3.47e-15 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 77.88 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 843 NLVKV----YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 914
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMLTVEEHIWFYARLKG-LSEKHVKAEMeQMALD-VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTqLPAPLLHSTV-MMKLEaVGLRGAA-KLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFLKN 1060
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
841-1049 |
3.60e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.88 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyILGKDIRsemstirqnLGVCPQ 920
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDMLTVEEHIW--------FYARLKGLSEKHVKAEMEQMALD------------------------VGLPSSKLKS 968
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgdaelraLEAELEELEAKLAEPDEDLERLAelqeefealggweaearaeeilsgLGFPEEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 969 KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRgiW--ELLLKYRqGrTIILSTHhmDEA--DVLGDRIAII 1044
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSH--DRYflDRVATRILEL 222
|
....*
gi 5734101 1045 SHGKL 1049
Cdd:COG0488 223 DRGKL 227
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
858-1049 |
4.03e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 4.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 858 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV--CPQHNVLFDMLTVEEHIW 935
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylVPQEPLLFPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 936 FYARLKGLSEKHVKAEMEQMA--LDVGLPSSKLKSKTSQLSGGMqRKLsvalafVGGSKVVILDEPTAGVDPYSR----R 1009
Cdd:PRK15439 109 FGLPKRQASMQKMKQLLAALGcqLDLDSSAGSLEVADRQIVEIL-RGL------MRDSRILILDEPTASLTPAETerlfS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 5734101 1010 GIWELLlkyRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK15439 182 RIRELL---AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
849-1049 |
4.60e-15 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 77.32 E-value: 4.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--------------SEMSTIRQN 914
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMLTVEEHIWFY-ARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENVMEApIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10619 174 LLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1823-2071 |
4.80e-15 |
|
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: 80.96 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1823 AKLSPLNDEDEDVRRERQRILDGGGQNDIlEIKELTKIYRrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGD 1902
Cdd:COG4988 309 EKIFALLDAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1903 TTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQFdaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGL---VK 1976
Cdd:COG4988 387 LPPYSGSILINGVDLSDlDPASWRRQIAWVPQN---PYLFAGtiRENLRLGR--PDASDEEL----EAALEAAGLdefVA 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1977 Y---------GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEEC 2047
Cdd:COG4988 458 AlpdgldtplGEG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ-ALRRLAKGRTVILITHRLALL 535
|
250 260
....*....|....*....|....
gi 5734101 2048 eALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:COG4988 536 -AQADRILVLDDGRIVEQGTHEEL 558
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1851-2067 |
5.34e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.86 E-value: 5.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-LSNIHE-VHQNM 1928
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsLLPLHArARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKV-GEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2007
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2008 LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2067
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1878-2061 |
5.65e-15 |
|
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: 76.18 E-value: 5.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1878 PGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-------RNSILSNIHEVHqnMGYCPQFDAITELLTGREHVEFf 1950
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsRKKINLPPQQRK--IGLVFQQYALFPHLNVRENLAF- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1951 ALLRGVPEKEVGKVGEWAIRkLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSV 2030
Cdd:cd03297 99 GLKRKRNREDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|..
gi 5734101 2031 VKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1852-2062 |
9.36e-15 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 74.27 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQfdaitelltgREHVeFFALLRgvpeKEVGKvgewairklglvkygekyagNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03247 81 NQ----------RPYL-FDTTLR----NNLGR--------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEgRSVVLTSHSMEECEALcTRMAIMVNGRF 2062
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
872-1049 |
1.32e-14 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 75.39 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 872 LGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMSTIRQNLGVCPQHNVLFDMLTVEEHIWF--YARLKgLSEKHvK 949
Cdd:PRK10771 31 LGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRPVSMLFQENNLFSHLTVAQNIGLglNPGLK-LNAAQ-R 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 950 AEMEQMALDVGLpSSKLKSKTSQLSGGmQRKlSVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TII 1025
Cdd:PRK10771 108 EKLHAIARQMGI-EDLLARLPGQLSGG-QRQ-RVALArcLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLL 184
|
170 180
....*....|....*....|....
gi 5734101 1026 LSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10771 185 MVSHSLEDAARIAPRSLVVADGRI 208
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1876-2046 |
1.39e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAiTELL--TGREHVE 1948
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPE-SQLFeeTVLKDVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1949 FFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCA 2027
Cdd:PRK13643 108 FGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF 187
|
170
....*....|....*....
gi 5734101 2028 LSVVKEGRSVVLTSHSMEE 2046
Cdd:PRK13643 188 ESIHQSGQTVVLVTHLMDD 206
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1852-2042 |
1.39e-14 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:cd03231 1 LEADELT--CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 5734101 2012 TTGMDPK-----ARRFLWNCAlsvvkEGRSVVLTSH 2042
Cdd:cd03231 153 TTALDKAgvarfAEAMAGHCA-----RGGMVVLTTH 183
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
841-1049 |
1.65e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKvyRDGMKVAVDGLALNfyEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLGVC 918
Cdd:PRK09700 268 VRNVTS--RDRKKVRDISFSVC--RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 PQH---NVLFDMLTVEEHIWFY-----ARLKG----LSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALA 986
Cdd:PRK09700 344 TESrrdNGFFPNFSIAQNMAISrslkdGGYKGamglFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
839-1053 |
1.80e-14 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 1.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVkVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMS-TIRQNLGV 917
Cdd:PRK09536 4 IDVSDLS-VEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSArAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVL---FDMLTVEE-----HIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSKTSqLSGGMQRKLSVALAFVG 989
Cdd:PRK09536 82 VPQDTSLsfeFDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMER----TGVAQFADRPVTS-LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 990 GSKVVILDEPTAGVDpySRRGIWELLLKYR---QGRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:PRK09536 157 ATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1866-2012 |
1.86e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.57 E-value: 1.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNsilSNIHEVHQNMGYCPQFDAITELLTGRE 1945
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1946 HV-----EFFALLRGVPE-----KEVGKV-------GEWAIR--------KLGL-VKYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:COG0488 88 ELraleaELEELEAKLAEpdedlERLAELqeefealGGWEAEaraeeilsGLGFpEEDLDRPVSELSGGWRRRVALARAL 167
|
170
....*....|...
gi 5734101 2000 IGGPPVVFLDEPT 2012
Cdd:COG0488 168 LSEPDLLLLDEPT 180
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1849-2061 |
2.00e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 75.89 E-value: 2.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYRR----KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNR--NSILSNIH 1922
Cdd:PRK13633 2 NEMIKCKNVSYKYESneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 EVHQNMGYCPQ------FDAITElltgrEHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYgEKYAGNY-SGGNKRKLST 1995
Cdd:PRK13633 82 DIRNKAGMVFQnpdnqiVATIVE-----EDVAFGPENLGIPPEEIRERVDESLKKVGMYEY-RRHAPHLlSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGR 2061
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1868-2073 |
2.06e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------RNSILSNIHEVHQNMGYCPQFDAIT 1938
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1939 ELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2018
Cdd:PRK09700 100 NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2019 ARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
850-1049 |
2.25e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.85 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 850 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 928
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIwfyaRL----KGLSEKHVKAEMEQmALDVGLPSSK-----LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 999
Cdd:PRK13657 424 SIEDNI----RVgrpdATDEEMRAAAERAQ-AHDFIERKPDgydtvVGERGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1000 TAGVDPYSRRGIWELLLKYRQGRT--II---LSThhMDEAdvlgDRIAIISHGKL 1049
Cdd:PRK13657 499 TSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRV 547
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
858-1071 |
2.62e-14 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 78.61 E-value: 2.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 858 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwF 936
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENI-A 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 937 YARLKGLSEKHVKAEMEQMALD--VGLPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGI 1011
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDfiMEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1012 WEllLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1071
Cdd:TIGR00958 657 QE--SRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1851-2061 |
2.85e-14 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 74.74 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS---NIHEVHQN 1927
Cdd:PRK09493 1 MIEFKNVSK--HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYC-PQFDAITELlTGREHVEFFAL-LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:PRK09493 79 AGMVfQQFYLFPHL-TALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
848-1047 |
4.35e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.59 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGVCPQHNVLF 925
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-STLKpeIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 DMlTVEEHIWF--YARLKGLSEKHVKAEMEQMaldvGLPSSKLKSKTSQLSGGMQRKLSVA--LAFVggSKVVILDEPTA 1001
Cdd:PRK10247 94 GD-TVYDNLIFpwQIRNQQPDPAIFLDDLERF----ALPDTILTKNIAELSGGEKQRISLIrnLQFM--PKVLLLDEITS 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5734101 1002 GVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:PRK10247 167 ALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1849-2048 |
4.40e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 74.84 E-value: 4.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--------DTTVTRGDAFLNRNSILsN 1920
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1921 IHE----VHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLS 1994
Cdd:PRK13640 82 IREkvgiVFQN----PdnQFVGATV----GDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKARrflwNCALSVVKE-----GRSVVLTSHSMEECE 2048
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1867-2043 |
5.32e-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: 77.40 E-value: 5.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIH-EVHQNMGYCPQ----FDA-ITE- 1939
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQdahlFDTtVREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1940 LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL-VKYGEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2013
Cdd:TIGR02868 429 LRLARPDAtdeELWAALERV------GLADW-LRALpdGLdTVLGEG-GARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|
gi 5734101 2014 GMDPKARRFLWNcALSVVKEGRSVVLTSHS 2043
Cdd:TIGR02868 501 HLDAETADELLE-DLLAALSGRTVVLITHH 529
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
855-1049 |
6.41e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQH-NVLFDMLTVEE 932
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHIGIVFQNpDNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 933 HIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1012
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|....*....
gi 5734101 1013 ELLLKYRQGR--TIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PRK13648 183 DLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1853-2068 |
6.47e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.61 E-value: 6.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI--LSN--IHEVHQ 1926
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtaLSEkeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQ-FDaiteLLTGREHVEFFAL---LRGVPEKEVGK-VGEWairkLGLVKYGEK---YAGNYSGGNKRKLSTAMA 1998
Cdd:PRK11153 83 QIGMIFQhFN----LLSSRTVFDNVALpleLAGTPKAEIKArVTEL----LELVGLSDKadrYPAQLSGGQKQRVAIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSV 2068
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSI----LELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1851-2061 |
6.56e-14 |
|
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: 75.09 E-value: 6.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNRNSILS----NI 1921
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1922 HEV-HQNMGYCPQfDAITEL---LTGREHV-EFFALLRGVPEKEVGKVgewAIRKLGLVK--YGEKYAGNY----SGGNK 1990
Cdd:COG0444 81 RKIrGREIQMIFQ-DPMTSLnpvMTVGDQIaEPLRIHGGLSKAEARER---AIELLERVGlpDPERRLDRYphelSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1991 RKLSTAMALIGGPPVVFLDEPTTGMDpkarrflwncaLSV-----------VKE-GRSVVLTSHSMEECEALCTRMAIMV 2058
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALD-----------VTIqaqilnllkdlQRElGLAILFITHDLGVVAEIADRVAVMY 225
|
...
gi 5734101 2059 NGR 2061
Cdd:COG0444 226 AGR 228
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
839-1048 |
6.77e-14 |
|
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: 76.79 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDI--RSEMSTIRQN 914
Cdd:TIGR02633 2 LEMKGIVKTF-GGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEM----EQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylraKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1853-2061 |
1.22e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 73.49 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFL--------NRNSILSNIHEV 1924
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskeNLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNmgycP--QFDAITelltgrehVE---FFALL-RGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:PRK13632 89 FQN----PdnQFIGAT--------VEddiAFGLEnKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2061
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGK 219
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
839-1061 |
1.25e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMkvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP----PTSGTAYI---------LGKDIR 905
Cdd:PRK09984 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvqregrLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 906 SEmstiRQNLGVCPQHNVLFDMLTVEEHIW--------FYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGM 977
Cdd:PRK09984 83 KS----RANTGYIFQQFNLVNRLSVLENVLigalgstpFWRTCFSWFTREQKQRALQALTRVGM-VHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 978 QRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSS 1055
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
....*.
gi 5734101 1056 LFLKNQ 1061
Cdd:PRK09984 238 QQFDNE 243
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1852-2042 |
1.29e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIyrRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYC 1931
Cdd:PRK13538 2 LEARNLACE--RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEW-AIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2010
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDEA----LWeALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 5734101 2011 PTTGMDPKA-----RRFLWNCAlsvvkEGRSVVLTSH 2042
Cdd:PRK13538 156 PFTAIDKQGvarleALLAQHAE-----QGGMVILTTH 187
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
838-1042 |
1.59e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 72.76 E-value: 1.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS-----GTAYILGKDI---RSEMS 909
Cdd:PRK14258 7 AIKVNNL-SFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQNLG-VCPQHNvLFDMlTVEEHIWFYARLKGLSEK-HVKAEMEQMALDVGL---PSSKLKSKTSQLSGGMQRKLSVA 984
Cdd:PRK14258 85 RLRRQVSmVHPKPN-LFPM-SVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 985 LAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIA 1042
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1862-2081 |
1.68e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 75.85 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1862 RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-DTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAITEL 1940
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1941 LTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAG------NYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:TIGR00955 114 LTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2012 TTGMDPkarrFLwncALSVVK-------EGRSVVLTSH--SMEECEaLCTRMAIMVNGRFRCLGSVQHLKNRFGD-GYTI 2081
Cdd:TIGR00955 194 TSGLDS----FM---AYSVVQvlkglaqKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1826-2042 |
1.86e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 1.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1826 SPLNDEDEDVRRERQriLDGGGQNDILEIKELT---KIYRRKRK--PAVDRICVgipPGECFGLLGVNGAGKSSTFKMLT 1900
Cdd:TIGR00956 736 TDLTDESDDVNDEKD--MEKESGEDIFHWRNLTyevKIKKEKRVilNNVDGWVK---PGTLTALMGASGAGKTTLLNVLA 810
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1901 GDTT---VTRGDaflnrnsILSNIHEV----HQNMGYCPQFDAITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIR 1970
Cdd:TIGR00956 811 ERVTtgvITGGD-------RLVNGRPLdssfQRSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIK 883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1971 KLGLVKYGEKYAGNYSGG----NKRKLSTAMALIGGPP-VVFLDEPTTGMDPKARrflWN-CAL--SVVKEGRSVVLTSH 2042
Cdd:TIGR00956 884 LLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTA---WSiCKLmrKLADHGQAILCTIH 960
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
854-1054 |
2.50e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 854 VAVDG----LALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIR----SEMSTIRQNLgvCPQHNVLF 925
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaAELARHRAYL--SQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 DMltveeHIWFYARL---KGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGG-MQRklsVALAFV---------GGSK 992
Cdd:PRK03695 83 AM-----PVFQYLTLhqpDKTRTEAVASALNEVAEALGL-DDKLGRSVNQLSGGeWQR---VRLAAVvlqvwpdinPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1851-2061 |
2.94e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTkiyrrkRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-RNSILSNIHE-VHQNM 1928
Cdd:COG1129 256 VLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDgKPVRIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQ-------------FDAITelLTGREHVEFFALLRgvpEKEVGKVGEWAIRKLGlVKYG--EKYAGNYSGGNKRKL 1993
Cdd:COG1129 330 AYVPEdrkgeglvldlsiRENIT--LASLDRLSRGGLLD---RRRERALAEEYIKRLR-IKTPspEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1994 STAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCAlsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKaeiyRLIRELA----AEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1851-2062 |
2.97e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 2.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrkrkPAV---DRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-LSNIHE--- 1923
Cdd:COG1129 4 LLEMRGISKSF-----GGVkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 -----VHQNMGYCPQFDaITE-LLTGREhveffallrgvpekevgkvgewaIRKLGLVKYGEKYA--------------- 1982
Cdd:COG1129 79 agiaiIHQELNLVPNLS-VAEnIFLGRE-----------------------PRRGGLIDWRAMRRrarellarlgldidp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1983 ----GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVK----EGRSVVLTSHSMEECEALCTRM 2054
Cdd:COG1129 135 dtpvGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL----FRIIRrlkaQGVAIIYISHRLDEVFEIADRV 210
|
....*...
gi 5734101 2055 AIMVNGRF 2062
Cdd:COG1129 211 TVLRDGRL 218
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
840-1054 |
3.06e-13 |
|
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: 70.63 E-value: 3.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFP---PTSGTAYILGKDIrSEMST---IRQ 913
Cdd:cd03217 2 EIKDL-HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 914 NLGVCPQHNVLFDMLTVEEHIWFyarlkglsekhvkaemeqmaLDVGLpssklksktsqlSGGMQRKLSVALAFVGGSKV 993
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNADFLRY--------------------VNEGF------------SGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEAD-VLGDRIAIISHGKLCCVGS 1054
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
839-1048 |
3.48e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.75 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQN-INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNV-----LFDMLTVEEHIwfyarlkglSEKHVKAEME--QMALDV-GLPS---SKLKSKTSQLSGGMQRKLSVALA 986
Cdd:PRK10790 420 VQQDPVvladtFLANVTLGRDI---------SEEQVWQALEtvQLAELArSLPDglyTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGK 1048
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTI-VEADTILVLHRGQ 551
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
838-1058 |
3.65e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 73.53 E-value: 3.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 917
Cdd:PRK11000 3 SVTLRNVTKAY-GDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 997
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQL-AHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 998 EPTAGVDPYSR---RgIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSLFL 1058
Cdd:PRK11000 159 EPLSNLDAALRvqmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1868-2024 |
3.76e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTF-------KMLTGDTTVTRGD----AFlnRNSILSNIhevhqnmGYCPQfda 1936
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagarKIQQGRVEVLGGDmadaRH--RRAVCPRI-------AYMPQ--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1937 itEL-------LTGREHVEFFALLRGVPEKEvgkvGEWAIRKL----GLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:NF033858 84 --GLgknlyptLSVFENLDFFGRLFGQDAAE----RRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170
....*....|....*....
gi 5734101 2006 VFLDEPTTGMDPKARRFLW 2024
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFW 176
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1866-2080 |
3.88e-13 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 71.65 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHE---VHQNMGYCPQFDAItellt 1942
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1943 grEHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2022
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2023 LWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRClgsVQHLKNRFGDGYT 2080
Cdd:PRK11248 167 MQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1848-2061 |
4.56e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 71.97 E-value: 4.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNRNS---ILS 1919
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlllpeAGTITVGGMVLSEETvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1920 NIHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 1997
Cdd:PRK13635 82 QVGMVFQN----PdnQFVGATV----QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1998 ALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNGR 2061
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
829-1049 |
4.97e-13 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 74.40 E-value: 4.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 829 EEEPTHL---KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 905
Cdd:COG4618 318 EPERMPLprpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 906 S-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwfyARLKGL-SEKHVKAEmeQMA----LDVGLP---SSKLKSKTSQLSGG 976
Cdd:COG4618 398 QwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDAdPEKVVAAA--KLAgvheMILRLPdgyDTRIGEGGARLSGG 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 977 -MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMdeaDVLG--DRIAIISHGKL 1049
Cdd:COG4618 472 qRQR---IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIraLK-ARGATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
853-1049 |
5.18e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 71.67 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 853 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY-----ILGKDIRS--EMSTIRQNLGVCPQHNVLF 925
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 DMLTVEEHIWFYARLKGLSEKHVKAEMEQMALDVGLPSS---KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1002
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAvkdRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 1003 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1851-2061 |
6.21e-13 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.20 E-value: 6.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMG 1929
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDAITELLTGREHVE--------FFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIG 2001
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAygrspwlsLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2002 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1852-2057 |
6.58e-13 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 71.05 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIY--RRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHE---VHQ 1926
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NmgycpqfDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:COG4525 84 K-------DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIM 2057
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEALFLATRLVVM 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
840-1049 |
6.84e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.26 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDG-------MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEM 908
Cdd:PRK10419 5 NVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 STIRQNL---------GVCPQHnvlfdmlTVEEHIWFYAR-LKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQ 978
Cdd:PRK10419 85 KAFRRDIqmvfqdsisAVNPRK-------TVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 979 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1876-2042 |
9.08e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 9.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTtvtRGDAFlnRNSILSN----IHEVHQNMGYCPQFDAITELLTGREHVEFFA 1951
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRI---QGNNF--TGTILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCS 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1952 LLR---GVPEKEVGKVGEWAIRKLGLVKYGEKYAGN-----YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2023
Cdd:PLN03211 166 LLRlpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170
....*....|....*....
gi 5734101 2024 WNCALSVVKEGRSVVLTSH 2042
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMH 264
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
842-1048 |
1.07e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 73.04 E-value: 1.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 842 QNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDIR------SE---MST 910
Cdd:PRK13549 9 KNITKTF-GGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQasnirdTEragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 IRQNLGVCPQhnvlfdmLTVEEHI-----WFYARLKGLSEKHVKAE--MEQMALDVglpssKLKSKTSQLSGGMQRKLSV 983
Cdd:PRK13549 87 IHQELALVKE-------LSVLENIflgneITPGGIMDYDAMYLRAQklLAQLKLDI-----NPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 984 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1852-2061 |
1.39e-12 |
|
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: 69.10 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS---NIHEVHQNM 1928
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQ----------FDAITELLTgrehveffaLLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:cd03262 79 GMVFQqfnlfphltvLENITLAPI---------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGR 212
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1869-2060 |
1.51e-12 |
|
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: 69.42 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1869 VDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHE---VHQNMGYCPqfdaiteLLTGRE 1945
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1946 HVEFF--ALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2023
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 5734101 2024 WNCALSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNG 2060
Cdd:TIGR01184 154 QEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1851-2085 |
1.85e-12 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 69.66 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFK----MLTGDTTVTRGDAFLNRN-----SILSNI 1921
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGSHIELLGRTvqregRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1922 HEVHQNMGYCPQFDAITELLTGREHVEFFAL---------LRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRK 1992
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1993 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVK-EGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*
gi 5734101 2072 KN-RFGDGYTIVVRI 2085
Cdd:PRK09984 241 DNeRFDHLYRSINRV 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
856-1049 |
2.24e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYILGK--DIRSEMSTIRQNLGVCP----QHNVLFDMl 928
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIVPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWF--YARLKGLSekHVKAEMEQMALDVGLpsSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEP 999
Cdd:PRK13549 357 GVGKNITLaaLDRFTGGS--RIDDAAELKTILESI--QRLKVKTAspelaiaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1000 TAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1049
Cdd:PRK13549 433 TRGIDVGAKYEIYKLINQLvQQGVAIIVISSELPE--VLGlsDRVLVMHEGKL 483
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1852-2061 |
2.39e-12 |
|
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: 67.24 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNrNSILSNIHEVH--QNMG 1929
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNElgDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQFDaitELLTGrehveffallrgvpekevgkvgewAIrklglvkygekyAGN-YSGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03246 80 YLPQDD---ELFSG------------------------SI------------AENiLSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2061
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1851-2061 |
2.74e-12 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 70.49 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI--LSN--IHEV 1924
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtaLSEreLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQ-FDaiteLLTGR---EHVEfFAL-LRGVPEKEV-GKVGEWairkLGLVKYGEKyAGNY----SGGNKRKLS 1994
Cdd:COG1135 81 RRKIGMIFQhFN----LLSSRtvaENVA-LPLeIAGVPKAEIrKRVAEL----LELVGLSDK-ADAYpsqlSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSI----LDLLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1868-2061 |
4.13e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 68.48 E-value: 4.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI--LSNiHEV--------HQNMGYCPQFDAI 1937
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPG-HQIarmgvvrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1938 TELLTGR-EHVE--FFALLRGVP-----EKE-VGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:PRK11300 99 ENLLVAQhQQLKtgLFSGLLKTPafrraESEaLDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
837-1049 |
4.14e-12 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 68.50 E-value: 4.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMS 909
Cdd:COG4161 1 MSIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 910 TIRQNLGVCPQHNVLFDMLTVEEH-IWFYARLKGLSEKHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFV 988
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRL-TDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1848-2060 |
4.69e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 68.76 E-value: 4.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAflnrnSIL--SNIHEVH 1925
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILgqPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNM-GYCPQ-------FDAITE--LLTGRE-HVeffALLRgVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLS 1994
Cdd:PRK15056 77 KNLvAYVPQseevdwsFPVLVEdvVMMGRYgHM---GWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTrMAIMVNG 2060
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1863-2042 |
4.74e-12 |
|
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: 68.02 E-value: 4.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1863 RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQfDAIteLL 1941
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ-DTF--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1942 TG--REHVEFFALLrgVPEKEVGKVGEWA-----IRKL--GLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2012
Cdd:cd03254 90 SGtiMENIRLGRPN--ATDEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190
....*....|....*....|....*....|
gi 5734101 2013 TGMDPKARRFLWNcALSVVKEGRSVVLTSH 2042
Cdd:cd03254 168 SNIDTETEKLIQE-ALEKLMKGRTSIIIAH 196
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1852-2045 |
4.80e-12 |
|
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: 71.16 E-value: 4.80e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGY 1930
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELlTGREHVEFFAllRGVPEKEVgkvgEWAIRKLGL------------VKYGEKYAGnYSGGNKRKLSTAMA 1998
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEI----REALERAGLdefvaalpqgldTPIGEGGAG-LSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKEGRSVVLTSHSME 2045
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLA 518
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
580-781 |
7.00e-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: 69.34 E-value: 7.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 580 MPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNSILWFSWFISSLIPLLVSAGLLVVILkLGNLLPYSDPSVVF 659
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 660 VFLSVFAVVTILQCFLISTLFSRANLAAACGGIIYFTLYLPYVLcVAWQDYVGFTLKIFASLLSPVAFGFGceyfalFEE 739
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGG-LFPLEDPPSFLQWIFSIIPFFSPIDG------LLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5734101 740 QGIGVQWDNLFespveedgfnltTSVSMMLFDTFLYGVMTWY 781
Cdd:pfam12698 316 LIYGDSLWEIA------------PSLIILLLFAVVLLLLALL 345
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
840-1048 |
7.12e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.03 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKD---------------- 903
Cdd:PRK11701 8 SVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 904 -IRSEMSTIRQN------LGVCPQHNVlfdmltVEehiwfyaRLKGLSEKHVkAEMEQMALD----VGLPSSKLKSKTSQ 972
Cdd:PRK11701 86 lLRTEWGFVHQHprdglrMQVSAGGNI------GE-------RLMAVGARHY-GDIRATAGDwlerVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 973 LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
866-1049 |
1.06e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCPQ---HNVLFDMLTVEEHIWFYARL 940
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADNINISARR 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 KGL--------------SEKHVKAemeqmaLDVGLPSSKlkSKTSQLSGGMQRK--LSVALAfvGGSKVVILDEPTAGVD 1004
Cdd:PRK11288 359 HHLragclinnrweaenADRFIRS------LNIKTPSRE--QLIMNLSGGNQQKaiLGRWLS--EDMKVILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5734101 1005 PYSRRGIWELLLKY-RQGRTIILSTHhmDEADVLG--DRIAIISHGKL 1049
Cdd:PRK11288 429 VGAKHEIYNVIYELaAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1852-2061 |
1.18e-11 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 66.70 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKpavdRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHE------- 1923
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAErpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 ----------VHQNMGycpqfdaitelltgrehvefFAL---LR-GVPEKEvgKVgEWAIRKLGLVKYGEKYAGNYSGGN 1989
Cdd:COG3840 78 qennlfphltVAQNIG--------------------LGLrpgLKlTAEQRA--QV-EQALERVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 1990 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEM----LDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1851-2075 |
1.20e-11 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 68.82 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS------NIHEV 1924
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenrHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2004
Cdd:PRK09452 92 FQSYALFPH-------MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2005 VVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRF 2075
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1847-2059 |
1.23e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 67.47 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1847 GQNDILEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI----LSNIH 1922
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 E----VHQN-----MGYCPQFDaitelltgrehVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKL 1993
Cdd:PRK13648 83 KhigiVFQNpdnqfVGSIVKYD-----------VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1994 STAMALIGGPPVVFLDEPTTGMDPKARRFLWNCaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVN 2059
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1876-2063 |
1.27e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 66.73 E-value: 1.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSiLSNIHEVH------QNMGYCPQFDAITELLTGREHVEF 1949
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1950 FALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2029
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 5734101 2030 VVKE-GRSVVLTSHSmEECEALCTRMAIMVNGRFR 2063
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
851-1054 |
1.30e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 67.32 E-value: 1.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGVCPQHNVLFDMLT 929
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 930 VEE--------HIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKSkTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1001
Cdd:PRK10253 98 VQElvargrypHQPLFTRWRKEDEEAVTKAMQA----TGITHLADQS-VDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1002 GVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK10253 173 WLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
851-1048 |
1.36e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.37 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---------RSEMSTIRQNLGVCPQH 921
Cdd:PRK10982 10 GVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 922 NVLfdmltveEHIWF--YArLKGLSEKH------VKAEMEQMALDVGlPssklKSKTSQLSGGMQRKLSVALAFVGGSKV 993
Cdd:PRK10982 89 SVM-------DNMWLgrYP-TKGMFVDQdkmyrdTKAIFDELDIDID-P----RAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 994 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
848-1047 |
1.41e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG--LFPPTSGTAYILGKDIRSEMSTIrqnlgvcpqhnvlf 925
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 926 dmltveEHIWfyarlkglSEKHVKAEMEQMAlDVGLPSSKL-KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:COG2401 104 ------DAIG--------RKGDFKDAVELLN-AVGLSDAVLwLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 5734101 1005 P-YSRRG--IWELLLKyRQGRTIILSTHHMDEADVLG-DRIAIISHG 1047
Cdd:COG2401 169 RqTAKRVarNLQKLAR-RAGITLVVATHHYDVIDDLQpDLLIFVGYG 214
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
839-1048 |
1.52e-11 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 64.01 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayilgkdirsemstirqnlgvc 918
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI---------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 pqhnvlfdmltveehiwfYARLKGLSEKHVkaemeqmaldvglpssklksktSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:cd03221 57 ------------------VTWGSTVKIGYF----------------------EQLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRqgRTIILSTHhmDEA--DVLGDRIAIISHGK 1048
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1852-2069 |
1.58e-11 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 67.06 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-------LSNIHEV 1924
Cdd:COG4559 2 LEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HqnmgycPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKyagNY---SGGNKRKLSTAMALI- 2000
Cdd:COG4559 80 L------PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGR---SYqtlSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2001 ------GGPPVVFLDEPTTGMDPK--------ARRFlwncalsvVKEGRSVV-------LTSHsmeeceaLCTRMAIMVN 2059
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQL--------ARRGGGVVavlhdlnLAAQ-------YADRILLLHQ 215
|
250
....*....|
gi 5734101 2060 GRFRCLGSVQ 2069
Cdd:COG4559 216 GRLVAQGTPE 225
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
838-1031 |
1.61e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.22 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemsTIRQNL-G 916
Cdd:PRK15056 6 GIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHN-------VLFD---MLTVEEHIWFYARLKGLSEKHVKAEMEQmaldVGLPSSKLKsKTSQLSGGMQRKLSVALA 986
Cdd:PRK15056 82 YVPQSEevdwsfpVLVEdvvMMGRYGHMGWLRRAKKRDRQIVTAALAR----VDMVEFRHR-QIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 987 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHM 1031
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
839-1005 |
1.76e-11 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 66.58 E-value: 1.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG-----------KDIRSe 907
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 mstIRQNLGVCPQHNVLFDMLTVEEH-IWFYARLKGLSEKHVKAEMEQMaldvgLPSSKLKSKTS----QLSGGMQRKLS 982
Cdd:PRK11124 80 ---LRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKL-----LERLRLKPYADrfplHLSGGQQQRVA 151
|
170 180
....*....|....*....|...
gi 5734101 983 VALAFVGGSKVVILDEPTAGVDP 1005
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP 174
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
866-1029 |
1.87e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 65.34 E-value: 1.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSIL-----TGLfppTSGTAYILGKDIRSemsTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL 940
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDK---NFQRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 KGLSekhvkaeMEQmaldvglpssklksktsqlsggmQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-R 1019
Cdd:cd03232 107 RGLS-------VEQ-----------------------RKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLaD 156
|
170
....*....|
gi 5734101 1020 QGRTIILSTH 1029
Cdd:cd03232 157 SGQAILCTIH 166
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1850-2077 |
2.07e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 67.06 E-value: 2.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1850 DILEIKELTKIYRR-KRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFL--------NRNSILSN 1920
Cdd:PRK13650 3 NIIEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdgdllteeNVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1921 IHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMA 1998
Cdd:PRK13650 83 IGMVFQN----PdnQFVGATV----EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1999 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECeALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2077
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1839-2061 |
2.61e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1839 RQRILDGGGQNDILEIKELTkiyRRKRKPAVDrICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--RNS 1916
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT---SRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1917 ILSNIHEVHQNMGYcpqfdaITElltGREHVEFF---------ALLRGVpeKEVGKVGEWAI-------------RKLGL 1974
Cdd:PRK09700 329 PRSPLDAVKKGMAY------ITE---SRRDNGFFpnfsiaqnmAISRSL--KDGGYKGAMGLfhevdeqrtaenqRELLA 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1975 VKYG--EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCT 2052
Cdd:PRK09700 398 LKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
....*....
gi 5734101 2053 RMAIMVNGR 2061
Cdd:PRK09700 478 RIAVFCEGR 486
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1879-2061 |
2.82e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.40 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1879 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--RNSILSNIHEVHQNMGYCPQ---FDAITELLTGRE-------- 1945
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADninisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1946 -HVEFFALLRGVPEKEVGkvgEWAIRKLGlVK--YGEKYAGNYSGGNKRK------LSTAMAliggppVVFLDEPTTGMD 2016
Cdd:PRK11288 359 hHLRAGCLINNRWEAENA---DRFIRSLN-IKtpSREQLIMNLSGGNQQKailgrwLSEDMK------VILLDEPTRGID 428
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5734101 2017 PKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11288 429 VGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGR 473
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1849-2063 |
3.30e-11 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 68.17 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDT-----TVTRGdaflnrnsilsniHE 1923
Cdd:COG0488 313 KKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELepdsgTVKLG-------------ET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VHqnMGYCPQ-FDAITELLTGREHVEffALLRGVPEKEVGKVgewairkLGlvKYG------EKYAGNYSGGNKRKLSTA 1996
Cdd:COG0488 378 VK--IGYFDQhQEELDPDKTVLDELR--DGAPGGTEQEVRGY-------LG--RFLfsgddaFKPVGVLSGGEKARLALA 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLwNCALSVVkEGrSVVLTSHSMEECEALCTRMAIMVNGRFR 2063
Cdd:COG0488 445 KLLLSPPNVLLLDEPTNHLDIETLEAL-EEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1867-2046 |
3.63e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 64.18 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDaflnrnsilsnihevHQNMGYCPQFDAITELL 1941
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlrptSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1942 --TGREHVE--FFA---LLRGvPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2014
Cdd:NF040873 71 plTVRDLVAmgRWArrgLWRR-LTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|..
gi 5734101 2015 MDPKARRFLWNCALSVVKEGRSVVLTSHSMEE 2046
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1867-2131 |
6.01e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 65.39 E-value: 6.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--RNSILSNIHEVHQNMGYCPQfDAITELL--T 1942
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIRKLVGIVFQ-NPETQFVgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1943 GREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2022
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2023 LWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKnrfgdgytivvriagSNPDLKpvqdFFGLA 2102
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL---------------SDVSLQ----TLGLT 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 5734101 2103 FPGSVP----KEKHRNMLQYQLPSSLSSLA----RIF 2131
Cdd:PRK13644 235 PPSLIElaenLKMHGVVIPWENTSSPSSFAeeicRLF 271
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
840-1049 |
7.31e-11 |
|
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: 67.40 E-value: 7.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYR--DGMKVAVDGLALNFYEGQITSFLGHNGAGKT-TTMSILtGLFPP----TSGTAYILGKDI----RSEM 908
Cdd:COG4172 8 SVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 STIRQN------------LgvcpqhNVLFdmlTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGL--PSSKLKSKTSQL 973
Cdd:COG4172 87 RRIRGNriamifqepmtsL------NPLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdPERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 974 SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDEADV--LGDRIAIISHGKL 1049
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH--DLGVVrrFADRVAVMRQGEI 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1866-2061 |
7.36e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 65.24 E-value: 7.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFK-----MLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAiTEL 1940
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnalLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPE-AQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1941 L--TGREHVEFFALLRGVPEKEV-GKVGEWaIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK13641 99 FenTVLKDVEFGPKNFGFSEDEAkEKALKW-LKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5734101 2017 PKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1876-2043 |
7.54e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 64.86 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GDAFLNRNSILS---NIHEVHQNMGYCPQFDAITELLTGREHV 1947
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTllrTFNRLLELNEEARveGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1948 EFFALLRGV--PEKEVGKVGEWAIRKLGL---VKYGEK-YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2021
Cdd:PRK14267 107 AIGVKLNGLvkSKKELDERVEWALKKAALwdeVKDRLNdYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180
....*....|....*....|..
gi 5734101 2022 FLWNCALSvVKEGRSVVLTSHS 2043
Cdd:PRK14267 187 KIEELLFE-LKKEYTIVLVTHS 207
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1851-2061 |
7.73e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.97 E-value: 7.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrkrkPAV---DRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------RNSIL 1918
Cdd:COG3845 5 ALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1919 SNIHEVHQN-MgycpQFDAIT--E-LLTGREHVEFFALLRGVPEKEVGKVGEwairklglvKYG-----EKYAGNYSGGN 1989
Cdd:COG3845 80 LGIGMVHQHfM----LVPNLTvaEnIVLGLEPTKGGRLDRKAARARIRELSE---------RYGldvdpDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1990 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
856-1037 |
1.04e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLalnFYEGQITSFLGHNGAGKTTTMSILTGlfppTSGTAYILGKDI----RSEMSTIRQNLGVCPQHNVLFDMLTVE 931
Cdd:TIGR00956 782 VDGW---VKPGTLTALMGASGAGKTTLLNVLAE----RVTTGVITGGDRlvngRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 932 EHIWFYARLK-----GLSEK--HVKA-----EMEQMAlD--VGLPSSKLKSKtsqlsggmQRK-LSVALAFVGGSKVVI- 995
Cdd:TIGR00956 855 ESLRFSAYLRqpksvSKSEKmeYVEEvikllEMESYA-DavVGVPGEGLNVE--------QRKrLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHH-----MDEADVL 1037
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
832-1049 |
1.18e-10 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.20 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 832 PTHLKlgVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMST 910
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 911 IRQNLGVCPQHNVLFdMLTVEEHIWFYARlkgLSEKHVKAemeqmALDVglpssklKSKTSQLSGGMQRKLSVALAFVGG 990
Cdd:cd03369 80 LRSSLTIIPQDPTLF-SGTIRSNLDPFDE---YSDEEIYG-----ALRV-------SEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKL 1049
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1851-2061 |
1.25e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.34 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKR---KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL--------S 1919
Cdd:COG1101 1 MLELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1920 NIHEVHQN--MGYCPQfdaitelLTGREHV-------EFFALLRGVPEKEVGKVGEW-AIRKLGLvkygEKY----AGNY 1985
Cdd:COG1101 81 YIGRVFQDpmMGTAPS-------MTIEENLalayrrgKRRGLRRGLTKKRRELFRELlATLGLGL----ENRldtkVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1986 SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRsvvLTS----HSMEECEALCTRMAIMVNGR 2061
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1878-2042 |
1.99e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 66.41 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1878 PGECFGLLGVNGAGKSSTFKMLTGDTT--VTRGD----AFLNRNSILSNIHevhqnmGYCPQFDAITELLTGREHVEFFA 1951
Cdd:PLN03140 905 PGVLTALMGVSGAGKTTLMDVLAGRKTggYIEGDirisGFPKKQETFARIS------GYCEQNDIHSPQVTVRESLIYSA 978
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1952 LLRgVPeKEVGK------VGEwAIRKLGLVKYGEKYAG-----NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKAR 2020
Cdd:PLN03140 979 FLR-LP-KEVSKeekmmfVDE-VMELVELDNLKDAIVGlpgvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAA 1055
|
170 180
....*....|....*....|..
gi 5734101 2021 RFLWNCALSVVKEGRSVVLTSH 2042
Cdd:PLN03140 1056 AIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1852-2045 |
2.01e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 64.34 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRK---PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG------------------DTTVTRGDA 1910
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1911 FLNRNSI-------LSNIHEVHQNMGYCPQFdAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL-VKYGEK 1980
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1981 YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2045
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
829-1049 |
2.24e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 65.64 E-value: 2.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 829 EEEPTHLKLGVSI--QNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFPPTSGTAYILGKDIRS 906
Cdd:PRK11174 338 GEKELASNDPVTIeaEDLEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKINGIELRE 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 907 -EMSTIRQNLGVCPQHNVLFDMlTVEEHIwfyarLKG---LSEKHVKAEMEQM-------ALDVGLpSSKLKSKTSQLSG 975
Cdd:PRK11174 416 lDPESWRKHLSWVGQNPQLPHG-TLRDNV-----LLGnpdASDEQLQQALENAwvseflpLLPQGL-DTPIGDQAAGLSV 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 976 GMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADVlgDRIAIISHGKL 1049
Cdd:PRK11174 489 GQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDlAQW--DQIWVMQDGQI 561
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1851-2061 |
2.38e-10 |
|
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: 63.67 E-value: 2.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYR-------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAF--------LNRN 1915
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1916 SILSNIHEVHQNMGYCPqfDAITELLTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKL 1993
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSP--SAVNPRMTVRQIIgEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1994 STAMALIGGPPVVFLDEPTTGMDpkarRFLWNCALSVVKE-----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1867-2061 |
2.39e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.61 E-value: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-----NIHEVHQNMGYCPQFdAITELL 1941
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQF-PESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1942 --TGREHVEFFALLRGVPEKEVGKVgewAIRKLGLVKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2015
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAEAL---AREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 2016 DPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
859-1049 |
3.35e-10 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 859 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC------PQHNVLFDM----- 927
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 928 ---LTVEEHIWFyarlkgLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:PRK15439 362 vcaLTHNRRGFW------IKPARENAVLERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 1005 PYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1852-2043 |
3.56e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 61.81 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIyrRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-RNSILSNIHEV-----H 1925
Cdd:PRK13539 3 LEGEDLACV--RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNmgycpqfdAITELLTGREHVEFFALLRGVPEKEVgkvgEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:PRK13539 81 RN--------AMKPALTVAENLEFWAAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*...
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHS 2043
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1867-2090 |
3.71e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.48 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQFDAITELLTGRE 1945
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1946 HVEFFA---LLRGVPEKEVGK-VGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD-PKAR 2020
Cdd:PRK09536 97 VVEMGRtphRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2021 RFLwNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG------SVQHLKNRFgDGYTIVvriaGSNP 2090
Cdd:PRK09536 177 RTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAF-DARTAV----GTDP 246
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
855-1063 |
3.91e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 65.04 E-value: 3.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEH 933
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 934 IwFYARlkglSEKHVKAEMEQMA-----------LDVGLPSSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1002
Cdd:PRK11176 437 I-AYAR----TEQYSREQIEEAArmayamdfinkMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 1003 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVlGDRIAIISHGKLCCVGSSLFLKNQLG 1063
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
855-1004 |
4.41e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 4.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNLGVCPQHNV--LFDML 928
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHI-----WFYARlkgLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1003
Cdd:PRK15079 116 TIGEIIaeplrTYHPK---LSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
.
gi 5734101 1004 D 1004
Cdd:PRK15079 193 D 193
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
861-1029 |
5.28e-10 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 64.43 E-value: 5.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 861 LNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--------RSEMSTIRQNlgvcpQHnvLFDMLtve 931
Cdd:COG4615 353 LTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreayRQLFSAVFSD-----FH--LFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 932 ehiwfYARLKGLSEKHVKAEMEQMALDvglpsSKLKSK-----TSQLSGGmQRK-LSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:COG4615 422 -----LGLDGEADPARARELLERLELD-----HKVSVEdgrfsTTDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDP 490
|
170 180
....*....|....*....|....*....
gi 5734101 1006 YSRRgiW---ELL--LKyRQGRTIILSTH 1029
Cdd:COG4615 491 EFRR--VfytELLpeLK-ARGKTVIAISH 516
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
830-1049 |
5.34e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 5.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 830 EEPTHLKLG--VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtAYILGkdiRSE 907
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---TAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 MSTIRQNLGVCPQHNVLFDMLTVEEHIwfyarlkGLSEK-HVKAEMEQmALD-VGLpSSKLKSKTSQLSGGMQRKLSVAL 985
Cdd:PRK11247 76 LAEAREDTRLMFQDARLLPWKKVIDNV-------GLGLKgQWRDAALQ-ALAaVGL-ADRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 986 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1856-2061 |
6.73e-10 |
|
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: 60.97 E-value: 6.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1856 ELTKIYRRKRKPAVDRICVgIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-------------------RNS 1916
Cdd:cd03298 2 RLDKIRFSYGEQPMHFDLT-FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaappadrpvsmlfqENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1917 ILSNIhEVHQNMGYCpqfdaitelLTGREHveffalLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTA 1996
Cdd:cd03298 81 LFAHL-TVEQNVGLG---------LSPGLK------LTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
840-1052 |
6.86e-10 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.96 E-value: 6.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 840 SIQNLVKVYRDGMKV--AVDGLALNFYEGQITSFLGHNGAGKT-TTMSILTGLfpPTSGTAYILGkDIR----------- 905
Cdd:PRK15134 7 AIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 906 --------SEMSTIRQNLGVC--PQHNV---LFDMLTVEehiwfyarlKGLSEKHVKAEMEQMALDVGL--PSSKLKSKT 970
Cdd:PRK15134 84 qtlrgvrgNKIAMIFQEPMVSlnPLHTLekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 971 SQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
....
gi 5734101 1049 lcCV 1052
Cdd:PRK15134 235 --CV 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
868-1054 |
6.88e-10 |
|
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: 63.21 E-value: 6.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 868 ITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMSTIRQNLGVCPQHNVLFDMLTVEEHIWF-YARLK 941
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRAR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 942 GLSEKHVKAEMEQMaldVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ- 1020
Cdd:TIGR02142 105 PSERRISFERVIEL---LGI-GHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAe 180
|
170 180 190
....*....|....*....|....*....|....*
gi 5734101 1021 -GRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:TIGR02142 181 fGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGP 215
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1852-2061 |
9.26e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 61.30 E-value: 9.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT-----GDTTVTRGDAFLNRNSILSN----IH 1922
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpEAGTIRVGDITIDTARSLSQqkglIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 EVHQNMGYCPQFDAITELLTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIG 2001
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2002 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
828-1058 |
9.52e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 61.73 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 828 MEEEPTHLKLGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE 907
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVS--FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 908 MS-TIRQNLGVCPQHNVLFDMLTVEEHI------WFYARLKGLSEKHVKAEmEQMALdVGLP--SSKLkskTSQLSGGMQ 978
Cdd:PRK10575 79 SSkAFARKVAYLPQQLPAAEGMTVRELVaigrypWHGALGRFGAADREKVE-EAISL-VGLKplAHRL---VDSLSGGER 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 979 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGSSL 1056
Cdd:PRK10575 154 QRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPA 233
|
..
gi 5734101 1057 FL 1058
Cdd:PRK10575 234 EL 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1872-2071 |
1.08e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 61.96 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1872 ICVGIPPGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFdaiTELLTGREH 1946
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQF---PEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1947 VE----FFALLRGVPEKEVGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2021
Cdd:PRK13634 103 VEkdicFGPMNFGVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2022 FLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:PRK13634 183 EMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
839-1049 |
1.10e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.37 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYR------DGMK------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyil 900
Cdd:PRK13546 5 VNIKNVTKEYRiyrtnkERMKdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 901 gkDIRSEMSTIRQNLGVCPQhnvlfdmLTVEEHIWFYARLKGLSEKHVKAEMEQMaldvgLPSSKLKSKTSQ----LSGG 976
Cdd:PRK13546 82 --DRNGEVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKI-----IEFSELGEFIYQpvkkYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 977 MQRKLSVALAFVGGSKVVILDEP-TAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1876-2129 |
1.26e-09 |
|
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: 62.44 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-------RNSILSNIHE-----VHQNMGYCPQFDAITELLTG 1943
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsRKGIFLPPEKrrigyVFQEARLFPHLSVRGNLRYG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1944 REHVEffALLRGVPEKEVgkvgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR-- 2021
Cdd:TIGR02142 100 MKRAR--PSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYei 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2022 --FLWNCALSVvkeGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR-------FGD-GYTIVVRIAGsnpd 2091
Cdd:TIGR02142 171 lpYLERLHAEF---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASpdlpwlaREDqGSLIEGVVAE---- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 5734101 2092 LKPVQDFFGLAFPGS---VPKEKHR--NMLQYQLPSSLSSLAR 2129
Cdd:TIGR02142 244 HDQHYGLTALRLGGGhlwVPENLGPtgARLRLRVPARDVSLAL 286
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1852-2061 |
1.51e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKiyrrkrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSN----------- 1920
Cdd:PRK10762 258 LKVDNLSG-------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1921 -IHE------------VHQNMGYCpqfdAITEL--LTGRehveffalLRGVPEKEVgkVGEWaIRkLGLVKYG--EKYAG 1983
Cdd:PRK10762 331 yISEdrkrdglvlgmsVKENMSLT----ALRYFsrAGGS--------LKHADEQQA--VSDF-IR-LFNIKTPsmEQAIG 394
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1984 NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK10762 395 LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1866-2081 |
1.73e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 60.83 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT-------GDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAIT 1938
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1939 ELLTGREHVEFFALLRGVPEK-EVGKVGEWAIRKLGLVKygEKY------AGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWK--EVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 2012 TTGMDPKARRFLWNCaLSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL----KNRFGDGYTI 2081
Cdd:PRK14246 181 TSMIDIVNSQAIEKL-ITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
851-1048 |
1.92e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 62.50 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL--G-----KDIR-SE---MSTIRQNLGVCP 919
Cdd:NF040905 13 GVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILfdGevcrfKDIRdSEalgIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 920 QhnvlfdmLTVEEHIWF---YARlKGL---SEKHVKAEmEQMAlDVGL---PSSKLKsktsQLSGGMQRKLSVALAFVGG 990
Cdd:NF040905 92 Y-------LSIAENIFLgneRAK-RGVidwNETNRRAR-ELLA-KVGLdesPDTLVT----DIGVGKQQLVEIAKALSKD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 991 SKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADVLGDRIAIISHGK 1048
Cdd:NF040905 158 VKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1876-2062 |
3.01e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI--LSNIHEVHQNMGYCPQ--------FDA-----ITEL 1940
Cdd:PRK15439 286 VRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnVCAL 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1941 LTGRehVEFFalLRgvPEKEvGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2019
Cdd:PRK15439 366 THNR--RGFW--IK--PARE-NAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5734101 2020 RRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
839-1050 |
3.26e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.91 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQnlgv 917
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRK---- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 cpqhnvLFDmlTVEEHIWFYARLKGLSEKHVKAEmeqmALDVGLPSSKLKSKTS---------QLSGGMQRKLSVALAFV 988
Cdd:PRK10522 398 ------LFS--AVFTDFHLFDQLLGPEGKPANPA----LVEKWLERLKMAHKLEledgrisnlKLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 989 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHmDEADVLGDRIAIISHGKLC 1050
Cdd:PRK10522 466 EERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1865-2061 |
3.26e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.02 E-value: 3.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1865 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNsilsnihevhqnMGYCPQFDAItelLTG- 1943
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWI---QNGt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1944 -REHVEFfallrGVPEKEvgkvgEW---AIRKLGLVK------------YGEKyaG-NYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:cd03250 82 iRENILF-----GKPFDE-----ERyekVIKACALEPdleilpdgdlteIGEK--GiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2007 FLDEPTTGMDPKARRFLW-NCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2061
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1848-2021 |
3.34e-09 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 60.89 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN-----RNSIlsnih 1922
Cdd:PRK11432 3 QKNFVVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1923 evhQNMGYCPQFD--AITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2000
Cdd:PRK11432 76 ---QQRDICMVFQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180
....*....|....*....|.
gi 5734101 2001 GGPPVVFLDEPTTGMDPKARR 2021
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRR 173
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1877-2016 |
3.82e-09 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 59.80 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1877 PPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF------ 1949
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwh 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1950 FALLR-GVPEKEvgKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK10575 115 GALGRfGAADRE--KVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
861-1047 |
3.99e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 62.30 E-value: 3.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 861 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYARL 940
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 KglSEKHVKA---EMEQMALDV--GLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL 1015
Cdd:PLN03232 706 E--SERYWRAidvTALQHDLDLlpGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
170 180 190
....*....|....*....|....*....|...
gi 5734101 1016 LKYR-QGRTIILSTHHMDEADVLgDRIAIISHG 1047
Cdd:PLN03232 784 MKDElKGKTRVLVTNQLHFLPLM-DRIILVSEG 815
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
839-1054 |
4.44e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNL-VKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI--------------LGK 902
Cdd:PRK10261 13 LAVENLnIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrqvieLSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 903 DIRSEMSTIR-QNLGVCPQHNV--LFDMLTVEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSK--LKSKTSQLSGG 976
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 977 MQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADVLGDRIAIISHGKLCCVGS 1054
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1852-2042 |
4.75e-09 |
|
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: 57.07 E-value: 4.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNsilsnihevhQNMGYC 1931
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFdaitelltgrehveffallrgvpekevgkvgewairklglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNcALSvvKEGRSVVLTSH 2042
Cdd:cd03221 98 TNHLDLESIEALEE-ALK--EYPGTVILVSH 125
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1849-2066 |
4.87e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.44 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIYR--RKRKP----------------AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDa 1910
Cdd:PRK13546 2 NVSVNIKNVTKEYRiyRTNKErmkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1911 fLNRNSILSNIhevHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNK 1990
Cdd:PRK13546 81 -VDRNGEVSVI---AISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1991 RKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNCaLSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLG 2066
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGD---QTFAQKC-LDKIYEfkeqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1828-2016 |
5.12e-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: 61.49 E-value: 5.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1828 LNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--- 1901
Cdd:TIGR03719 296 LLSQEFQKRNETAEIYIPPGPrlgDKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGqeq 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1902 -DT-TVTRGDAflnrnsilsniheVHqnMGYCPQFdaiTELLTGREHVeFFALLRGVPEKEVGKVgEWAIRK-LGLVKYG 1978
Cdd:TIGR03719 374 pDSgTIEIGET-------------VK--LAYVDQS---RDALDPNKTV-WEEISGGLDIIKLGKR-EIPSRAyVGRFNFK 433
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5734101 1979 ----EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:TIGR03719 434 gsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1876-2016 |
5.76e-09 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 58.67 E-value: 5.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI--LSNIHEV---HQNMGYCPQFDAITELLTGREHVEFF 1950
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMskLSSAAKAelrNQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1951 ALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK11629 112 LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1851-2061 |
6.20e-09 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 60.99 E-value: 6.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGDAFLNRNSI----LS 1919
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYWSGSPLKASNIrdteRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1920 NIHEVHQNMGYCPQFDAITELLTGREhveffALLRG--VPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTA 1996
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNE-----ITLPGgrMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
861-1004 |
7.07e-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: 58.04 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 861 LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIW 935
Cdd:cd03233 26 FSGVvkPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLD 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 936 FYARLKGlsekhvkaemEQMaldvglpssklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:cd03233 106 FALRCKG----------NEF--------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1852-2075 |
8.24e-09 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 60.59 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGdaflnrnsilsnihEVHQNMG 1929
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSG--------------RIIYHVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQF-------------------------------DAITELLTGREHVEF---FAL------LRGVPE--KEVGKVGEW 1967
Cdd:TIGR03269 65 LCEKCgyverpskvgepcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLqrtFALygddtvLDNVLEalEEIGYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1968 AIRK----LGLVKYGEKY---AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVVL 2039
Cdd:TIGR03269 145 AVGRavdlIEMVQLSHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVL 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 5734101 2040 TSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRF 2075
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1852-2071 |
8.25e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 60.61 E-value: 8.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIHE--VHQNMG 1929
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 YCPQfdaitelltgREHVeFFALLR-----GVPEKEVGKVGEwAIRKLGLVKYGEKYAG----------NYSGGNKRKLS 1994
Cdd:PRK11160 418 VVSQ----------RVHL-FSATLRdnlllAAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE---GRSVVLTSH---SMEECEALCtrmaIMVNGRFRCLGSV 2068
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQI----LELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTH 557
|
...
gi 5734101 2069 QHL 2071
Cdd:PRK11160 558 QEL 560
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
866-1030 |
8.49e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 8.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFyarlkGLSE 945
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENCLY-----DIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 946 KHVKAEMEQMALDVGLpSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTI 1024
Cdd:PRK13540 102 SPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAV 180
|
....*.
gi 5734101 1025 ILSTHH 1030
Cdd:PRK13540 181 LLTSHQ 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1851-2062 |
8.81e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 60.40 E-value: 8.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYrrkrkP---AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGdttVTRGDA----FLN--------RN 1915
Cdd:PRK10762 4 LLQLKGIDKAF-----PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTG---IYTRDAgsilYLGkevtfngpKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1916 SILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFAllrGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLST 1995
Cdd:PRK10762 76 SQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFG---RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
866-1042 |
9.54e-09 |
|
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: 60.60 E-value: 9.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF-DmlTVEEHIWfYARLkGL 943
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRP-DA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 944 SEkhvkAEMEQMA----LD---VGLPSSK--------LKsktsqLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDP 1005
Cdd:COG5265 460 SE----EEVEAAAraaqIHdfiESLPDGYdtrvgergLK-----LSGGeKQR---VAIArtLLKNPPILIFDEATSALDS 527
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 5734101 1006 YSRRGIWELLLKYRQGRT--II---LST-HHMDEADVLGD-RIA 1042
Cdd:COG5265 528 RTERAIQAALREVARGRTtlVIahrLSTiVDADEILVLEAgRIV 571
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1955-2045 |
9.96e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1955 GVPEKEVGKVGEWAIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE 2033
Cdd:PRK13631 146 GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN 225
|
90
....*....|..
gi 5734101 2034 GRSVVLTSHSME 2045
Cdd:PRK13631 226 NKTVFVITHTME 237
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
863-1004 |
1.16e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 863 FYEGQITSFLGHNGAGKTTTMSILTGlfPPTSGtaYILGkDIRSEMSTIRQNL-----GVCPQHNVLFDMLTVEEHIWFY 937
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISGFPKKQETfarisGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 938 ARLK-----GLSEK--HVKAEMEQMALD------VGLPSsklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:PLN03140 978 AFLRlpkevSKEEKmmFVDEVMELVELDnlkdaiVGLPG------VTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1865-2066 |
1.18e-08 |
|
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: 60.15 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1865 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-LSNIHEVHQNMGYCPQfdaitelltg 1943
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsQWDREELGRHIGYLPQ---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1944 reHVEFF--------ALLRGV-PEKevgkVGEWA--------IRKL--GlvkY----GEkyAGNY-SGGNKRKLSTAMAL 1999
Cdd:COG4618 414 --DVELFdgtiaeniARFGDAdPEK----VVAAAklagvhemILRLpdG---YdtriGE--GGARlSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKE-GRSVVLTSHSMeecEAL--CTRMAIMVNGRFRCLG 2066
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKArGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
841-1047 |
1.27e-08 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 57.83 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKVY----RDGMK-VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILgkdIRSEMSTIrqnl 915
Cdd:COG4778 7 VENLSKTFtlhlQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS--IL---VRHDGGWV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 gvcpqhnvlfDMLTVEEHIWFYARlkglseKH--------------VKAE--MEQMALDVGLPSSKLKSKTSQL------ 973
Cdd:COG4778 78 ----------DLAQASPREILALR------RRtigyvsqflrviprVSALdvVAEPLLERGVDREEARARARELlarlnl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 974 ------------SGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDR 1040
Cdd:COG4778 142 perlwdlppatfSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADR 221
|
....*..
gi 5734101 1041 IAIISHG 1047
Cdd:COG4778 222 VVDVTPF 228
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1851-2061 |
1.28e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKiyrrKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL-SNIHEVHQNmg 1929
Cdd:PRK10982 250 ILEVRNLTS----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINH-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1930 ycpQFDAITEL-----LTGREHVEFFALLRGVpEKEVGKVG-----------EWAIRKLGLVKYGEKYA-GNYSGGNKRK 1992
Cdd:PRK10982 324 ---GFALVTEErrstgIYAYLDIGFNSLISNI-RNYKNKVGlldnsrmksdtQWVIDSMRVKTPGHRTQiGSLSGGNQQK 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 1993 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1849-2060 |
1.34e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 58.57 E-value: 1.34e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELtkIYRRKRKPAVDR---ICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEV 1924
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 HQNMGYCPQF-DAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLT-SHSMEECeALCTRMAIMVNG 2060
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAG 216
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1868-2062 |
1.49e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.54 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN---------RNSILSNIHEVHQNMGYCPQFDAIT 1938
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfastTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1939 ELLTGREHVEFFALLRGVPEKEVGKvgewAIRKLGL-------VKYgekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:PRK11288 99 NLYLGQLPHKGGIVNRRLLNYEARE----QLEHLGVdidpdtpLKY-------LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2012 TTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1861-2045 |
1.68e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 58.09 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1861 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--------------RNSILSNIHEVHQ 1926
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgkpldyskrgllalRQQVATVFQDPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCpqfDAITELLtgrehvefFALLR-GVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2005
Cdd:PRK13638 89 QIFYT---DIDSDIA--------FSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 5734101 2006 VFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSME 2045
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1851-2048 |
1.76e-08 |
|
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: 57.10 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYR-RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHE-VHQNM 1928
Cdd:cd03248 11 IVKFQNVTFAYPtRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKyLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GycpqfdaitelLTGREHVEFFALLR-----GVPEKEVGKVGEWA--------IRKLGLVKY---GEKyAGNYSGGNKRK 1992
Cdd:cd03248 91 S-----------LVGQEPVLFARSLQdniayGLQSCSFECVKEAAqkahahsfISELASGYDtevGEK-GSQLSGGQKQR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1993 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLwNCALSVVKEGRSVVLTSHSMEECE 2048
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQV-QQALYDWPERRTVLVIAHRLSTVE 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
861-1048 |
1.79e-08 |
|
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: 56.71 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 861 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKdirsemstirqnLGVCPQHNVLFDMlTVEEHIWFYARL 940
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWIQNG-TIRENILFGKPF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 -KGLSEKHVKA-----EMEQMAL----DVGlpssklkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1010
Cdd:cd03250 93 dEERYEKVIKAcalepDLEILPDgdltEIG-------EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRH 165
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5734101 1011 IWELLL--KYRQGRTIILSTHHMD---EAdvlgDRIAIISHGK 1048
Cdd:cd03250 166 IFENCIlgLLLNNKTRILVTHQLQllpHA----DQIVVLDNGR 204
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1861-2076 |
1.94e-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: 57.50 E-value: 1.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1861 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI-LSNIHEVHQNMGYCPQfdaiTE 1939
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1940 LLTGREHVEFFALLR-GVPEKEVGKVGEWA-----IRKLGL---VKYGEKYAGnYSGGNKRKLSTAMALIGGPPVVFLDE 2010
Cdd:cd03252 86 VLFNRSIRDNIALADpGMSMERVIEAAKLAgahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 2011 PTTGMDPKARRFLWNcALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFG 2076
Cdd:cd03252 165 ATSALDYESEHAIMR-NMHDICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
866-1030 |
2.21e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.51 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDiRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYARL---KG 942
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 943 LSEKHVKAEMEQMALDVGLPSSKL----KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR-RGIWELLLK 1017
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENtiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSL 252
|
170
....*....|...
gi 5734101 1018 YRQGRTIILSTHH 1030
Cdd:PLN03211 253 AQKGKTIVTSMHQ 265
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1827-2061 |
2.24e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 59.48 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1827 PLNDEDEDVRRERQRILDGGGQND-ILEIKELTKIY--------RRKRK-PAVDRICVGIPPGECFGLLGVNGAGKSSTF 1896
Cdd:PRK10261 288 PLISLEHPAKQEPPIEQDTVVDGEpILQVRNLVTRFplrsgllnRVTREvHAVEKVSFDLWPGETLSLVGESGSGKSTTG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1897 KMLTGDTTVTRGDAFLNRNSI----LSNIHEVHQNMGYCPQ------------FDAITELLtgREHveffALLRGvpeKE 1960
Cdd:PRK10261 368 RALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQdpyasldprqtvGDSIMEPL--RVH----GLLPG---KA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1961 VGKVGEWAIRKLGLV-KYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKE-GRSVV 2038
Cdd:PRK10261 439 AAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYL 518
|
250 260
....*....|....*....|...
gi 5734101 2039 LTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK10261 519 FISHDMAVVERISHRVAVMYLGQ 541
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1852-2068 |
2.44e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 56.38 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGDAFLNRNSILS-NIHEvHQNM 1928
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDlPPEE-RARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 G------YCPQFDAITelltgrehVEFFalLRGVPEkevgkvgewairklglvkygekyagNYSGGNKRKLSTAMALIGG 2002
Cdd:cd03217 78 GiflafqYPPEIPGVK--------NADF--LRYVNE-------------------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 2003 PPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEAL-CTRMAIMVNGRFRCLGSV 2068
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
839-1054 |
2.93e-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: 59.57 E-value: 2.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 918
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 pQHNVLFDmltveehiwfyarlKGLSEKHVKAEMEQMAL--DVG-LPS---SKLKSKTSQLSGGMQRKLSVALAFVGGSK 992
Cdd:TIGR00957 716 -RENILFG--------------KALNEKYYQQVLEACALlpDLEiLPSgdrTEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 993 VVILDEPTAGVDPYSRRGIWELLLKYR---QGRTIILSTHHMD---EADVlgdrIAIISHGKLCCVGS 1054
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISylpQVDV----IIVMSGGKISEMGS 844
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1884-2067 |
3.22e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 57.33 E-value: 3.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1884 LLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQ------NMGYC---PQFDAITEllTGREHVEFFALLR 1954
Cdd:PRK13645 42 VIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVfqfPEYQLFQE--TIEKDIAFGPVNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1955 GVPEKEV-GKVGEWairkLGLVKYGEKYAG----NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2029
Cdd:PRK13645 120 GENKQEAyKKVPEL----LKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFER 195
|
170 180 190
....*....|....*....|....*....|....*....
gi 5734101 2030 VVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGS 2067
Cdd:PRK13645 196 LNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
859-1029 |
3.52e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 55.65 E-value: 3.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 859 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGVCPQhnvlfdmLTVEEHI 934
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLGLKLE-------MTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 935 WFYarlkglSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1014
Cdd:PRK13541 92 KFW------SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*.
gi 5734101 1015 L-LKYRQGRTIILSTH 1029
Cdd:PRK13541 166 IvMKANSGGIVLLSSH 181
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1879-2045 |
3.94e-08 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 56.90 E-value: 3.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1879 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNsilsNIHEVHQNMGYCPQFDAIT-ELLTGR-----EHV---EF 1949
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKVADKNQlRLLRTRltmvfQHFnlwSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1950 FALLRGVPEKEVGKVG-------EWAIRKLGLVKYGEKYAGNY----SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2018
Cdd:PRK10619 107 MTVLENVMEAPIQVLGlskqearERAVKYLAKVGIDERAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*..
gi 5734101 2019 ARRFLWNCALSVVKEGRSVVLTSHSME 2045
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
850-1029 |
4.17e-08 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 57.43 E-value: 4.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 850 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMSTIRQNlgvcpQHN 922
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRAE-----QIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 923 VLF-DMLT-------VEEHIWFYARL-KGLSEKHVKAEMEQMALDVGLPSSKLKSKT--SQLSGGMQRKLSVALAFVGGS 991
Cdd:PRK09473 101 MIFqDPMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 5734101 992 KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTH 1029
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1866-2074 |
4.72e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSST----FKMLTGDTTVTRGDAFLNRNSILSN------IHEVHQNmgycPQfD 1935
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgrkIATIMQN----PR-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1936 AITELLTGREHVEFFALLRGVPEKEVGKVGewAIRKLGLVKYG---EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2012
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2013 TGMDPKAR-RFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNR 2074
Cdd:PRK10418 169 TDLDVVAQaRILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1851-2061 |
5.67e-08 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.09 E-value: 5.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIY-RRKrkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDA-FLNRNSILSNIHE----- 1923
Cdd:PRK11701 6 LLSVRGLTKLYgPRK---GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYAlseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 -----------VHQN--MGYCPQFDA---ITElltgRehveffalLRGVPEKEVGKVGEWAIRKLGLVKYGEK----YAG 1983
Cdd:PRK11701 83 rrrllrtewgfVHQHprDGLRMQVSAggnIGE----R--------LMAVGARHYGDIRATAGDWLERVEIDAAriddLPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1984 NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD--PKARrfLWNCALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNG 2060
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQG 228
|
.
gi 5734101 2061 R 2061
Cdd:PRK11701 229 R 229
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1868-2077 |
5.78e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.98 E-value: 5.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEvhqnmgycpqfdAITELLTGREHV 1947
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1948 EFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNC- 2026
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKKCl 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 2027 -ALSVVKE-GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGD 2077
Cdd:PRK13545 184 dKMNEFKEqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1849-2063 |
6.60e-08 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 6.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1849 NDILEIKELTKIY----RRKRkpaVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGD-TTVTRGDAFLNRNSI------ 1917
Cdd:TIGR02633 255 DVILEARNLTCWDvinpHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnpa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1918 ------LSNIHEVHQNMGYCPQFdAITELLTGREHVEFFALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYA-GNYSGGNK 1990
Cdd:TIGR02633 332 qairagIAMVPEDRKRHGIVPIL-GVGKNITLSVLKSFCFKMRIDAAAELQIIGS-AIQRLKVKTASPFLPiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1991 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRFR 2063
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
851-1027 |
8.88e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 57.49 E-value: 8.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYiLGKDIRsemstirqnLGVCPQHNVLFdMLTV 930
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-LAKGIK---------LGYFAQHQLEF-LRAD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 931 EEHIWFYARLkglsekhVKAEMEQMALD----VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1006
Cdd:PRK10636 392 ESPLQHLARL-------APQELEQKLRDylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|.
gi 5734101 1007 SRRGIWELLLKYrQGRTIILS 1027
Cdd:PRK10636 465 MRQALTEALIDF-EGALVVVS 484
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1866-2042 |
9.91e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.57 E-value: 9.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAITELLTGRE 1945
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1946 HVeFFALLRGVPEKEVGKVgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2025
Cdd:PRK13540 94 NC-LYDIHFSPGAVGITEL----CRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*..
gi 5734101 2026 CALSVVKEGRSVVLTSH 2042
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1855-2060 |
1.00e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.94 E-value: 1.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1855 KELTKIYRRK---RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSN-----IHEVHQ 1926
Cdd:PRK13646 6 DNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQF--DAITELLTGREhVEFFALLRGVPEKEVGKVGEWAIRKLGLVK-YGEKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:PRK13646 86 RIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2004 PVVFLDEPTTGMDPKARRFLWNCALSV-VKEGRSVVLTSHSMEECEALCTRMAIMVNG 2060
Cdd:PRK13646 165 DIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
972-1029 |
1.05e-07 |
|
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: 53.52 E-value: 1.05e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 972 QLSGGMQRKLSVALAF----VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTH 1029
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITH 139
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1866-2071 |
1.21e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.49 E-value: 1.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GDAFLNRNSILS--NIHEVHQNMGYCPQ----- 1933
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSGYRysGDVLLGGRSIFNyrDVLEFRRRVGMLFQrpnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1934 -FDAITELLTG-REHV-----EFfallRGVPEKEVGKVGEWAIRKLGLvkygEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:PRK14271 114 pMSIMDNVLAGvRAHKlvprkEF----RGVAQARLTEVGLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2007 FLDEPTTGMDP----KARRFLWNCAlsvvkEGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:PRK14271 186 LLDEPTSALDPttteKIEEFIRSLA-----DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1852-2061 |
1.49e-07 |
|
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: 56.65 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLN--------RNSILSNIHE 1923
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghdladytLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VHQNMGYcpqFDAitellTGREHVEFFALlRGVPEKEVGKVGEWAIRK-------LGL-VKYGEKyAGNYSGGNKRKLST 1995
Cdd:TIGR02203 411 VSQDVVL---FND-----TIANNIAYGRT-EQADRAEIERALAAAYAQdfvdklpLGLdTPIGEN-GVLLSGGQRQRLAI 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKARRfLWNCALSVVKEGRSVVLTSHSMEECEAlCTRMAIMVNGR 2061
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIEK-ADRIVVMDDGR 544
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1872-2073 |
1.51e-07 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 54.64 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1872 ICVGIPPGECFGLLGVNGAGKSSTFKML-------TGDTTVTrGDAF-LNRNSILSNIHEVHQNMGYCPQFDAITELLTG 1943
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIA-GNHFdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1944 REH-VEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrf 2022
Cdd:PRK11124 100 QQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2023 LWNCALSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKN 2073
Cdd:PRK11124 176 ITAQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
839-1032 |
1.86e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIWFYARLKglsekhvKAEMEQMALDVGLPSS----------KLKSKTSQLSGGMQRKLSVALAF 987
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPYEQWS-------DEEIWKVAEEVGLKSVieqfpdkldfVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMD 1032
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1851-2062 |
1.88e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 56.19 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTkIYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI------------L 1918
Cdd:COG3845 257 VLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrrlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1919 SNIHEVHQNMGYCPQFDaITE--LLTGREHVEF--FALLRGvpekevGKVGEWAIRKLglvkygEKY----------AGN 1984
Cdd:COG3845 336 AYIPEDRLGRGLVPDMS-VAEnlILGRYRRPPFsrGGFLDR------KAIRAFAEELI------EEFdvrtpgpdtpARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1985 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1852-2069 |
1.99e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.48 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNIHEVHQNMGYC 1931
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 PQFDAITELLTGREHVEFFalLRGVPEKEvgKVGEWAIRK-----LGLVKYG---EKYAGNYSGGNKRKLSTAMALIGGP 2003
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG--LTVLPRRE--RPNAAAIKAkvtqlLEMVQLAhlaDRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 2004 PVVFLDEPTTGMDPKARRFL--WNCALSVVKEGRSVVLTsHSMEECEALCTRMAIMVNGRFRCLGSVQ 2069
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELrrWLRQLHEELKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1878-2016 |
2.31e-07 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 53.42 E-value: 2.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1878 PGECFGLLGVNGAGKSSTFKMLTGDTTVT---RGDAFLNRNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLR 1954
Cdd:cd03233 32 PGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALRCK 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1955 GvpeKEVgkvgewaIRKLglvkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:cd03233 112 G---NEF-------VRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1853-2042 |
2.35e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 54.32 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1853 EIKELTKIYRRKrkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKML-------TGDTTV-------TRGDAFLNRNSIL 1918
Cdd:COG4604 3 EIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMIsrllppdSGEVLVdgldvatTPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1919 snihevhqnmgycPQFDAITELLTGREHVEF--FALLRGVPEKE-VGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLST 1995
Cdd:COG4604 81 -------------RQENHINSRLTVRELVAFgrFPYSKGRLTAEdREIIDE-AIAYLDLEDLADRYLDELSGGQRQRAFI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKA--------RRflwncalsVVKE-GRSVVLTSH 2042
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLDMKHsvqmmkllRR--------LADElGKTVVIVLH 194
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
839-1049 |
2.51e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 56.52 E-value: 2.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGV 917
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLF------DMLTVEEH----IWfyarlKGLSEKHVKAEMEQMALdvGLpSSKLKSKTSQLSGGMQRKLSVALAF 987
Cdd:PLN03232 1315 IPQSPVLFsgtvrfNIDPFSEHndadLW-----EALERAHIKDVIDRNPF--GL-DAEVSEGGENFSVGQRQLLSLARAL 1386
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdVLGDRIAIISHGKL 1049
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-IDCDKILVLSSGQV 1447
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
851-1054 |
2.53e-07 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 54.35 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyilgkdIRSEMSTIrqnlGVCPQhNVLFDM--- 927
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRI----GYVPQ-KLYLDTtlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 928 LTVEEhiwfYARLKGlsekHVKAEMEQMALDVGLPSSKLKSKTSQLSGG-MQRKLsVALAFVGGSKVVILDEPTAGVDPY 1006
Cdd:PRK09544 84 LTVNR----FLRLRP----GTKKEDILPALKRVQAGHLIDAPMQKLSGGeTQRVL-LARALLNRPQLLVLDEPTQGVDVN 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 1007 SRRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHgKLCCVGS 1054
Cdd:PRK09544 155 GQVALYDLIDQLRRelDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGT 203
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1851-2060 |
2.69e-07 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 54.01 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLT--GD----TTVTrgdaflnrNSILSNIHEV 1924
Cdd:PRK14239 5 ILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpeVTIT--------GSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1925 hqnmgYCPQFDAItEL---------------LTGREHVEFFALLRGVPEKEV-GKVGEWAIRKLGL---VK-YGEKYAGN 1984
Cdd:PRK14239 75 -----YSPRTDTV-DLrkeigmvfqqpnpfpMSIYENVVYGLRLKGIKDKQVlDEAVEKSLKGASIwdeVKdRLHDSALG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1985 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSvVKEGRSVVLTSHSMEECEALCTRMAIMVNG 2060
Cdd:PRK14239 149 LSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1867-2016 |
3.32e-07 |
|
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: 55.52 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1867 PAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIlSNI--HEVHQNMGYCPQ----FD-AITE 1939
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIdrHTLRQFINYLPQepyiFSgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1940 -LLTGREhveffallRGVPEKEVGKVGEWA-IRK------LGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2011
Cdd:TIGR01193 567 nLLLGAK--------ENVSQDEIWAACEIAeIKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 5734101 2012 TTGMD 2016
Cdd:TIGR01193 639 TSNLD 643
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1848-2061 |
3.45e-07 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 53.73 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS--NIHEVH 1925
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNMGYCPQFDAITELLTGREHVE---FFALlRGVPEKEVGKVGEWAIRklgLVKYGEKYAGNYSGGNKRKLSTAMALIGG 2002
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAmggFFAE-RDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2003 PPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
855-1029 |
4.36e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 54.36 E-value: 4.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYIL---GKDIR------------SEMSTIRQN--LG 916
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLefnGQDLQrisekerrnlvgAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 917 VCPQHNVLFD-MLTVEEHiwfyarlKGLSekhvKAEMEQMALD----VGLP--SSKLKSKTSQLSGGMQRKLSVALAFVG 989
Cdd:PRK11022 102 LNPCYTVGFQiMEAIKVH-------QGGN----KKTRRQRAIDllnqVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 5734101 990 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTH 1029
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITH 212
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
841-1055 |
4.42e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 53.64 E-value: 4.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 841 IQNLVKV--YRDGM-----KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK-----DIRSEM 908
Cdd:PRK15112 7 VRNLSKTfrYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 909 STIRQ-----NLGVCPQHNV--LFDM-------LTVEEHiwfyarlkglsEKHVKAEMEQmaldVGLPSSKLKSKTSQLS 974
Cdd:PRK15112 87 QRIRMifqdpSTSLNPRQRIsqILDFplrlntdLEPEQR-----------EKQIIETLRQ----VGLLPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 975 GGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADVLGDRIAIISHGKLCCV 1052
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
...
gi 5734101 1053 GSS 1055
Cdd:PRK15112 232 GST 234
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1852-2049 |
4.82e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.48 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTkIYRRKRkPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTT---VTRGDAFLNRNSILS-NIHEvhQN 1927
Cdd:COG4136 2 LSLENLT-ITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTAlPAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1928 MGYCPQfdaiTELLtgrehveF----------FALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 1997
Cdd:COG4136 78 IGILFQ----DDLL-------FphlsvgenlaFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1998 ALIGGPPVVFLDEPTTGMDP----KARRFLWNcalSVVKEGRSVVLTSHSMEECEA 2049
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAalraQFREFVFE---QIRQRGIPALLVTHDEEDAPA 199
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1878-2042 |
5.70e-07 |
|
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: 53.14 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1878 PGECFGLLGVNGAGKSSTFKMLTGdttvtrgdaflnrnsilsnihEVHQNMG-YC--PQFDAITELLTGREHVEFFALLR 1954
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSELQNYFTKLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1955 G--------------VPEKEVGKVGE------------WAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2008
Cdd:cd03236 84 EgdvkvivkpqyvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFF 163
|
170 180 190
....*....|....*....|....*....|....
gi 5734101 2009 DEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2042
Cdd:cd03236 164 DEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
839-1049 |
6.11e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 53.32 E-value: 6.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMlTVEEHIWFYarlkglsEKHVKAEMEQMALDVGLPSS----------KLKSKTSQLSGGMQRKLSVALAF 987
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPY-------GKWSDEEIWKVAEEVGLKSVieqfpgqldfVLVDGGCVLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 988 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKL 1049
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1861-2054 |
6.65e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1861 YRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNihEVHQNMGYCPQFDAITEL 1940
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1941 LTGREHVEFFALLRGV-PEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2019
Cdd:PRK13543 97 LSTLENLHFLCGLHGRrAKQMPGS----ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180 190
....*....|....*....|....*....|....*
gi 5734101 2020 RRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRM 2054
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
873-1005 |
6.77e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.16 E-value: 6.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 873 GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVCPQhnvLFDMLTVEEHIWFyarLKGLSEKHVKaE 951
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAK-Q 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 952 MEQMALD-VGLPSSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1005
Cdd:PRK13543 117 MPGSALAiVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1852-2061 |
7.09e-07 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.76 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDaFLNRNSILSNIHEVHQNMgyc 1931
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-LLAGTAPLAEAREDTRLM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 pqfdaitelltgrehvefFALLRGVPEKEV------GKVGEW------AIRKLGLVKYGEKYAGNYSGGNKRKLSTAMAL 1999
Cdd:PRK11247 87 ------------------FQDARLLPWKKVidnvglGLKGQWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKAR-------RFLWNcalsvvKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRiemqdliESLWQ------QHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
863-1048 |
7.41e-07 |
|
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: 51.84 E-value: 7.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 863 FYEGqITSFLGHNGAGKTTTMS----ILTGLFPPTSGTAYILGKDIRSEMS----------------TIRQNLGV----- 917
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGEVraqvklafenangkkyTITRSLAIlenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 -CPQhnvlfdmltvEEHIWFYARLKGlsekhvkaemeqmaldvglpssklksktsQLSGGMQRKLSV----ALAFVGGSK 992
Cdd:cd03240 99 fCHQ----------GESNWPLLDMRG-----------------------------RCSGGEKVLASLiirlALAETFGSN 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 993 --VVILDEPTAGVDPYSRRGIWELLLKYRQG---RTIILSTHHMDEADVLGD--RIAIISHGK 1048
Cdd:cd03240 140 cgILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1865-2016 |
9.55e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 52.68 E-value: 9.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1865 RKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNI-HEVHQNMGYCPQfDAIT----- 1938
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRIGLLAQ-NATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1939 --ELLT-GR-EHVEFFALLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2014
Cdd:PRK10253 98 vqELVArGRyPHQPLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 5734101 2015 MD 2016
Cdd:PRK10253 174 LD 175
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
837-1067 |
1.30e-06 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.56 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 837 LGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILGKDI---RSEMSTIRQ 913
Cdd:PRK10789 314 LDVNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIpltKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 914 NLGVCPQHNVLFDMlTV------------EEHIWFYARLKGLSEKHVKaemeqmaldvgLPS---SKLKSKTSQLSGGMQ 978
Cdd:PRK10789 390 RLAVVSQTPFLFSD-TVannialgrpdatQQEIEHVARLASVHDDILR-----------LPQgydTEVGERGVMLSGGQK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 979 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADVLGDRIAIISHGKLCCVGSSLFL 1058
Cdd:PRK10789 458 QRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQL 536
|
....*....
gi 5734101 1059 KNQlgTGYY 1067
Cdd:PRK10789 537 AQQ--SGWY 543
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
866-1031 |
1.37e-06 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 51.56 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-----RQNLGVCPQHNVLFDMlTVEEHIWFYARL 940
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 941 kglSEKHVKAEMEQMAL--DVGL----PSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY-SRRGIWE 1013
Cdd:cd03290 106 ---NKQRYKAVTDACSLqpDIDLlpfgDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQE 182
|
170 180
....*....|....*....|
gi 5734101 1014 LLLKYRQG--RTIILSTHHM 1031
Cdd:cd03290 183 GILKFLQDdkRTLVLVTHKL 202
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1866-2042 |
1.50e-06 |
|
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: 51.46 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1866 KPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnrnSIL---SNIHEVHQN-----MGYCPQ---- 1933
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSG-------SILidgQDIREVTLDslrraIGVVPQdtvl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1934 FDAITE--LLTGR-----EHVEFFA-------LLRGVPEKEVGKVGEwaiRKLGLvkygekyagnySGGNKRKLSTAMAL 1999
Cdd:cd03253 87 FNDTIGynIRYGRpdatdEEVIEAAkaaqihdKIMRFPDGYDTIVGE---RGLKL-----------SGGEKQRVAIARAI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5734101 2000 IGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSH 2042
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQA-ALRDVSKGRTTIVIAH 194
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1879-2016 |
1.64e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 52.42 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1879 GECFGLLGVNGAGKSSTFKMLTG---DTTVTRGDAFLNRNSILsNIHEVHQNMGYCPQF-----DAITEL----LTGREH 1946
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREIL-NLPEKELNKLRAEQIsmifqDPMTSLnpymRVGEQL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 1947 VEFFALLRGVPEKEVGkvgEWAIRKLGLVKYGEK------YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK09473 121 MEVLMLHKGMSKAEAF---EESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
855-1053 |
1.87e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 855 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNLGVCPQ--HNVLFDML 928
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 929 TVEEHIWFYARLKGLSEKHVKAEMEQMALD-VGLPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYS 1007
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAARVAWLLErVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 5734101 1008 RRGIWELLLKYRQ--GRTIILSTHHMDEADVLGDRIAIISHGKLCCVG 1053
Cdd:PRK10261 499 RGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1983-2063 |
2.01e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 53.01 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1983 GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGRF 2062
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
.
gi 5734101 2063 R 2063
Cdd:PRK13549 484 K 484
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
839-1004 |
2.59e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 2.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 917
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLF------DMLTVEEH----IWfyarlKGLSEKHVKAEMEQMALdvGLpSSKLKSKTSQLSGGMQRKLSVALAF 987
Cdd:PLN03130 1318 IPQAPVLFsgtvrfNLDPFNEHndadLW-----ESLERAHLKDVIRRNSL--GL-DAEVSEAGENFSVGQRQLLSLARAL 1389
|
170
....*....|....*..
gi 5734101 988 VGGSKVVILDEPTAGVD 1004
Cdd:PLN03130 1390 LRRSKILVLDEATAAVD 1406
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
859-1049 |
2.89e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.42 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 859 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTI----------RQNLGVCPQHNVLFD 926
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 927 MLtVEEHIWFYARLKGLSEKHVKAEMEQM--ALDVGLPSSKlkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:PRK10982 347 SL-ISNIRNYKNKVGLLDNSRMKSDTQWVidSMRVKTPGHR--TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGID 423
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 5734101 1005 PYSRRGIWELLLKY-RQGRTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10982 424 VGAKFEIYQLIAELaKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
839-1027 |
2.98e-06 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 52.24 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRseMSTIRQNlgvc 918
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETVK--LAYVDQS---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 919 pqHNVLFDMLTVEEHIwfyarLKGLSEKHV-KAEMEQMALdVG---LPSSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 994
Cdd:TIGR03719 394 --RDALDPNKTVWEEI-----SGGLDIIKLgKREIPSRAY-VGrfnFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|...
gi 5734101 995 ILDEPTAGVDPYSRRGIWELLLKYrQGRTIILS 1027
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNF-AGCAVVIS 497
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1713-2045 |
3.35e-06 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 51.24 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1713 VNLFIGINGSVATFVLELFtdnklnnindilksvflifphfclgRGLIDMVKNQAMADALERFGENRFVSPLSWDLvGRN 1792
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEAL-------------------------RFLADFDALVIGLTDERSRNGGIGGIPSLLNG-IDP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1793 LFAMAVEGVVFFLITVLIQYRFFIRPRPVNAKLSPLNDEDEDvRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRI 1872
Cdd:pfam13304 55 KEPIEFEISEFLEDGVRYRYGLDLEREDVEEKLSSKPTLLEK-RLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1873 CVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVHQnmgYCPQFDAITELLTGREHVEFFAL 1952
Cdd:pfam13304 134 ELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR---LVRGLKLADLNLSDLGEGIEKSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1953 LRGVPEKEVGKVgeWAIRKLGlvkyGEKYAGNYSGGNKRKLSTAMALI---GGPPVVFLDEPTTGMDPKARRFLWNCALS 2029
Cdd:pfam13304 211 LVDDRLRERGLI--LLENGGG----GELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKE 284
|
330
....*....|....*.
gi 5734101 2030 VVKEGRSVVLTSHSME 2045
Cdd:pfam13304 285 LSRNGAQLILTTHSPL 300
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
839-1033 |
3.86e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.94 E-value: 3.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST---IRQNL 915
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSGETiwdIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GV------------CPQHNVL----FDmltveeHIWFYarlKGLSEKHVKAEMEQMALdVGLPSSKLKSKTSQLSGGMQR 979
Cdd:PRK10938 339 GYvssslhldyrvsTSVRNVIlsgfFD------SIGIY---QAVSDRQQKLAQQWLDI-LGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 5734101 980 KLSVALAFVGGSKVVILDEPTAGVDPYSR---RGIWELLLkyRQGRTIILSTHHMDE 1033
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI--SEGETQLLFVSHHAE 463
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1851-2061 |
4.74e-06 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 49.87 E-value: 4.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSIL----SNIHEVHQ 1926
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2006
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 2007 FLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGH 214
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1876-2016 |
6.95e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 6.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTtvtrgDAFLNRNS--ILSNIHEVHQNMG-------YCPQFDAITELLTGREH 1946
Cdd:TIGR00956 84 IKPGELTVVLGRPGSGCSTLLKTIASNT-----DGFHIGVEgvITYDGITPEEIKKhyrgdvvYNAETDVHFPHLTVGET 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1947 VEFFALLR-------GVPEKE-VGKVGEWAIRKLGL-----VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2013
Cdd:TIGR00956 159 LDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNATR 238
|
...
gi 5734101 2014 GMD 2016
Cdd:TIGR00956 239 GLD 241
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
1982-2062 |
8.21e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1982 AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGR 481
|
.
gi 5734101 2062 F 2062
Cdd:NF040905 482 I 482
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
838-1047 |
9.56e-06 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 50.23 E-value: 9.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 838 GVSIQNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 917
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 CPQHNVLFDMLTVEEHIWFYARLKGLSEKHVKAEMEQMA--LDVGlpsSKLKSKTSQLSGGmQRKlSVAL--AFVGGSKV 993
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAAriLELE---PLLDRKPRELSGG-QRQ-RVAMgrAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 994 VILDEPTAGVDPYSR---RgiWELL-LKYRQGRTIILSTHHMDEADVLGDRIAIISHG 1047
Cdd:PRK11650 156 FLFDEPLSNLDAKLRvqmR--LEIQrLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1877-2061 |
1.19e-05 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 48.86 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1877 PPGECFGLLGVNGAGKSSTFKML-------TGDTTVTRGDAFLNRNSILSNIHEVHQNMGYCPQFDAITELLTGREH-VE 1948
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIAGHQFDFSQKPSEKAIRLLRQKVGMVFQQYNLWPHLTVMENlIE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1949 FFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrfLWNCAL 2028
Cdd:COG4161 106 APCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQVV 181
|
170 180 190
....*....|....*....|....*....|....*..
gi 5734101 2029 SVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:COG4161 182 EIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
971-1029 |
1.27e-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: 49.70 E-value: 1.27e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 5734101 971 SQLSGGMQRKLSVALAF---VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRT-IILSTH 1029
Cdd:pfam13304 235 FELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
849-1049 |
1.86e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 849 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG---------LFP---------------PTSGTAYILGKDi 904
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsyTFPgnwqlawvnqetpalPQPALEYVIDGD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 905 rSEMSTIRQNLGVCPQHNVLFDMLTVeehiwfYARLKGLSEKHVKAEMEQMALDVGLPSSKLKSKTSQLSGGMQRKLSVA 984
Cdd:PRK10636 89 -REYRQLEAQLHDANERNDGHAIATI------HGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 5734101 985 LAFVGGSKVVILDEPTAGVDPYSRrgIW-ELLLKYRQGrTIILSTHHMDEADVLGDRIAIISHGKL 1049
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAV--IWlEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
848-1054 |
1.89e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.16 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 848 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQHNVLFD 926
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYgLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 927 ---MLTVE-------EHIWFYARLKGLSEkHVKAEMEqmaldvGLPSSKLKSKtSQLSGGMQRKLSVALAFVG-GSKVVI 995
Cdd:PTZ00243 1398 gtvRQNVDpfleassAEVWAALELVGLRE-RVASESE------GIDSRVLEGG-SNYSVGQRQLMCMARALLKkGSGFIL 1469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 996 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADVLgDRIAIISHGKLCCVGS 1054
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1876-2042 |
1.91e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 48.37 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTV-----TRGDAFLNRNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF 1949
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1950 -FALLRGVPEK-EVGKVGEWAIRKLGL---VKYG-EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2023
Cdd:PRK14247 106 gLKLNRLVKSKkELQERVRWALEKAQLwdeVKDRlDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170
....*....|....*....
gi 5734101 2024 WNCALSVVKEgRSVVLTSH 2042
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTH 203
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
851-1020 |
2.05e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 851 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYILGKDI----RSEMSTIRQNLGVCPQ--HNVL 924
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 925 FDMLTVEEHIWFYARL--KGLS----EKHVKAEMEQMALDvglPSSKLKSKtSQLSGGMQRKLSVALAFVGGSKVVILDE 998
Cdd:PRK15134 376 NPRLNVLQIIEEGLRVhqPTLSaaqrEQQVIAVMEEVGLD---PETRHRYP-AEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180
....*....|....*....|..
gi 5734101 999 PTAGVDPYSRRGIWELLLKYRQ 1020
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQ 473
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
845-1031 |
2.06e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 845 VKVYRDgmkvavdgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG----KDIrsEMSTIRQNLGVCPQ 920
Cdd:PTZ00265 398 VEIYKD--------LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLFDML---TVEEHIWFYARLKGLSEK---------------------------------------HVKAEMEQM--- 955
Cdd:PTZ00265 468 DPLLFSNSiknNIKYSLYSLKDLEALSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQTIkds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 956 -ALDV-----------GLP---SSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKY 1018
Cdd:PTZ00265 548 eVVDVskkvlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKG 627
|
250
....*....|...
gi 5734101 1019 RQGRTIILSTHHM 1031
Cdd:PTZ00265 628 NENRITIIIAHRL 640
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
856-1049 |
2.30e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.40 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 856 VDGLALNFYEGQITSFLGHNGAGKT-TTMSILT---GLFppTSGTAYILGKDIRseMSTI--------------RQNLGV 917
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyGRN--ISGTVFKDGKEVD--VSTVsdaidaglayvtedRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 918 cpqhnVLFDmlTVEEHIWFyARLKGLSEKHVKAEMEQMAL------DVGLPSSKLKSKTSQLSGGMQRKlsVALA---FV 988
Cdd:NF040905 352 -----NLID--DIKRNITL-ANLGKVSRRGVIDENEEIKVaeeyrkKMNIKTPSVFQKVGNLSGGNQQK--VVLSkwlFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 989 GgSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadVLG--DRIAIISHGKL 1049
Cdd:NF040905 422 D-PDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPE--LLGmcDRIYVMNEGRI 482
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
866-1049 |
2.83e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 2.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 866 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYARLKGLS- 944
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERy 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 945 EKHVKAEMEQMALDVgLPSSKLKS---KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-Q 1020
Cdd:PLN03130 711 ERAIDVTALQHDLDL-LPGGDLTEigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190
....*....|....*....|....*....|..
gi 5734101 1021 GRTIILST---HHMDEAdvlgDRIAIISHGKL 1049
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMI 817
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
873-1004 |
3.43e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 3.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 873 GHNGAGKTTTMSILTGLFPPTSGTaYILGKDI----------RSEMSTIRQNL--GVCPQ-------HNVLFDMLT--VE 931
Cdd:PRK11147 36 GRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLivarlqqdppRNVEGTVYDFVaeGIEEQaeylkryHDISHLVETdpSE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 932 EHIWFYARLKGLSEKH--------VKAEMEQMALDvglPSSKLksktSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1003
Cdd:PRK11147 115 KNLNELAKLQEQLDHHnlwqlenrINEVLAQLGLD---PDAAL----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHL 187
|
.
gi 5734101 1004 D 1004
Cdd:PRK11147 188 D 188
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
853-1055 |
3.67e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 853 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYilgkdirSEMStirqnLGVCPQHNVLFDMlTVEE 932
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERS-----IAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 933 HIWFY-----ARLkglsekHVKAEMEQMALDVGLPSSKLKS----KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1003
Cdd:PTZ00243 740 NILFFdeedaARL------ADAVRVSQLEADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 1004 DPY-SRRGIWELLLKYRQGRTIILSTHHMDEADvLGDRIAIISHGKLCCVGSS 1055
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS 865
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
865-1044 |
5.10e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.24 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 865 EGQITSFLGHNGAGKTTTMSILTGLF---------PPT--------SGTA---YIlgKDIRS-EMSTIRQnlgvcPQHnv 923
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfRGTElqdYF--KKLANgEIKVAHK-----PQY-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 924 lFDML------TVEEhiwfyaRLKGLSEKHVKAE-MEQMALDvglpsSKLKSKTSQLSGG-MQRkLSVALAFVGGSKVVI 995
Cdd:COG1245 169 -VDLIpkvfkgTVRE------LLEKVDERGKLDElAEKLGLE-----NILDRDISELSGGeLQR-VAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 5734101 996 LDEPTAGVDPYSR----RGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAII 1044
Cdd:COG1245 236 FDEPSSYLDIYQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1876-2071 |
5.44e-05 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 46.88 E-value: 5.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRN------------SIL---SNI--H-EVHQN--MGYCPQFD 1935
Cdd:PRK10771 22 VERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQdhtttppsrrpvSMLfqeNNLfsHlTVAQNigLGLNPGLK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1936 aitelLTGREHveffallrgvpekevGKVGEWAiRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2015
Cdd:PRK10771 102 -----LNAAQR---------------EKLHAIA-RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 5734101 2016 DPKARrflwNCALSVVKE---GRSVVL--TSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:PRK10771 161 DPALR----QEMLTLVSQvcqERQLTLlmVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
839-1046 |
5.90e-05 |
|
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: 45.61 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGmKVAVDGLALNFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTSGTayilgkdirsemstirqnL 915
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGR------------------I 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 916 GVCPQHNVLFdmltVEEHIWFYA-RLKglsekhvkaemEQMALdvglPSSKlksktsQLSGGMQRKLSVALAFVGGSKVV 994
Cdd:cd03223 59 GMPEGEDLLF----LPQRPYLPLgTLR-----------EQLIY----PWDD------VLSGGEQQRLAFARLLLHKPKFV 113
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 995 ILDEPTAGVDPYSRRGIWELLlkyRQGRTIILSTHHMDEADVLGDRIAIISH 1046
Cdd:cd03223 114 FLDEATSALDEESEDRLYQLL---KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1851-2061 |
6.12e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 6.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRkpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGDAFLNRNSIL----S 1919
Cdd:PRK13549 5 LLEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyEGEIIFEGEELQASNIRdterA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1920 NIHEVHQNMGYCPQFDAITELLTGREHVEFfallrGVP--EKEVGKVGEWaIRKLGLVKYGEKYAGNYSGGNKRKLSTAM 1997
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPG-----GIMdyDAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1998 ALIGGPPVVFLDEPTTGMDPKARRFLwncaLSVVKE----GRSVVLTSHSMEECEALCTRMAIMVNGR 2061
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVL----LDIIRDlkahGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1848-2108 |
6.19e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 47.07 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTkiYRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSI----LSNIHE 1923
Cdd:PRK11831 4 VANLVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VHQNMGYCPQFDAITELLTGREHVEFfallrgvPEKEVGKVGEWAIRKLGLVKY---GEKYAGNY-----SGGNKRKLST 1995
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKLeavGLRGAAKLmpselSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1996 AMALIGGPPVVFLDEPTTGMDPKARRFL------WNCALSVvkegrSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQ 2069
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVLvkliseLNSALGV-----TCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQ 229
|
250 260 270
....*....|....*....|....*....|....*....
gi 5734101 2070 HLKNrfgdgytivvriagsNPDLKPVQDFFGLAfPGSVP 2108
Cdd:PRK11831 230 ALQA---------------NPDPRVRQFLDGIA-DGPVP 252
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
921-1032 |
6.21e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLfDMlTVEEHIWFYARLKGLSEKHvkaemeQMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVALAF-VGGSKVVILD 997
Cdd:cd03271 126 ADVL-DM-TVEEALEFFENIPKIARKL------QTLCDVGLGYIKLGQPATTLSGGeAQRiKLAKELSKrSTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....*.
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMD 1032
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLD 233
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1851-2042 |
6.28e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.94 E-value: 6.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKiyRRKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGDAFLNRNSILSNIHEVHQNM 1928
Cdd:CHL00131 7 ILEIKNLHA--SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1929 GYCPQFDAITElLTGREHVEFFAL-------LRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNY-----SGGNKRK---L 1993
Cdd:CHL00131 85 GIFLAFQYPIE-IPGVSNADFLRLaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNvnegfSGGEKKRneiL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 5734101 1994 StaMALIgGPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSH 2042
Cdd:CHL00131 164 Q--MALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1852-2042 |
7.49e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 47.79 E-value: 7.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1852 LEIKELTKIYRRKrKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEV-HQNMGY 1930
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQ---------FDAITellTGR-----------EHVEFFALLRGVPEKEVGKVGEwairklglvkygekYAGNYSGGNK 1990
Cdd:PRK10790 420 VQQdpvvladtfLANVT---LGRdiseeqvwqalETVQLAELARSLPDGLYTPLGE--------------QGNNLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1991 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSVVKEGRSVVLTSH 2042
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQ-ALAAVREHTTLVVIAH 533
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1872-2016 |
7.98e-05 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 46.65 E-value: 7.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1872 ICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGdaflnrnsilSNIHEVHQNMGYCPQ---FDAITELLTGRehve 1948
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR---- 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 5734101 1949 FFALLRGVPEKEVGKvgewAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK09544 89 FLRLRPGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1851-2016 |
1.22e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 47.41 E-value: 1.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKML-------TGDTTVTRGD-AFLNRNSiLSN 1920
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDvATLDADA-LAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1921 IHEVHqnMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALI 2000
Cdd:PRK10535 83 LRREH--FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170
....*....|....*.
gi 5734101 2001 GGPPVVFLDEPTTGMD 2016
Cdd:PRK10535 161 NGGQVILADEPTGALD 176
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1851-2042 |
1.23e-04 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 46.32 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYR-------RKRKPAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDaflnrnsILSNIHE 1923
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGE-------LLIDDHP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1924 VH-QNMGYCPQ-----FDAITELLTGREHV----EFFALLR---GVPEKEvgKVGEWAIRKLGLVK-YGEKYAGNYSGGN 1989
Cdd:PRK15112 77 LHfGDYSYRSQrirmiFQDPSTSLNPRQRIsqilDFPLRLNtdlEPEQRE--KQIIETLRQVGLLPdHASYYPHMLAPGQ 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 1990 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSVV-KEGRS-VVLTSH 2042
Cdd:PRK15112 155 KQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISyIYVTQH 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1828-2016 |
2.02e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.27 E-value: 2.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1828 LNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYRrkrkpavDRICV-----GIPPGECFGLLGVNGAGKSSTFKML 1899
Cdd:PRK11819 298 LLSEEYQKRNETNEIFIPPGPrlgDKVIEAENLSKSFG-------DRLLIddlsfSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1900 TG----DT-TVTRGDAflnrnsilsniheVHqnMGYCPQFdaitelltgREHVEffallrgvPEKEVGKV--GEWAIRKL 1972
Cdd:PRK11819 371 TGqeqpDSgTIKIGET-------------VK--LAYVDQS---------RDALD--------PNKTVWEEisGGLDIIKV 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 5734101 1973 GLVK-----Y-------G---EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK11819 419 GNREipsraYvgrfnfkGgdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1851-2016 |
2.68e-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: 46.08 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1851 ILEIKELTKIYRRKRKpAVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSilsnihevhqNMGY 1930
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE-ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGI----------KVGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1931 CPQFDAITELLTGREHVE--------------------------FFALLR--GVPEKEVGKVGEWAI-RKLGLVKY---- 1977
Cdd:TIGR03719 73 LPQEPQLDPTKTVRENVEegvaeikdaldrfneisakyaepdadFDKLAAeqAELQEIIDAADAWDLdSQLEIAMDalrc 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 5734101 1978 --GEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:TIGR03719 153 ppWDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD 193
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
839-1056 |
3.05e-04 |
|
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: 45.95 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTA-YILG---KDIRSEM-STI 911
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiYHVAlceKCGYVERpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 912 RQNLGVCPQHNVLFD--------------------ML----------TVEEHIwfyarLKGLSEKHVKAEME-QMALDVg 960
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEvdfwnlsdklrrrirkriaiMLqrtfalygddTVLDNV-----LEALEEIGYEGKEAvGRAVDL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 961 LPSSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEA 1034
Cdd:TIGR03269 153 IEMVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|..
gi 5734101 1035 DVLGDRIAIISHGKLCCVGSSL 1056
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPD 254
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1845-2016 |
3.11e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.11 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1845 GGGQNDILEIKELTKIY-------RRKRKP--AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRN 1915
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfGRTVGVvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1916 SILS-----------NIHEVHQNmgycPQ---------FDAITELLtgREHveffallRGVPEKEV-GKVGEwAIRKLGL 1974
Cdd:COG4608 81 DITGlsgrelrplrrRMQMVFQD----PYaslnprmtvGDIIAEPL--RIH-------GLASKAERrERVAE-LLELVGL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 5734101 1975 -VKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:COG4608 147 rPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
835-1004 |
4.97e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 4.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 835 LKLGVSIQNLVKVYRDGMKVA----VDGLAlnfYEGQITSFLGHNGAGKTTTMSILTG-----LFPPTSGTAY--ILGKD 903
Cdd:TIGR00956 55 LKILTRGFRKLKKFRDTKTFDilkpMDGLI---KPGELTVVLGRPGSGCSTLLKTIASntdgfHIGVEGVITYdgITPEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 904 IRSEMstiRQNLGVCPQHNVLFDMLTVEEHIWFYARLK-------GLSEKHVKAEMEQMALDV-GLPSSKlKSKTSQ--- 972
Cdd:TIGR00956 132 IKKHY---RGDVVYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEYAKHIADVYMATyGLSHTR-NTKVGNdfv 207
|
170 180 190
....*....|....*....|....*....|....
gi 5734101 973 --LSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:TIGR00956 208 rgVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1876-2082 |
5.57e-04 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 45.10 E-value: 5.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILS-NIHEVHQNMGYCPQfdaiTELLTGREHVEFFAL-L 1953
Cdd:TIGR00958 504 LHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ----EPVLFSGSVRENIAYgL 579
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1954 RGVPEKEVGKVGEWA-----IRKLGLVKY---GEKyaGNY-SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL- 2023
Cdd:TIGR00958 580 TDTPDEEIMAAAKAAnahdfIMEFPNGYDtevGEK--GSQlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLq 657
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2024 -WNCAlsvvkEGRSVVLTSHSMEECEAlCTRMAIMVNGRFRCLGSVQHLKNRFGDGYTIV 2082
Cdd:TIGR00958 658 eSRSR-----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
954-1029 |
5.63e-04 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.79 E-value: 5.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 954 QMALDVGLPSSKLKSKTSQLSGG-MQRklsVALAFVGGSKVV----ILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILS 1027
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVV 195
|
..
gi 5734101 1028 TH 1029
Cdd:cd03270 196 EH 197
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1876-2071 |
6.16e-04 |
|
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: 44.32 E-value: 6.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKSSTFKMLTGDTTVTRGDAFLNrNSILSNIHE-----VHQ-NMGYCPQfDAitEL---LTGREH 1946
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVLQDSARgiflpPHRrRIGYVFQ-EA--RLfphLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1947 VEFfALLRGVPEKEVGKVGEwAIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR----F 2022
Cdd:COG4148 98 LLY-GRKRAPRAERRISFDE-VVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAeilpY 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 5734101 2023 LwncaLSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHL 2071
Cdd:COG4148 176 L----ERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1876-2016 |
6.34e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.80 E-value: 6.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1876 IPPGECFGLLGVNGAGKsSTF-KMLTGDTTVTRGdaflnrnSILSNIhevhqNMGYCPQFdaitelLTGREHVEFFALLR 1954
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGK-TTFaKLLAGVLKPDEG-------EVDPEL-----KISYKPQY------IKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1955 GVPEK--------EVgkvgewaIRKLGLVKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2016
Cdd:PRK13409 423 SITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1957-2046 |
7.48e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 43.87 E-value: 7.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1957 PEKEVGKVGEWAIRKLGL---VKYG-EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDP----KARRFLWNCAL 2028
Cdd:PRK14258 119 PKLEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPiasmKVESLIQSLRL 198
|
90
....*....|....*...
gi 5734101 2029 svvKEGRSVVLTSHSMEE 2046
Cdd:PRK14258 199 ---RSELTMVIVSHNLHQ 213
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1868-2074 |
7.79e-04 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 44.13 E-value: 7.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1868 AVDRICVGIPPGECFGLLGVNGAGKSSTFKMLTG----DTTVTRGDAFLN------------RNSILSNIHEVHQNMGYC 1931
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdNWHVTADRFRWNgidllklsprerRKIIGREIAMIFQEPSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1932 pqFDAITELltGREhveffaLLRGVPEKEVGkvGEW----------AIR---KLGlVKYGEKYAGNY----SGGNKRKLS 1994
Cdd:COG4170 102 --LDPSAKI--GDQ------LIEAIPSWTFK--GKWwqrfkwrkkrAIEllhRVG-IKDHKDIMNSYphelTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1995 TAMALIGGPPVVFLDEPTTGMDPKAR----RFLwnCALSVVKeGRSVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQH 2070
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQaqifRLL--ARLNQLQ-GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 5734101 2071 LKNR 2074
Cdd:COG4170 246 ILKS 249
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1860-2080 |
1.38e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.54 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1860 IYRRK--RKPAVDRICVGIPPGECFGLLGVNGAGKSST----FKMLTGDTTVTRGDAFL---NRNSIL---SNIHEVHQ- 1926
Cdd:PRK15134 291 ILKRTvdHNVVVKNISFTLRPGETLGLVGESGSGKSTTglalLRLINSQGEIWFDGQPLhnlNRRQLLpvrHRIQVVFQd 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1927 -NMGYCPQFDA---ITELLTgrehVEFFALLRGVPEKEVGKVgewaIRKLGL-VKYGEKYAGNYSGGNKRKLSTAMALIG 2001
Cdd:PRK15134 371 pNSSLNPRLNVlqiIEEGLR----VHQPTLSAAQREQQVIAV----MEEVGLdPETRHRYPAEFSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 2002 GPPVVFLDEPTTGMDPKARRFLWNCALSVVKEGR-SVVLTSHSMEECEALCTRMAIMVNGRFRCLGSVQHLKNRFGDGYT 2080
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
954-1039 |
2.25e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.15 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 954 QMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHH 1030
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLSTLSGGeLQRvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHN 148
|
90
....*....|..
gi 5734101 1031 ---MDEADVLGD 1039
Cdd:cd03238 149 ldvLSSADWIID 160
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1848-2021 |
2.36e-03 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 41.62 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1848 QNDILEIKELTkiYRRKRKPAVDRICVGIPPGEcFGLL-GVNGAGKSSTFKMLTGDTTVTRGDAFLNRNSILSNIHEVH- 1925
Cdd:PRK10247 4 NSPLLQLQNVG--YLAGDAKILNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 1926 QNMGYCPQfdaiTELLTG---REHVEFFALLRGVpekevgKVGEWAIRKlGLVKYG------EKYAGNYSGGNKRKLSTA 1996
Cdd:PRK10247 81 QQVSYCAQ----TPTLFGdtvYDNLIFPWQIRNQ------QPDPAIFLD-DLERFAlpdtilTKNIAELSGGEKQRISLI 149
|
170 180
....*....|....*....|....*
gi 5734101 1997 MALIGGPPVVFLDEPTTGMDPKARR 2021
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKH 174
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
839-1004 |
2.44e-03 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 43.40 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 839 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTttmSILTGLF---PPTSGTAYILGKDI-RSEMSTIRQN 914
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 915 LGVCPQHNVLF--------DMLT--VEEHIWFyarlkGLSEKHVKAEMEqmaldvGLPsSKLKSKTSQ----LSGGMQRK 980
Cdd:TIGR00957 1362 ITIIPQDPVLFsgslrmnlDPFSqySDEEVWW-----ALELAHLKTFVS------ALP-DKLDHECAEggenLSVGQRQL 1429
|
170 180
....*....|....*....|....
gi 5734101 981 LSVALAFVGGSKVVILDEPTAGVD 1004
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD 1453
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
921-1032 |
3.97e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 3.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 921 HNVLfDMlTVEEHIWFYARLKGLSEKHvkaemeQMALDVGLPSSKLKSKTSQLSGG-MQR-KLSVAL-AFVGGSKVVILD 997
Cdd:TIGR00630 786 ADVL-DM-TVEEAYEFFEAVPSISRKL------QTLCDVGLGYIRLGQPATTLSGGeAQRiKLAKELsKRSTGRTLYILD 857
|
90 100 110
....*....|....*....|....*....|....*.
gi 5734101 998 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMD 1032
Cdd:TIGR00630 858 EPTTGLHFDDIKKLLEVLQRLVdKGNTVVVIEHNLD 893
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
959-1048 |
4.71e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 41.71 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 5734101 959 VGLPSSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEA 1034
Cdd:PRK15093 143 VGIKDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQML 222
|
90
....*....|....
gi 5734101 1035 DVLGDRIAIISHGK 1048
Cdd:PRK15093 223 SQWADKINVLYCGQ 236
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1986-2042 |
5.75e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 39.65 E-value: 5.75e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 5734101 1986 SGGNKRKLSTAMAL----IGGPPVVFLDEPTTGMDPK-ARRFLWNCALSVVKeGRSVVLTSH 2042
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRdGQALAEAILEHLVK-GAQVIVITH 139
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1972-2043 |
7.44e-03 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.61 E-value: 7.44e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 5734101 1972 LGLVKYGEKyAGNYSGGNKRKLSTAMALIGGP-PVVF-LDEPTTGMDPKARRFLWNCALSVVKEGRSVVLTSHS 2043
Cdd:cd03238 76 LGYLTLGQK-LSTLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
842-896 |
9.30e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 40.87 E-value: 9.30e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 5734101 842 QNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGT 896
Cdd:PRK11819 328 ENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT 380
|
|
| |
