|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2236 |
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: 2506.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1 MAWGSQLRLLLWKNLTFRRRQTCQLLLEVAWPLFIFLILISVRLSYPPYEQHECHFPNKAMPSAGTLPWVQGIICNANNP 80
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKAMPSAGMLPWLQGIFCNVNNP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 81 CFRYPTPGEAPGIVGNFNKSIVSRLFSDAQRLLLYSQRDTSMKDIHKVLGTLRQIENS---------NSSLKLRDFLVDN 151
Cdd:TIGR01257 81 CFQSPTPGESPGIVSNYNNSILARVYRDFQELLMDAPESQHLGQVWAELRTLSQFMDTlrthperiaGRGIRIRDILKDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 152 ETFSGFLHHNLSLPRPMVHRVTGATVSLHKvFLHGY-QLHLTNL-CNGSKLGEVIQLGDQELAK-----LCSLPRERLDA 224
Cdd:TIGR01257 161 EALTLFLMKNIGLSDSVVYLLVNSQVRPEQ-FAYGVpDLELKDIaCSEALLERFIIFSQRRGAQtvrdaLCSLSQGTLQW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 225 AERVLRSNMDILKpilaelnttspfpskeLAEATKTLLYSlgnlAQELFSMRSW----SDMR------------REVLYL 288
Cdd:TIGR01257 240 IEDTLYANVDFFK----------------LFHVLPTLLDS----RSQGINLRSWggilSDMSpriqefihrpsvQDLLWV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 289 T----NVNSSSSSTQIYQAVSRIVCGHPEGGGLKIKSLNWYEDNNYKALFGGNGTEEDAGTFYDNSTTPYCNDLMKNLES 364
Cdd:TIGR01257 300 TrpllQNGGPETFTQLMGILSDLLCGYPEGGGSRVFSFNWYEDNNYKAFLGIDSTRKDPIYSYDKRTTSFCNALIQSLES 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 365 SPLSRIIWKALKPLLVGKILYTPDTPVTRHVMAEVNKTFQELAVFHDLEGMWEELSPKIWTFMESSQEMDLVRTLLDSRG 444
Cdd:TIGR01257 380 NPLTKIAWRAAKPLLMGKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDKSTQMTMIRDTLQNPT 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 445 NDQFWEQQLEGLGWTAQDIVAFLAKHPEDAQDINGSVYTWREAFNETSQAIQTISRFMECVNLNKLEPVATEVGLINQSM 524
Cdd:TIGR01257 460 VKDFINRQLGEEGITAEAVLNFLYNGPREKQADDMTNFDWRDIFNITDRFLRLANQYLECLVLDKFESYDDEVQLTQRAL 539
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 525 RLLDERKFWAGIVFTGITPNSVELPHHVKYKIRMDIDNVERTNKIKDAYWDPGPRADPFEDMRYVWGGFAYLQDVVEQAI 604
Cdd:TIGR01257 540 SLLEENRFWAGVVFPDMYPWTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRADPVEDFRYIWGGFAYLQDMVEQGI 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 605 IRVQTGLEKKTGVYMQQMPYPCYVDDIFLRVMSRSMPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNGILWFS 684
Cdd:TIGR01257 620 TRSQMQAEPPVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIVLEKELRLKETLKNQGVSNAVIWCT 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 685 WFISSLIPLLVSASLLVVILKLGNLLPYSDPSVVFVFLSVFAVVTILQCFLLSTLFSRANLAAACGGILYFILYLPYVLC 764
Cdd:TIGR01257 700 WFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFFSKASLAAACSGVIYFTLYLPHILC 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 765 VAWQDYVGFNLKVFASLLSPVAFGFGCEYFALFEEQGIGVQWDNLFESLVEGDGFNLTTSVSMMLFDTFIYGVMTWYIEA 844
Cdd:TIGR01257 780 FAWQDRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEGDEFSFLLSMKMMLLDAALYGLLAWYLDQ 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 845 VFPGQYGIPRPWYFPCTKSYWFG--------EESDEKSHPGSSQ-------KGVSEIRMEEEPTHLKLGVSIQNLVKVYR 909
Cdd:TIGR01257 860 VFPGDYGTPLPWYFLLQESYWLGgegcstreERALEKTEPLTEEmedpehpEGINDSFFERELPGLVPGVCVKNLVKIFE 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLT 989
Cdd:TIGR01257 940 PSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLT 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 VEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGL-HHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1070 GIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVK--KDVESSLGSCRNSSS 1147
Cdd:TIGR01257 1099 SIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTPLFLKNCFGTGFYLTLVRkmKNIQSQRGGCEGTCS 1178
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1148 TVSnlKKEDSVSQSSSDAGLgsdhESDTLTIDVSAISNLIRKHVAEARLVEDIGHELTYVLPYEAAKEGAFVELFHEIDD 1227
Cdd:TIGR01257 1179 CTS--KGFSTRCPARVDEIT----PEQVLDGDVNELMDLVYHHVPEAKLVECIGQELIFLLPNKNFKQRAYASLFRELEE 1252
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1228 RLSDLGISSYGISETTLEEIFLKVAEESGVDAETSDGtlpARRNRRAFGDRQSCLRPfTEDDGVDPNDSDIDPESRETDL 1307
Cdd:TIGR01257 1253 TLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGG---AQQKRENANLRHPCSGP-TEKAGQTPQASHTCSPGQPAAH 1328
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1308 LSGM-----DGKGSYQVKGWKLTQQQFVALLWKRLLIAKRSRKGFFAQIVLPAVFVCIALVFSLIVPPFGKYPNLELQPW 1382
Cdd:TIGR01257 1329 PEGQpppepEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPW 1408
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1383 MYNEQYTFVSNDAPEDVSTQQLLNALTKDPGFGTRCMEGDPIPEMPCsVGEEEWTTASVPQTIMDLFQNGNWTMESPSPA 1462
Cdd:TIGR01257 1409 MYGQQYTFFSMDEPNSEHLEVLADVLLNKPGFGNRCLKEEWLPEYPC-GNSTPWKTPSVSPNITHLFQKQKWTAAHPSPS 1487
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1463 CQCSSDKIKKMLPVCPAGAGGLPPPQRRQNTADILQNLTGRNISDYLVKTYVQIIAKSLKNKIWVNEFRYGGFSLGAsRS 1542
Cdd:TIGR01257 1488 CRCSTREKLTMLPECPEGAGGLPPPQRTQRSTEILQDLTDRNISDFLVKTYPALIRSSLKSKFWVNEQRYGGISIGG-KL 1566
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1543 HALPPS-EEVNNAIEQMKKHLKLAKDSSADRFLSSLGRFMTGLDTKNNVKVWFNNKGWHAISSFLNVINNAILRANLQKG 1621
Cdd:TIGR01257 1567 PAIPITgEALVGFLSDLGQMMNVSGGPVTREASKEMPDFLKHLETEDNIKVWFNNKGWHALVSFLNVAHNAILRASLPKD 1646
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1622 ENPNKYGITAFNHPLNLTKQQLSEVALMTTSVDVLVSICVIFAMSFVPASFVVFLIQERVSKAKHLQFISGVKPVIYWLS 1701
Cdd:TIGR01257 1647 RDPEEYGITVISQPLNLTKEQLSEITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLT 1726
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1702 NFVWDMCNYVVPATLVIIIFICFQQKSYVSSTNLPVLALLLLLYGWSITPLMYPASFVFKIPSTAYVVLTSVNLFIGING 1781
Cdd:TIGR01257 1727 NFLWDIMNYAVSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINS 1806
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1782 SVATFVLELFTNNK-LNNINDILKSVFLIFPHFCLGRGLIDMVKNQAMADALERFGENRFISPLSWDLVGRNLFAMAVEG 1860
Cdd:TIGR01257 1807 SAITFVLELFENNRtLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGEEHSANPFQWDLIGKNLVAMAVEG 1886
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1861 VVFFLITVLIQYRFFIRPRAVKTKFLPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPRGE 1940
Cdd:TIGR01257 1887 VVYFLLTLLIQHHFFLSRWIAEPAKEPIFDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSPAVDRLCVGVRPGE 1966
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1941 CFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKE 2020
Cdd:TIGR01257 1967 CFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEE 2046
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2021 VGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLT 2100
Cdd:TIGR01257 2047 IEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLT 2126
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2101 SHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGDGYTIVVRIAGSN----PDLKPVQEFFGLAFPGSVLKEKHRNML 2176
Cdd:TIGR01257 2127 SHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllPDLNPVEQFFQGNFPGSVQRERHYNML 2206
|
2250 2260 2270 2280 2290 2300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2177 QYQLPSslSSLARIFSILSQSKKQLHIEDYSVSQTTLDQVFVNFAKDQSDDdhlKDLSLH 2236
Cdd:TIGR01257 2207 QFQVSS--SSLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTET---YDLPLH 2261
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
899-1119 |
8.62e-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: 362.98 E-value: 8.62e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLK 1119
Cdd:cd03263 160 PTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
1912-2132 |
1.16e-114 |
|
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: 362.59 E-value: 1.16e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSiIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLK 2132
Cdd:cd03263 161 TSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
899-1136 |
8.12e-83 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 271.94 E-value: 8.12e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:COG1131 1 IEVRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTD-AADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVKKDVE 1136
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLLEDVFLELTGEEAR 236
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
1912-2135 |
1.69e-74 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 248.05 E-value: 1.69e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG1131 1 IEVRGLTKRY--GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRF 2135
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
899-1109 |
9.66e-66 |
|
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: 9.66e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03230 1 IEVRNLSKRYGK--KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIwfyaclkglsekhvkvemeqmaldvglppsklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03230 79 PEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKkEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
901-1109 |
1.19e-61 |
|
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: 211.64 E-value: 1.19e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQ 980
Cdd:COG4555 4 VENLSKKYGK--VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEE-FLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 1061 AGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG4555 161 NGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
899-1119 |
1.24e-59 |
|
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: 204.91 E-value: 1.24e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03265 1 IEVENLVKKY--GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADR-LVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1059 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLK 1119
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
906-1195 |
1.24e-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: 202.23 E-value: 1.24e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 906 KVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLF 985
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELG-EAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1066 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGtgyyltlvkKDVesslgsCRN 1144
Cdd:TIGR01188 158 RTRRAIWDYIRALKEeGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG---------KDT------LES 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1145 SSSTVSNLKKEDSVSQS----SSDAGLGSDHESDTLTIDVSAISNLIRKHVAEAR 1195
Cdd:TIGR01188 223 RPRDIQSLKVEVSMLIAelgeTGLGLLAVTVDSDRIKILVPDGDETVPEIVEAAI 277
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
1912-2132 |
1.34e-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: 199.13 E-value: 1.34e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03265 1 IEVENLVKKYGDFE--AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03265 79 FQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLK 2132
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
1927-2220 |
2.59e-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: 201.46 E-value: 2.59e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGREH 2006
Cdd:TIGR01188 7 KAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTGREN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2007 VEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNC 2086
Cdd:TIGR01188 87 LEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRAIWDY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2087 ALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGDGYTIVVRIAGSnpDLKPVQEFFGLAFPGS 2166
Cdd:TIGR01188 167 IRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLESRPRDIQ--SLKVEVSMLIAELGET 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2167 VL--KEKHRNMLQYQLPSSLSS--LARIFSILsqSKKQLHIEDYSVSQTTLDQVFVNF 2220
Cdd:TIGR01188 245 GLglLAVTVDSDRIKILVPDGDetVPEIVEAA--IRNGIRIRSISTERPSLDDVFLKL 300
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
1912-2122 |
1.85e-55 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 191.07 E-value: 1.85e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03230 1 IEVRNLSKRY--GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEffallrgvpekevgkvgewairklgllkygekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
899-1109 |
1.07e-53 |
|
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: 187.40 E-value: 1.07e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMkvAVDGLALNFYEGqITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRA-KKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03264 157 PTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1912-2137 |
1.46e-53 |
|
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: 188.53 E-value: 1.46e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG4555 2 IEVENLSKKY--GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGD 2137
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 ... |
900-1108 |
2.88e-47 |
|
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: 169.18 E-value: 2.88e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVC 978
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQH-NVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03225 81 FQNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLkAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
1912-2123 |
4.65e-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: 165.44 E-value: 4.65e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGeCFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03264 1 LQLENLTKRYGKKR--ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2072 TTGMDPKAR-RF--LwncaLSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFR 2123
Cdd:cd03264 158 TAGLDPEERiRFrnL----LSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1108 |
4.93e-46 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 168.75 E-value: 4.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 978
Cdd:COG4152 2 LELKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGL-GDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:COG4152 156 PFSGLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGR 206
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
899-1114 |
7.91e-46 |
|
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: 165.58 E-value: 7.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:COG1122 1 IELENLSFSYPGG-TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQH--NVLFdMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLppSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:COG1122 80 VFQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGL--EHLADRpPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1055 ILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
899-1109 |
1.18e-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: 1.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQnLGVC 978
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-IGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVemeqmALD-VGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDE-----VLDvVGLKDSA-KKKVKGFSLGMKQRLGIALALLGNPDLLILD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03268 152 EPTNGLDPDGIKELRELILSLRdQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
899-1113 |
6.54e-45 |
|
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: 162.54 E-value: 6.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 976
Cdd:cd03266 2 ITADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEEL-LDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
916-1061 |
1.40e-43 |
|
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: 156.27 E-value: 1.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-RQNLGVCPQHNVLFDMLTVEEHI 994
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 995 WFYACLKGLSEKHVKVEMEQMALDVGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
899-1114 |
2.68e-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: 158.43 E-value: 2.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:cd03261 1 IELRGLTKSFGG--RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMLTVEEHIWFYaclkgLSEKHVKVE-------MEQMALdVGLPPSKLKsKTSQLSGGMQRKLSVALAF 1047
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFP-----LREHTRLSEeeireivLEKLEA-VGLRGAEDL-YPAELSGGMKKRVALARAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:cd03261 152 ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGT 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
899-1114 |
4.39e-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: 158.23 E-value: 4.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:cd03295 1 IEFENVTKRYGGG-KKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADRyPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
899-1114 |
5.41e-43 |
|
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: 157.83 E-value: 5.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:COG1127 6 IEVRNLTKSFGD--RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMLTVEEHIWFYacLK---GLSEKhvkvEMEQMALD----VGLPPSKLKsKTSQLSGGMQRKLSVALAF 1047
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFP--LRehtDLSEA----EIRELVLEklelVGLPGAADK-MPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
899-1109 |
2.24e-42 |
|
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: 154.98 E-value: 2.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03259 1 LELKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEG-LLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1059 PTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03259 157 PLSALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1911-2126 |
1.63e-41 |
|
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: 152.91 E-value: 1.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNM 1988
Cdd:cd03266 1 MITADALTKRFRDVKKTvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03266 81 GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2069 DEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
1912-2121 |
7.93e-41 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 150.45 E-value: 7.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNiHEVHQNMGYC 1991
Cdd:cd03268 1 LKTNDLTKTY--GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN-IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVgewaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03268 78 IEAPGFYPNLTARENLRLLARLLGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGK 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
899-1108 |
1.21e-40 |
|
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: 150.12 E-value: 1.21e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstIRQNLGVC 978
Cdd:cd03269 1 LEVENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSE-YANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELaRAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
899-1105 |
1.37e-40 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 150.31 E-value: 1.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDG--MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstIRQNLG 976
Cdd:cd03293 1 LEVRNVSKTYGGGggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG----PGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGF-ENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEADILGDRIAIIS 1105
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
899-1109 |
2.65e-40 |
|
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: 149.18 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 -QNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:cd03255 81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADiLGDRIAIISHGKL 1109
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
899-1101 |
3.85e-40 |
|
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: 148.40 E-value: 3.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:COG4133 3 LEAENLSCRRGE--RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEmeqMALD-VGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAID---EALEaVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHhmDEADILGDRI 1101
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLaRGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
900-1108 |
1.86e-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: 144.69 E-value: 1.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVC 978
Cdd:cd00267 1 EIENLSFRYGG--RTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQhnvlfdmltveehiwfyaclkglsekhvkvemeqmaldvglppsklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
899-1108 |
2.66e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 149.57 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKvEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVFGRYFGLSAAAAR-ALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1059 PTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1911-2121 |
7.82e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 148.03 E-value: 7.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGY 1990
Cdd:PRK13537 7 PIDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELLTGREHVEFFALLRGVPEKevgkvgewAIRKL--GLLKYG------EKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVFGRYFGLSAA--------AARALvpPLLEFAklenkaDAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2063 PPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
897-1108 |
1.40e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 148.44 E-value: 1.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG 976
Cdd:PRK13536 40 VAIDLAGVSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMaLDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13536 118 VVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSL-LEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1115 |
1.24e-37 |
|
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: 150.05 E-value: 1.24e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTI 971
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 972 RQNLGVCPQH--NVLFDMLTVEEHIWF-YACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG1123 341 RRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1115
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
888-1107 |
1.80e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 142.54 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 888 MEEEPTHLklgvSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 965
Cdd:COG1116 1 MSAAAPAL----ELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 966 SemstIRQNLGVCPQHNVLFDMLTVEEHIWFyaclkGLSEKHV-KVEMEQMALD----VGLPPsKLKSKTSQLSGGMQRK 1040
Cdd:COG1116 77 G----PGPDRGVVFQEPALLPWLTVLDNVAL-----GLELRGVpKAERRERAREllelVGLAG-FEDAYPHQLSGGMRQR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHG 1107
Cdd:COG1116 147 VAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2226 |
2.16e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 143.71 E-value: 2.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlsnIHEVHQNMGY 1990
Cdd:COG4152 1 MLELKGLTKRFGDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL---DPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPqfdaitE---L---LTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:COG4152 76 LP------EergLypkMKVGEQLVYLARLKGLSKAEAKRrADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2064 PVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGdGYTIVV 2143
Cdd:COG4152 149 ELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2144 RIAGSNPDLKpvqeffglAFPGSVLKEKHRNMLQYQLPSSLSSlARIFSILSQskkQLHIEDYSVSQTTLDQVFVNFAKD 2223
Cdd:COG4152 228 EADGDAGWLR--------ALPGVTVVEEDGDGAELKLEDGADA-QELLRALLA---RGPVREFEEVRPSLNEIFIEVVGE 295
|
...
gi 507682765 2224 QSD 2226
Cdd:COG4152 296 KAE 298
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
899-1109 |
3.17e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 3.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsERELARLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 -QNLGVCPQ-HNvLFDMLTVEEHIWFYACLKGLSEKhvkvEMEQMALD----VGLPpSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:COG1136 85 rRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRK----ERRERAREllerVGLG-DRLDHRPSQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADIlGDRIAIISHGKL 1109
Cdd:COG1136 159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAAR-ADRVIRLRDGRI 222
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
1912-2126 |
1.07e-36 |
|
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: 138.57 E-value: 1.07e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSnihEVHQNMGYC 1991
Cdd:cd03269 1 LEVENVTKRFGRVT--ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDI---AARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGK-VGEWaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRrIDEW-LERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2071 PTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1912-2102 |
1.52e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 138.00 E-value: 1.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKiyRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:COG4133 3 LEAENLSC--RRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEvGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADR-EAIDE-ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
899-1109 |
2.19e-36 |
|
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: 138.41 E-value: 2.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03257 2 LEVKNLSVSFptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 QNLGVCPQH--NVLFDMLTVEEHI----WFYACLKGLSEKHVKVEMEQMAldVGLPPSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:cd03257 82 KEIQMVFQDpmSSLNPRMTIGEQIaeplRIHGKLSKKEARKEAVLLLLVG--VGLPEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
899-1108 |
2.73e-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: 135.97 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIwfyaclkglsekhvkvemeqmaldvglppsklksktsqLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03228 81 VPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGK 1108
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
901-1108 |
1.15e-35 |
|
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: 134.62 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGV 977
Cdd:cd03229 3 LKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIwfyaclkglsekhvkvemeqmaldvGLPpsklksktsqLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03229 81 VFQDFALFPHLTVLENI-------------------------ALG----------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1058 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd03229 126 EPTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1912-2151 |
3.44e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 138.81 E-value: 3.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKrkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:PRK13536 42 IDLAGVSKSYGDK--AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL-KNRFGdgyTIVVRIAGSNP 2150
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALiDEHIG---CQVIEIYGGDP 276
|
.
gi 507682765 2151 D 2151
Cdd:PRK13536 277 H 277
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
900-1114 |
3.45e-35 |
|
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: 135.26 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP 979
Cdd:cd03219 2 EVRGLTKRF-GGLV-ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 980 --QHNVLFDMLTVEE------------HIWFYACLKGLSEKHVKVEmeqMALD-VGLPPsKLKSKTSQLSGGMQRKLSVA 1044
Cdd:cd03219 80 tfQIPRLFPELTVLEnvmvaaqartgsGLLLARARREEREARERAE---ELLErVGLAD-LADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRErGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGT 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
899-1109 |
9.55e-35 |
|
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: 133.86 E-value: 9.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:cd03258 2 IELKNVSKVFGDTGGkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 QNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03258 82 RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGL-EDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
1913-2121 |
1.66e-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: 132.59 E-value: 1.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:cd03225 1 ELKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03225 81 FQ-NPDDQFFgpTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2070 EPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1589-1869 |
1.98e-34 |
|
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: 136.37 E-value: 1.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1589 NVKVWFNNKGWHAISSFLNVINNAILRANLQKGENPNKYGITAFNHPLNLTKQQLSEvalmTTSVDVLVSICVIFAMSFV 1668
Cdd:pfam12698 100 TVTVYINSSNLLVSKLILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQ----SGYAYYLVGLILMIIILIG 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1669 PASFVVFLIQERVSKAKHLQFISGVKPVIYWLSNFVWDMCNYVVPatLVIIIFICFQQksYVSSTNLPVLALLLLLYGWS 1748
Cdd:pfam12698 176 AAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQ--LLIILLLLFGI--GIPFGNLGLLLLLFLLYGLA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1749 ITPLMYPASFVFKIPSTAYVVLTSVNLFIGInGSVATFVlelftnnkLNNINDILKSVFLIFPHFCLGRGLIDMVKNQAM 1828
Cdd:pfam12698 252 YIALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFP--------LEDPPSFLQWIFSIIPFFSPIDGLLRLIYGDSL 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 507682765 1829 ADalerfgenrfisplswdlVGRNLFAMAVEGVVFFLITVL 1869
Cdd:pfam12698 323 WE------------------IAPSLIILLLFAVVLLLLALL 345
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
900-1110 |
2.66e-34 |
|
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: 131.89 E-value: 2.66e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVCP 979
Cdd:cd03235 1 EVEDLTVSYGG--HPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 980 QH-NVLFDM-LTVEE--------HIWFyacLKGLSEKHVKVEMEqmALD-VGLppSKLKSKT-SQLSGGMQRKLSVALAF 1047
Cdd:cd03235 75 QRrSIDRDFpISVRDvvlmglygHKGL---FRRLSKADKAKVDE--ALErVGL--SELADRQiGELSGGQQQRVLLARAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLC 1110
Cdd:cd03235 148 VQDPDLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLLLNRTVVA 211
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
899-1114 |
7.55e-34 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 132.09 E-value: 7.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLG 976
Cdd:COG1120 2 LEAENLSVGYGG--RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL-ASLSRreLARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEE--------HI-WFyaclKGLSEKHVKVEMEQMALdVGLppSKLKSKT-SQLSGGMQRKLSVALA 1046
Cdd:COG1120 79 YVPQEPPAPFGLTVRElvalgrypHLgLF----GRPSAEDREAVEEALER-TGL--EHLADRPvDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
899-1111 |
9.93e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 131.36 E-value: 9.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 978
Cdd:COG1121 7 IELENLTVSYGG--RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQH-NVLFDM-LTVEE--------HIWFyacLKGLSEKHVKVEMEqmALD-VGLppSKLKSKT-SQLSGGMQRKLSVALA 1046
Cdd:COG1121 81 PQRaEVDWDFpITVRDvvlmgrygRRGL---FRRPSRADREAVDE--ALErVGL--EDLADRPiGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCC 1111
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRrEGKTILVVTHDLGAVREYFDRVLLLNRGLVAH 219
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
914-1108 |
1.39e-33 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 141.80 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTiRQNLGVCPQHNVLFDMLTVEE 992
Cdd:NF033858 280 TAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDIAT-RRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 993 HIWFYACLKGLSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1072
Cdd:NF033858 359 NLELHARLFHLPAAEIAARVAEMLERFDLADV-ADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFW 437
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 1073 ELL--LKYRQGRTIILSTHHMDEADiLGDRIAIISHGK 1108
Cdd:NF033858 438 RLLieLSREDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
899-1109 |
2.49e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.40 E-value: 2.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQ 973
Cdd:COG2884 2 IRFENVSKRYPGG-REALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 974 NLGVCPQ-HNVLFDMlTVEEHIWFyaCLK--GLSEKHVKVEMEQmALD-VGLPpSKLKSKTSQLSGGMQRKLSVALAFVG 1049
Cdd:COG2884 80 RIGVVFQdFRLLPDR-TVYENVAL--PLRvtGKSRKEIRRRVRE-VLDlVGLS-DKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
1913-2121 |
2.68e-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: 126.98 E-value: 2.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSN-IHEVHQNMGYC 1991
Cdd:cd00267 1 EIENLSFRY--GGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLpLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFdaitelltgrehveffallrgvpekevgkvgewairklgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd00267 79 PQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
1912-2121 |
3.99e-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: 128.99 E-value: 3.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL-SNIHEVHQNMGY 1990
Cdd:COG1122 1 IELENLSFSYPGGT-PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITkKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQF--DAITELlTGREHVEFfALL-RGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:COG1122 80 VFQNpdDQLFAP-TVEEDVAF-GPEnLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2068 LDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGR 211
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
900-1109 |
5.18e-33 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 128.01 E-value: 5.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGV 977
Cdd:COG4619 2 ELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHI--WFYACLKGLSEKHVKVEMEQmaldVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:COG4619 79 VPQEPALWGG-TVRDNLpfPFQLRERKFDRERALELLER----LGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
899-1114 |
8.47e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 130.17 E-value: 8.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE---MSTIR 972
Cdd:PRK13637 3 IKIENLTHIYMEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 QNLGVC---PQHNvLFDMlTVEEHIWFYACLKGLSEKHVKVEM-EQMALdVGLPPSKLKSKTS-QLSGGMQRKLSVALAF 1047
Cdd:PRK13637 83 KKVGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVkRAMNI-VGLDYEDYKDKSPfELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
901-1108 |
1.33e-32 |
|
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: 128.07 E-value: 1.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----------RSEMS 969
Cdd:cd03256 3 VENLSKTYPNG-KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkgkalrqlRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNLGVCPQHNVLFDMLT--VEEHIWFYACLKGLSEKHVKVEMEqmALD-VGLpPSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSgrLGRRSTWRSLFGLFPKEEKQRALA--ALErVGL-LDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
900-1108 |
1.96e-32 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 126.78 E-value: 1.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 976
Cdd:cd03224 2 EVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPherARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFYACLkgLSEKHVKVEMEQMaldVGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERV---YELFPrlkERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRdEGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
899-1114 |
3.64e-32 |
|
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: 126.58 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1059 PTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:cd03300 157 PLGALDLKLRKDMQLELkrLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
881-1113 |
3.97e-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: 127.37 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 881 KGVSEI---RMEEEPTHLKLGVSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA 957
Cdd:cd03294 4 KGLYKIfgkNPQKAFKLLAKGKSKEEILK--KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 958 YILGKDI----RSEMSTIRQN-LGVCPQHNVLFDMLTVEEHIWFyaclkGLSEKHV-KVEMEQMALD----VGLPPSKlK 1027
Cdd:cd03294 82 LIDGQDIaamsRKELRELRRKkISMVFQSFALLPHRTVLENVAF-----GLEVQGVpRAEREERAAEalelVGLEGWE-H 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1028 SKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIIS 1105
Cdd:cd03294 156 KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMK 235
|
....*...
gi 507682765 1106 HGKLCCVG 1113
Cdd:cd03294 236 DGRLVQVG 243
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
899-1128 |
5.33e-32 |
|
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: 126.12 E-value: 5.33e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTiRQNLGV 977
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 C--PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:cd03218 78 GylPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLR-KSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEADILGDRIAIISHGKLCCVGSS-LFLKNQLGTGYYL 1128
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKD-RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPeEIAANELVRKVYL 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
899-1114 |
6.31e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 127.03 E-value: 6.31e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGV 977
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQH-NVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13632 88 IFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGM-EDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEAdILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEA-ILADKVIVFSEGKLIAQGK 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
899-1109 |
6.78e-32 |
|
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: 125.37 E-value: 6.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-----PTSGTAYILGKDIRSEMSTI-- 971
Cdd:cd03260 1 IELRDLNVYYGD--KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDVle 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 972 -RQNLGVCPQHNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALD-VGLPPS-KLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:cd03260 79 lRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRkAALWDEvKDRLHALGLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
899-1109 |
7.52e-32 |
|
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: 132.72 E-value: 7.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT---SGTAYILGKDIRSEMSTIR-QN 974
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQH-NVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:COG1123 85 IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRI 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
897-1128 |
1.05e-31 |
|
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: 132.97 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEmSTIRQN 974
Cdd:COG4987 332 PSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDE-DDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMlTVEEHIWFyAClKGLSEKhvkvEMEQMALDVGLPP----------SKLKSKTSQLSGGMQRKLSVA 1044
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRL-AR-PDATDE----ELWAALERVGLGDwlaalpdgldTWLGEGGRRLSGGERRRLALA 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1045 LAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKNQLGT 1124
Cdd:COG4987 484 RALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELLAQNGR 562
|
....
gi 507682765 1125 GYYL 1128
Cdd:COG4987 563 YRQL 566
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
914-1109 |
2.65e-31 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 124.77 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFDMLTVE 991
Cdd:COG0411 18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 992 EHI-----------WFYACLKGLSEKHVKVEMEQMALD----VGLPPsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:COG0411 98 ENVlvaaharlgrgLLAALLRLPRARREEREARERAEEllerVGLAD-RADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYR--QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG0411 177 DEPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
897-1109 |
1.46e-30 |
|
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: 122.06 E-value: 1.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVK-VYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNL 975
Cdd:cd03267 19 LIGSLKSLFKrKYRE--VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 G-VCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMA--LDVGlppSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03267 97 GvVFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSelLDLE---ELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
900-1115 |
1.97e-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: 121.61 E-value: 1.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV-- 977
Cdd:TIGR04406 3 VAENLIKSY--KKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIgy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIwfYACL---KGLSEKHVKVEMEQMALDVGLppSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKV 1053
Cdd:TIGR04406 81 LPQEASIFRKLTVEENI--MAVLeirKDLDRAEREERLEALLEEFQI--SHLRDNKAMsLSGGERRRVEIARALATNPKF 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1115
Cdd:TIGR04406 157 ILLDEPFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1109 |
3.40e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 123.66 E-value: 3.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYR-----DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI 959
Cdd:COG4586 2 IEVENLSKTYRvyekePGLKgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 960 LGKDIRSEMSTIRQNLGVcpqhnV-------LFDmLTVEEHIWFYACLKGLSEKHVKVEMEQMA--LDVGlppSKLKSKT 1030
Cdd:COG4586 82 LGYVPFKRRKEFARRIGV-----VfgqrsqlWWD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVelLDLG---ELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1031 SQLSGGmQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDeaDI--LGDRIAIIS 1105
Cdd:COG4586 153 RQLSLG-QRmRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMD--DIeaLCDRVIVID 229
|
....
gi 507682765 1106 HGKL 1109
Cdd:COG4586 230 HGRI 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2216 |
5.31e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 122.89 E-value: 5.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP-------------------AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNA- 1970
Cdd:COG4586 1 IIEVENLSKTYRVYEKEpglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1971 ------FLNKNSILSNIHEVhqnMGycpQ-----FDaitelLTGREHVEFFALLRGVPEKEVGKvgewAIRKL-GLLKYG 2038
Cdd:COG4586 81 vlgyvpFKRRKEFARRIGVV---FG---QrsqlwWD-----LPAIDSFRLLKAIYRIPDAEYKK----RLDELvELLDLG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2039 EKYagnysggNK--RKLS--------TAMALIGGPPVVFLDEPTTGMDPKA----RRFlwncalsiIKE-----GRSVVL 2099
Cdd:COG4586 146 ELL-------DTpvRQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSkeaiREF--------LKEynrerGTTILL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2100 TSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGDGYTIVVRIAGSNPDLKpvqeffgLAFPGSVLK-EKHRnmLQY 2178
Cdd:COG4586 211 TSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLE-------LPRGGEVIErEGNR--VRL 281
|
330 340 350
....*....|....*....|....*....|....*...
gi 507682765 2179 QLPSSLsSLARIFSILSQskkQLHIEDYSVSQTTLDQV 2216
Cdd:COG4586 282 EVDPRE-SLAEVLARLLA---RYPVRDLTIEEPPIEEV 315
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
900-1113 |
6.82e-30 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 117.92 E-value: 6.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMST--IRQNLGV 977
Cdd:cd03214 1 EVENLSVGYGG--RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPkeLARKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLtveehiwfyaclkGLSEKHVkvemeqmaldvglppsklksktSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03214 78 VPQALELLGLA-------------HLADRPF----------------------NELSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1058 EPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:cd03214 123 EPTSHLDIAHQIELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
901-1113 |
1.03e-29 |
|
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: 119.36 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYRDgmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 980
Cdd:cd03299 3 VENLSKDWKE---FKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGID-HLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1061 AGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:cd03299 158 SALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVG 212
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
899-1114 |
1.24e-29 |
|
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: 126.80 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:COG4988 337 IELEDVSFSYPGG-RPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIWFYAclKGLSEKhvkvEMEQMALDVGLP------PSKLKSKT----SQLSGG-MQRkLSVALA 1046
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGR--PDASDE----ELEAALEAAGLDefvaalPDGLDTPLgeggRGLSGGqAQR-LALARA 487
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGS 1114
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDGRIVEQGT 554
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
899-1109 |
1.95e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 119.14 E-value: 1.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGM--KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNL 975
Cdd:COG1124 2 LEVRNLSVSYGQGGrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQH--NVLFDMLTVEEHIwfYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGG-MQRklsVAL--AFVGG 1050
Cdd:COG1124 82 QMVFQDpyASLHPRHTVDRIL--AEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGqRQR---VAIarALILE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG1124 157 PELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
1912-2121 |
2.16e-29 |
|
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: 117.62 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNihEVHQ-NMGY 1990
Cdd:cd03259 1 LELKGLSKTYGSVR--ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV--PPERrNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELLTGREHVEFfAL-LRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2070 EPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03259 156 EPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGR 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
899-1109 |
3.29e-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: 115.60 E-value: 3.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 978
Cdd:cd03216 1 LELRGITKRF--GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 pqhnvlfdmLTVeehiwfyaclkglsekhvkvemeqmaldvglppsklksktSQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03216 78 ---------AMV----------------------------------------YQLSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1059 PTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03216 109 PTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
902-1109 |
2.18e-28 |
|
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: 114.81 E-value: 2.18e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGV 977
Cdd:cd03292 4 INVTKTY-PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKvEMEQMALD-VGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03292 83 VFQDFRLLPDRNVYENVAFALEVTGVPPREIR-KRVPAALElVGLS-HKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1911-2129 |
2.94e-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: 115.91 E-value: 2.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMG 1989
Cdd:COG1120 1 MLEAENLS--VGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAITELLTGREHVE-----FFALLRGVPEKEVGKVgEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVAlgrypHLGLFGRPSAEDREAV-EEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2065 VVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQ 2129
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEV----LELLRRlarerGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPE 223
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
899-1113 |
6.22e-28 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 113.50 E-value: 6.22e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMA--LDVGlppSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAelLQIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1057 DEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:cd03301 155 DEPLSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
900-1115 |
1.59e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 113.20 E-value: 1.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSemstiR 972
Cdd:COG1137 5 EAENLVKSYGK--RTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIthlpmhkRA-----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 QNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLppSKL-KSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGI--THLrKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQgRTI-ILST-HHMDEadILG--DRIAIISHGKLCCVGSS 1115
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKE-RGIgVLITdHNVRE--TLGicDRAYIISEGKVLAEGTP 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
899-1114 |
2.07e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 2.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLG 976
Cdd:COG3845 6 LELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIW--------FYACLKGLSEKhVKVEMEQMALDVglPPSKlksKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVlgleptkgGRLDRKAARAR-IRELSERYGLDV--DPDA---KVEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLccVGS 1114
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAaEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1911-2130 |
2.35e-27 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 112.88 E-value: 2.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKrkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKnsilSNIHEVHQNMGY 1990
Cdd:COG1121 6 AIELENLTVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITEL--LTGREHVEF-----FALLRGVPEKEVGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:COG1121 80 VPQRAEVDWDfpITVRDVVLMgrygrRGLFRRPSRADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2064 PVVFLDEPTTGMDPKARRFLwncaLSIIKE----GRSVVLTSHSMEECEALCTRmAIMVNGKFRCLGSVQH 2130
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEAL----YELLRElrreGKTILVVTHDLGAVREYFDR-VLLLNRGLVAHGPPEE 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
899-1121 |
2.54e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 113.68 E-value: 2.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGV 977
Cdd:PRK13647 5 IEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQ--HNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQmALD-VGLppSKLKSKTS-QLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK13647 84 VFQdpDDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEE-ALKaVRM--WDFRDKPPyHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQ 1121
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
908-1114 |
4.61e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 4.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLAL-----NFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-----MSTIRQNLGV 977
Cdd:PRK13634 10 HRYQYKTPFERRALydvnvSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkkLKPLRKKVGI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 C---PQHNvLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:PRK13634 90 VfqfPEHQ-LFEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1055 ILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13634 168 VLDEPTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGT 229
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
899-1114 |
6.09e-27 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 114.79 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:COG3839 4 LELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGG-MQRklsVAL--AFVGGSKVVI 1055
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGqRQR---VALgrALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1056 LDEPTAGVDPYSR---RGiwEL--LLKyRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:COG3839 157 LDEPLSNLDAKLRvemRA--EIkrLHR-RLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGT 217
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
891-1128 |
7.74e-27 |
|
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: 119.17 E-value: 7.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 891 EPTHLKLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMS 969
Cdd:COG2274 466 SLPRLKGDIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPA 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNLGVCPQHNVLFDMlTVEEHIWFYAclKGLSEKhvkvEMEQMALDVGLP------PSKLKSK----TSQLSGGMQR 1039
Cdd:COG2274 546 SLRRQIGVVLQDVFLFSG-TIRENITLGD--PDATDE----EIIEAARLAGLHdfiealPMGYDTVvgegGSNLSGGQRQ 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1040 KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAdilgDRIAIISHGKLCCVGSSL 1116
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHrlsTIRLA----DRIIVLDKGRIVEDGTHE 694
|
250
....*....|..
gi 507682765 1117 FLKNQLGTGYYL 1128
Cdd:COG2274 695 ELLARKGLYAEL 706
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
897-1109 |
9.20e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.62 E-value: 9.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--- 970
Cdd:PRK13641 1 MSIKFENVDYIYSPGTpmeKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 --IRQNLGVCPQ--HNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK13641 81 kkLRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1911-2131 |
1.02e-26 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 116.93 E-value: 1.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGNAFLNKNSIL-SNIHEVHQ 1986
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLeLSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQfDAITEL--LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:COG1123 84 RIGMVFQ-DPMTQLnpVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2065 VVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:COG1123 163 LLIADEPTTALDVTTQAEI----LDLLRElqrerGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1929-2073 |
1.03e-26 |
|
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: 107.73 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1929 VDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHV 2007
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2008 EFFALLRGVPEKEVGKVGEWAIRKLGLLKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2073
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
908-1094 |
1.10e-26 |
|
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: 109.05 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 982
Cdd:TIGR01166 1 YPGGPEV-LKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 983 VLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLppSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGA--SGLRERpTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156
|
170 180 190
....*....|....*....|....*....|....
gi 507682765 1062 GVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEA 1094
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRaEGMTVVISTHDVDLA 190
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
897-1133 |
1.50e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 111.76 E-value: 1.50e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EM 968
Cdd:PRK13649 1 MGINLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 STIRQNLGVCPQ--HNVLFDMlTVEEHIWFYACLKGLS-EKHVKVEMEQMALdVGLPPSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:PRK13649 81 KQIRKKVGLVFQfpESQLFEE-TVLKDVAFGPQNFGVSqEEAEALAREKLAL-VGISESLFEKNPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--------SL 1116
Cdd:PRK13649 159 ILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKpkdifqdvDF 238
|
250 260
....*....|....*....|.
gi 507682765 1117 FLKNQLG----TGYYLTLVKK 1133
Cdd:PRK13649 239 LEEKQLGvpkiTKFAQRLADR 259
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
1912-2121 |
1.51e-26 |
|
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: 109.89 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRR--KRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIHEV----- 1984
Cdd:cd03255 1 IELKNLSKTYGGggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDI-SKLSEKelaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 -HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2064 PVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEEcEALCTRMAIMVNGK 2121
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPEL-AEYADRIIELRDGK 217
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
897-1114 |
2.07e-26 |
|
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: 110.12 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLG 976
Cdd:cd03296 1 MSIEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFyaclkGLSEKHV-----KVEMEQMALD----VGLppSKLKSK-TSQLSGGMQRKLSVALA 1046
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAF-----GLRVKPRserppEAEIRAKVHEllklVQL--DWLADRyPAQLSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGI--WELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
903-1109 |
2.11e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.94 E-value: 2.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 903 NLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCP 979
Cdd:PRK13639 6 DLKYSYPDG-TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 980 QH--NVLFdMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGL------PPsklksktSQLSGGMQRKLSVALAFVGGS 1051
Cdd:PRK13639 85 QNpdDQLF-APTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMegfenkPP-------HHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
1912-2133 |
2.92e-26 |
|
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: 109.17 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHE-VHQNMG 1989
Cdd:cd03218 1 LRAENLSKRY--GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKlPMHKrARLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03218 79 YLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2070 EPTTGMDPKARRFLWNcalsIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:cd03218 159 EPFAGVDPIAVQDIQK----IIKIlkdrGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
899-1136 |
4.63e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 110.25 E-value: 4.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMST 970
Cdd:PRK13646 3 IRFDNVSYTYQKGTpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 IRQNLGVCPQ--HNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKNQLGT 1124
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSpkELFKDKKKLA 241
|
250
....*....|....*..
gi 507682765 1125 GYYLTL-----VKKDVE 1136
Cdd:PRK13646 242 DWHIGLpeivqLQYDFE 258
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
918-1109 |
8.12e-26 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 107.74 E-value: 8.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEmsTIRQNLGVCPQHNVLFDMLTVEEHI 994
Cdd:cd03234 25 DVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 995 WFYACLKG---LSEKHVKVEMEQMAL-DVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:cd03234 103 TYTAILRLprkSSDAIRKKRVEDVLLrDLALTRIG-GNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507682765 1071 IWELLLKY-RQGRTIILSTHHmDEADI--LGDRIAIISHGKL 1109
Cdd:cd03234 182 LVSTLSQLaRRNRIVILTIHQ-PRSDLfrLFDRILLLSSGEI 222
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
900-1109 |
1.02e-25 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 106.96 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-----RSEMSTIRQN 974
Cdd:cd03226 1 RIENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 lgvcPQHNVLFDmlTVEEHIwfYACLKGLSEKHVKVE--MEQMALdvglppSKLKSKTSQ-LSGGMQRKLSVALAFVGGS 1051
Cdd:cd03226 80 ----VDYQLFTD--SVREEL--LLGLKELDAGNEQAEtvLKDLDL------YALKERHPLsLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03226 146 DLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
915-1109 |
3.07e-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: 104.82 E-value: 3.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC-----PQHNVLFDMLT 989
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAyvpedRKREGLVLDLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 VEEHIwfyaclkglsekhvkvemeqmALdvglppsklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:cd03215 95 VAENI---------------------AL------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKA 141
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 1070 GIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03215 142 EIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1912-2133 |
3.35e-25 |
|
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: 106.37 E-value: 3.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEV------ 1984
Cdd:cd03219 1 LEVRGLTKRFGGLV--ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGlPPHEIarlgig 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 --HQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWA---IRKLGLLKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
923-1109 |
5.88e-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: 104.17 E-value: 5.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 923 FYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTAYILGKDirSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYACL 1000
Cdd:cd03213 32 AKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRP--LDKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1001 KGLSekhvkvemeqmaldvglppsklksktsqlsGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ 1080
Cdd:cd03213 110 RGLS------------------------------GGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLAD 159
|
170 180 190
....*....|....*....|....*....|..
gi 507682765 1081 -GRTIILSTHHMdEADILG--DRIAIISHGKL 1109
Cdd:cd03213 160 tGRTIICSIHQP-SSEIFElfDKLLLLSQGRV 190
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
908-1109 |
8.42e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 104.59 E-value: 8.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF- 985
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 ----DMLTV------EEHIWFYACLKGLSE---KHVKvemeQMALDVGlppsklkSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAELAGVTDfvnKHPN----GLDLQIG-------ERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKL 1109
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
908-1130 |
1.07e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.47 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNLGVCPQH--N 982
Cdd:PRK13636 15 YSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 983 VLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSkTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:PRK13636 94 QLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKP-THCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAG 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1063 VDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG--SSLFLKNQLGTGYYLTL 1130
Cdd:PRK13636 172 LDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGnpKEVFAEKEMLRKVNLRL 243
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
900-1108 |
1.45e-24 |
|
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: 104.68 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMST---IRQNLG 976
Cdd:COG0410 5 EVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-LPPhriARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFyACLKGLSEKHVKVEMEQMaldVGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:COG0410 82 YVPEGRRIFPSLTVEENLLL-GAYARRDRAEVRADLERV---YELFPrlkERRRQRAGTLSGGEQQMLAIGRALMSRPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:COG0410 158 LLLDEPSLGLAPLIVEEIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
899-1109 |
1.59e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 107.09 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG1135 2 IELENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 QNLGVCPQH-NvLFDMLTVEEHIWFyaCLK--GLS--EKHVKVEmEQMALdVGLPpSKLKSKTSQLSGGMQRKLSVALAF 1047
Cdd:COG1135 82 RKIGMIFQHfN-LLSSRTVAENVAL--PLEiaGVPkaEIRKRVA-ELLEL-VGLS-DKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
1912-2117 |
1.62e-24 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 104.09 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYR--RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlsniHEVHQNMG 1989
Cdd:cd03293 1 LEVRNVSKTYGggGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV----TGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 2070 EPTTGMDPKARRFLWNCALSII-KEGRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:cd03293 157 EPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1911-2121 |
2.79e-24 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 103.35 E-value: 2.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEV---- 1984
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkir 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQfDAITEL---LTGREHVE--FFALLRGVPEKEVGKVGEWAIRKLGLLK-YGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03257 81 RKEIQMVFQ-DPMSSLnprMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQI----LDLLKKlqeelGLTLLFITHDLGVVAKIADRVAVMYAGK 223
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1911-2121 |
4.26e-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: 103.97 E-value: 4.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIY---RrkrkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEV-- 1984
Cdd:COG0411 4 LLEVRGLTKRFgglV-----AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlPPHRIar 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 ------HQNMGYCPQFDAITELLTG---REHVEFFALLRGVP-----EKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNK 2050
Cdd:COG0411 79 lgiartFQNPRLFPELTVLENVLVAahaRLGRGLLAALLRLPrarreEREARERAEELLERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2051 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEEL----AELIRRlrderGITILLIEHDMDLVMGLADRIVVLDFGR 230
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1911-2140 |
4.27e-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: 108.84 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIY---RRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL----SNIHE 1983
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 VHQNMGYCPQ--FDAITELLTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGL-LKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNR 2134
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQI----LNLLRDlqrelGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
....*.
gi 507682765 2135 FGDGYT 2140
Cdd:COG1123 496 PQHPYT 501
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1911-2131 |
6.08e-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: 6.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIY--RRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSN--IHEV 1984
Cdd:cd03258 1 MIELKNVSKVFgdTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtlLSGkeLRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQ-FDaiteLLTGR---EHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:cd03258 81 RRRIGMIFQhFN----LLSSRtvfENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:cd03258 157 NNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
899-1108 |
1.23e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.86 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGM---KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEM 968
Cdd:COG1101 2 LELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklpeykRAKY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 -STIRQN--LGVCPQhnvlfdmLTVEEHIWFyACLKG--------LSEKHVKVEMEQMA-LDVGLPpSKLKSKTSQLSGG 1036
Cdd:COG1101 82 iGRVFQDpmMGTAPS-------MTIEENLAL-AYRRGkrrglrrgLTKKRRELFRELLAtLGLGLE-NRLDTKVGLLSGG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1037 mQRK-LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:COG1101 153 -QRQaLSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
899-1093 |
1.32e-23 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.08 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNlVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSG-TAYILGKDIRSE-MSTIRQNLG 976
Cdd:COG1119 4 LELRN-VTVRRGG-KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEdVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCpqHNVLFDMLTVEEHIW------FYACLkGLSeKHVKVEMEQMALD----VGLppSKLKSKT-SQLSGGMQRKLSVAL 1045
Cdd:COG1119 82 LV--SPALQLRFPRDETVLdvvlsgFFDSI-GLY-REPTDEQRERAREllelLGL--AHLADRPfGTLSQGEQRRVLIAR 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDE 1093
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEE 205
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1913-2126 |
1.54e-23 |
|
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: 99.82 E-value: 1.54e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:cd03214 1 EVENLS--VGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQfdaitelltgrehveffallrgvpekevgkvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03214 79 PQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2072 TTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:cd03214 125 TSHLDIAHQIEL----LELLRRlarerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
1913-2126 |
2.10e-23 |
|
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: 100.30 E-value: 2.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsilsNIHEVHQNMGYCP 1992
Cdd:cd03235 1 EVEDLT--VSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGK----PLEKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1993 QFDAI--TELLTGREHVE-----FFALLRGVPEKEVGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03235 75 QRRSIdrDFPISVRDVVLmglygHKGLFRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2066 VFLDEPTTGMDPKARRFLwncaLSIIK----EGRSVVLTSHSMEECEALCTRmAIMVNGKFRCLG 2126
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDI----YELLRelrrEGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
899-1109 |
2.13e-23 |
|
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: 100.30 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---RSEMSTIRQNL 975
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQHNVLFDMLTVEEHI-----WfyacLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03262 79 GMVFQQFNLFPHLTVLENItlapiK----VKGMSKAEAEERALELLEKVGLA-DKADAYPAQLSGGQQQRVAIARALAMN 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03262 154 PKVMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1928-2121 |
2.46e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 108.67 E-value: 2.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQ-FDAITElLTGREH 2006
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQaFSLYGE-LTVRQN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2007 VEFFALLRGVPEKEV-GKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2085
Cdd:NF033858 360 LELHARLFHLPAAEIaARVAE-MLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWR 438
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 2086 --CALSiIKEGRSVVLTSHSMEECEaLCTRMAIMVNGK 2121
Cdd:NF033858 439 llIELS-REDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
899-1095 |
3.84e-23 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.22 E-value: 3.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP-ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIWFYAclKGLSEKHVKVEMEQMALD---VGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGS 1051
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEIREALERAGLDefvAALPQgldTPIGEGGAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH---HMDEAD 1095
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
1912-2135 |
4.91e-23 |
|
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: 100.00 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS------NIHEVH 1985
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNlpphkrPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03300 79 QNYALFPH-------LTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL----KNRF 2135
Cdd:cd03300 152 LLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1912-2121 |
6.80e-23 |
|
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: 99.71 E-value: 6.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRK-------------------PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNA-- 1970
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyrevEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVrv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1971 -----FLNKNSILSNIHEVhqnmgycpqFDAITELLTGREHVEFFALLR---GVPEKEVGKvgewAIRKLG-LLKYGE-- 2039
Cdd:cd03267 81 aglvpWKRRKKFLRRIGVV---------FGQKTQLWWDLPVIDSFYLLAaiyDLPPARFKK----RLDELSeLLDLEEll 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2040 -KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:cd03267 148 dTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVI 227
|
....
gi 507682765 2118 VNGK 2121
Cdd:cd03267 228 DKGR 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
899-1110 |
1.33e-22 |
|
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: 98.33 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTV-----------EEHIWfyACLK--GLSEKhvkVEMEQMALDvglppSKLKSKTSQLSGGmQRKL-SV 1043
Cdd:cd03244 83 IPQDPVLFSG-TIrsnldpfgeysDEELW--QALErvGLKEF---VESLPGGLD-----TVVEEGGENLSVG-QRQLlCL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEadILG-DRIAIISHGKLC 1110
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDT--IIDsDRILVLDKGRVV 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
899-1114 |
1.35e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.94 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRseMSTIR--QNLG 976
Cdd:COG1129 5 LEMRGISKSF-GGVK-ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRdaQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VC--PQHNVLFDMLTVEEHIWfyacLKGLSEKHVKV---EMEQMA------LDVGLPPSKlksKTSQLSGGMQRKLSVAL 1045
Cdd:COG1129 81 IAiiHQELNLVPNLSVAENIF----LGREPRRGGLIdwrAMRRRArellarLGLDIDPDT---PVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1046 AFVGGSKVVILDEPTAgvdPYSRRGIWELL-----LKyRQGRTIILSTHHMDEADILGDRIAIISHGKLccVGS 1114
Cdd:COG1129 154 ALSRDARVLILDEPTA---SLTEREVERLFriirrLK-AQGVAIIYISHRLDEVFEIADRVTVLRDGRL--VGT 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
1913-2122 |
1.77e-22 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 97.71 E-value: 1.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-----LSNIHEVHQN 1987
Cdd:cd03226 1 RIENISFSYKKGTE-ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkakerRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYcpQFdaitelltGREHVeFFALLRGVPEK-EVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03226 80 VDY--QL--------FTDSV-REELLLGLKELdAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:cd03226 149 IFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1900-2146 |
1.98e-22 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 101.35 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1900 QRILDGGGQNDIlEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAG--KSSTFKMLTGDTTVTRGNAFLnknSI 1977
Cdd:NF000106 3 RKTISNGARNAV-EVRGLVKHFGEVK--AVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*---TW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1978 LSNIHEVHQNMG-YCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:NF000106 77 CANRRALRRTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFG 2136
Cdd:NF000106 157 ASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
250
....*....|
gi 507682765 2137 dGYTIVVRIA 2146
Cdd:NF000106 237 -GRTLQIRPA 245
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
900-1114 |
1.98e-22 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.08 E-value: 1.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS----EMSTIRqnl 975
Cdd:PRK13548 4 EARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwspaELARRR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQHNVL-FDmLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLppSKLKSKT-SQLSGG-MQRklsVALAFV---- 1048
Cdd:PRK13548 79 AVLPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDL--AHLAGRDyPQLSGGeQQR---VQLARVlaql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1049 ----GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLArqLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGT 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
916-1116 |
2.03e-22 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 98.31 E-value: 2.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQnlgVCPQHNVLFDMLTVEEHIW 995
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 996 FY--ACLKGL--SEKHVKVEmEQMALdVGLPPSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGI 1071
Cdd:TIGR01184 77 LAvdRVLPDLskSERRAIVE-EHIAL-VGLTEAADK-RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 1072 WELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSL 1116
Cdd:TIGR01184 154 QEELMQIWEehRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQIL 200
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
919-1113 |
2.35e-22 |
|
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: 97.56 E-value: 2.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYA 998
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQENNLFAHLTVEQNVGLGL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 999 C----LKGLSEKHVKVEMEQMALDvglppSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1074
Cdd:cd03298 96 SpglkLTAEDRQAIEVALARVGLA-----GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 1075 LLKYRQGR--TIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:cd03298 171 VLDLHAETkmTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1912-2121 |
3.78e-22 |
|
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: 98.48 E-value: 3.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVG----------------------IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGN 1969
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKGkskeeilkktgqtvgvndvsldVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1970 AFLNKNSILS------------NIHEVHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKY 2037
Cdd:cd03294 81 VLIDGQDIAAmsrkelrelrrkKISMVFQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2038 GEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAI 2116
Cdd:cd03294 154 EHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAI 233
|
....*
gi 507682765 2117 MVNGK 2121
Cdd:cd03294 234 MKDGR 238
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
901-1109 |
4.76e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 99.88 E-value: 4.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYRDGMK--VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK11153 4 LKNISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHnvlFDML---TVEEHIWFYACLKGLSEKHVK--VEmEQMALdVGLppSKLKSK-TSQLSGGMQRKLSVALAFV 1048
Cdd:PRK11153 84 IGMIFQH---FNLLssrTVFDNVALPLELAGTPKAEIKarVT-ELLEL-VGL--SDKADRyPAQLSGGQKQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK11153 157 SNPKVLLCDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
901-1114 |
5.59e-22 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 100.68 E-value: 5.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYrDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVCPQ 980
Cdd:PRK11607 22 IRNLTKSF-DG-QHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFA-KRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1061 AGVDPYSR-RGIWELL-LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK11607 178 GALDKKLRdRMQLEVVdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
902-1109 |
7.70e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 97.85 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYRDG----MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNL 975
Cdd:PRK13633 8 KNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLwdIRNKA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQH--NVLFDMLtVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK13633 88 GMVFQNpdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYR-RHAPHLLSGGQKQRVAIAGILAMRPEC 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1054 VILDEPTAGVDPYSRR----GIWELLLKYrqGRTIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:PRK13633 166 IIFDEPTAMLDPSGRRevvnTIKELNKKY--GITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1911-2117 |
8.85e-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: 97.08 E-value: 8.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRK--RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlsniHEVHQNM 1988
Cdd:COG1116 7 ALELRGVSKRFPTGggGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV----TGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAiteLL---TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:COG1116 83 GVVFQEPA---LLpwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQEtGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1911-2121 |
9.15e-22 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 9.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSN--IHE-VHQN 1987
Cdd:COG1137 3 TLEAENLVKSY--GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:COG1137 80 IGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2068 LDEPTTGMDPKA----RRflwncalsIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG1137 160 LDEPFAGVDPIAvadiQK--------IIRHlkerGIGVLITDHNVRETLGICDRAYIISEGK 213
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
899-1103 |
1.00e-21 |
|
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: 98.59 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMS 969
Cdd:COG0444 2 LEVRNLKVYFptRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQN-LGVCPQhnvlfD-------MLTVEEHIW-FYACLKGLSEKHVKVEMEQMALDVGLPPSK--LKSKTSQLSGGMQ 1038
Cdd:COG0444 82 KIRGReIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPErrLDRYPHELSGGMR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAI 1103
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAV 223
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
909-1133 |
1.13e-21 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 96.07 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDM 987
Cdd:cd03249 13 RPDVPI-LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 988 lTVEEHIWFyaclkGLSEKHVkVEMEQMALD-------VGLP---PSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:cd03249 92 -TIAENIRY-----GKPDATD-EEVEEAAKKanihdfiMSLPdgyDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdeADILG-DRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLVKK 1133
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAMKGRTTIVIAHRL--STIRNaDLIAVLQNGQVVEQGTHDELMAQ--KGVYAKLVKA 237
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
899-1130 |
1.23e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRdGMKVAVDGLalNFYEGQIT--SFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNL 975
Cdd:PRK13652 4 IETRDLCYSYS-GSKEALNNI--NFIAPRNSriAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQH--NVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLppSKLKSKTSQ-LSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK13652 81 GLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGL--EELRDRVPHhLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKNQLGTGYYL 1128
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTveEIFLQPDLLARVHL 237
|
..
gi 507682765 1129 TL 1130
Cdd:PRK13652 238 DL 239
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
899-1109 |
1.55e-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: 93.92 E-value: 1.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC 978
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMlTVEEhiwfyaclkglsekhvkvemeqmalDVGLppsklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03247 81 NQRPYLFDT-TLRN-------------------------NLGR----------RFSGGERQRLALARILLQDAPIVLLDE 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdeadiLG----DRIAIISHGKL 1109
Cdd:cd03247 125 PTVGLDPITERQLLSLIFEVLKDKTLIWITHHL-----TGiehmDKILFLENGKI 174
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1912-2140 |
1.64e-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: 96.03 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYR--RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHEVHQNM 1988
Cdd:COG1124 2 LEVRNLSVSYGqgGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQfDAITEL---LTGREHVEFFALLRGVPEKEVgKVGEwAIRKLGLlkyGEKYAGNY----SGGNKRKLSTAMALIG 2061
Cdd:COG1124 82 QMVFQ-DPYASLhprHTVDRILAEPLRIHGLPDREE-RIAE-LLEQVGL---PPSFLDRYphqlSGGQRQRVAIARALIL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGDGYT 2140
Cdd:COG1124 156 EPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYT 235
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
899-1125 |
1.87e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.51 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEmstiRQNLGVC 978
Cdd:NF033858 2 ARLEGVSHRY--GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADA----RHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQ---------HNvLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGL------PPSKLksktsqlSGGMQRKLSV 1043
Cdd:NF033858 76 PRiaympqglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLapfadrPAGKL-------SGGMKQKLGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR---TIILSTHHMDEADILgDRIAIISHGKLCCVGSSLFLKN 1120
Cdd:NF033858 148 CCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
|
....*
gi 507682765 1121 QLGTG 1125
Cdd:NF033858 227 RTGAD 231
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
902-1114 |
2.27e-21 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 95.35 E-value: 2.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYRdGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCP 979
Cdd:PRK10895 7 KNLAKAYK-GRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 980 QHNVLFDMLTVEEHIwfYACL---KGLSEKHVKVEMEQMALDVGLppSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK10895 85 QEASIFRRLSVYDNL--MAVLqirDDLSAEQREDRANELMEEFHI--EHLRDSMGQsLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
1912-2126 |
3.49e-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: 3.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS------NIHEVH 1985
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03301 79 QNYALYPH-------MTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
1912-2131 |
3.52e-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: 95.06 E-value: 3.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:cd03295 1 IEFENVTKRYG-GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL--LKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2069 DEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
899-1109 |
3.56e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 96.69 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKV---AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST----- 970
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 --------------------IRQNLGVCPQ--HNVLFDMlTVEEHIWFYACLKGLSekhvKVEMEQMALD----VGLPPS 1024
Cdd:PRK13651 83 vleklviqktrfkkikkikeIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVS----KEEAKKRAAKyielVGLDES 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1025 KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAI 1103
Cdd:PRK13651 158 YLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIF 237
|
....*.
gi 507682765 1104 ISHGKL 1109
Cdd:PRK13651 238 FKDGKI 243
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
1912-2121 |
3.56e-21 |
|
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: 94.94 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHE-------- 1983
Cdd:cd03256 1 IEVENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKalrqlrrq 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 ---VHQNMGYCPQFDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03256 80 igmIFQQFNLIERLSVLENVLSGRlgRRSTWRSLFGLFPKEEKQRALA-ALERVGLLDKAYQRADQLSGGQQQRVAIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSI-IKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03256 159 LMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
926-1108 |
5.12e-21 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 94.05 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE------MSTIRQnlgvcpQHNvLFDMLTVEEHIWFyac 999
Cdd:COG3840 25 GERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppaerpVSMLFQ------ENN-LFPHLTVAQNIGL--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1000 lkGLS-------EKHVKVEmeQMALDVGLPpSKLKSKTSQLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:COG3840 95 --GLRpglkltaEQRAQVE--QALERVGLA-GLLDRLPGQLSGGqRQR---VALArcLVRKRPILLLDEPFSALDPALRQ 166
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 1070 GIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:COG3840 167 EMLDLVdeLCRERGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
881-1113 |
1.46e-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: 1.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 881 KGVSEIRMEEEPTHLKLGVSIQNLVKVY---RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA 957
Cdd:TIGR03269 262 EGVSEVEKECEVEVGEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 958 YILGKDIRSEMSTIR--------QNLGVCPQHNVLFDMLTVEEHIWFYACL---KGLSEKHVKVEMEQMALDVGLPPSKL 1026
Cdd:TIGR03269 342 NVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYPHRTVLDNLTEAIGLelpDELARMKAVITLKMVGFDEEKAEEIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1027 KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAII 1104
Cdd:TIGR03269 422 DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALM 501
|
....*....
gi 507682765 1105 SHGKLCCVG 1113
Cdd:TIGR03269 502 RDGKIVKIG 510
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
921-1114 |
1.78e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 94.03 E-value: 1.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-----YILGKDIRSEMSTIRQNLGVCPQ--HNVLFDMlTVEEH 993
Cdd:PRK13643 27 LEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE-TVLKD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 994 IWFYACLKGLS-EKHVKVEMEQMALdVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIW 1072
Cdd:PRK13643 106 VAFGPQNFGIPkEKAEKIAAEKLEM-VGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMM 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507682765 1073 ELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13643 185 QLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
1936-2133 |
1.84e-20 |
|
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: 92.56 E-value: 1.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNI----HEVHQNMGYCPQFDAITELLTGREHVEFFa 2011
Cdd:cd03261 23 VRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaelYRLRRRMGMLFQSGALFDSLTVFENVAFP- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2012 lLR---GVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:cd03261 102 -LRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEPTAGLDPIASGVIDDLIR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507682765 2089 SIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:cd03261 181 SLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
888-1114 |
1.91e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.78 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 888 MEEEPTHLKLGVSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSE 967
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSFDG--KEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 MSTIRQNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVK---------VEMEQMAldvglppsklKSKTSQLSGGMQ 1038
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITprvmealrmVQLEEFA----------QRKPHQLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1039 RKLSVALAFVGGSKVVILDEPTAGVDpYSRRGIWELLLKYRQ---GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK09452 151 QRVAIARAVVNKPKVLLLDESLSALD-YKLRKQMQNELKALQrklGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
910-1107 |
2.06e-20 |
|
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: 92.29 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 988
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWF---YAclkglSEKHVKVEMEQMALD---VGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:cd03254 92 TIMENIRLgrpNA-----TDEEVIEAAKEAGAHdfiMKLPNgydTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1060 TAGVDPYSRRGIWELLLKYRQGRTIILSTHHMD---EAD--ILGDRIAIISHG 1107
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNADkiLVLDDGKIIEEG 219
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
911-1115 |
2.47e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.92 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPPTSGTAYIL--GKDI---RSEMSTIRQNLGVCPQHN 982
Cdd:PRK14239 16 NKKKALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPEVTITGSIVynGHNIyspRTDTVDLRKEIGMVFQQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 983 VLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMAL-------DVglpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK14239 96 NPFPM-SIYENVVYGLRLKGIKDKQVLDEAVEKSLkgasiwdEV---KDRLHDSALGLSGGQQQRVCIARVLATSPKIIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1115
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDT 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
905-1090 |
2.63e-20 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 97.43 E-value: 2.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 905 VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNV 983
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAH 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 984 LFDMlTVEEHIWFyACLKGLSEkhvkvEMEQMALDVGLPP----------SKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:TIGR02868 420 LFDT-TVRENLRL-ARPDATDE-----ELWAALERVGLADwlralpdgldTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHH 1090
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1878-2122 |
2.89e-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: 2.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1878 PRAVKTKFLplnDEDEDVRRERQRILdgggQNDILEIKELTKIY---RRKRKPAVDRICVGIPRGECFGLLGVNGAGKSS 1954
Cdd:TIGR03269 253 PDEVVAVFM---EGVSEVEKECEVEV----GEPIIKVRNVSKRYisvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTT 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1955 TFKMLTGDTTVTRGN---------------AFLNKNSILSNIHEVHQNMGYCPQFDaITELLTGREHVEF---FALLRGV 2016
Cdd:TIGR03269 326 LSKIIAGVLEPTSGEvnvrvgdewvdmtkpGPDGRGRAKRYIGILHQEYDLYPHRT-VLDNLTEAIGLELpdeLARMKAV 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2017 PE-KEVGKVGEWAIRKLgllkygEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-G 2094
Cdd:TIGR03269 405 ITlKMVGFDEEKAEEIL------DKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmE 478
|
250 260
....*....|....*....|....*...
gi 507682765 2095 RSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:TIGR03269 479 QTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1936-2102 |
4.04e-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: 91.56 E-value: 4.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGNAFLNKNSilSNIHEVHQNMGYCPQFDAITELLTGREHVEFFAL 2012
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQP--RKPDQFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2013 LR-------GVPEKEVGKVGewaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPkarrFLwn 2085
Cdd:cd03234 108 LRlprkssdAIRKKRVEDVL---LRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FT-- 178
|
170 180
....*....|....*....|....
gi 507682765 2086 cALSII-------KEGRSVVLTSH 2102
Cdd:cd03234 179 -ALNLVstlsqlaRRNRIVILTIH 201
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
908-1114 |
6.56e-20 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 96.39 E-value: 6.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 986
Cdd:COG1132 349 YPGD-RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MlTVEEHIwFYAClKGLSEKhvkvEMEQ-----MALDV--GLPP---SKLKSKTSQLSGGmQR-KLSVALAFVGGSKVVI 1055
Cdd:COG1132 428 G-TIRENI-RYGR-PDATDE----EVEEaakaaQAHEFieALPDgydTVVGERGVNLSGG-QRqRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH------HMdeadilgDRIAIISHGKLCCVGS 1114
Cdd:COG1132 500 LDEATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGT 557
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
915-1114 |
7.38e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 92.38 E-value: 7.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA----YILGKDIRS--EMSTIRQNLGVC---PQHNVLF 985
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DmlTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1066 YSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK13645 184 KGEEDFINLFERLnkEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1903-2126 |
8.68e-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: 90.28 E-value: 8.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1903 LDGGGQNDILEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsiLSNIH 1982
Cdd:cd03220 12 TYKGGSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR--VSSLL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1983 EVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:cd03220 90 GL--GGGFNPE-------LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2063 PPVVFLDEPTTGMDP----KARRFLwncaLSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:cd03220 161 PDILLIDEVLAVGDAafqeKCQRRL----RELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
915-1109 |
8.87e-20 |
|
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: 90.51 E-value: 8.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGKD-----IRS-EMSTIRQNlgvcPQhNVL 984
Cdd:TIGR02770 1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPllplsIRGrHIATIMQN----PR-TAF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 985 FDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:TIGR02770 76 NPLFTMGNHAIETLRSLGKLSKQARALILEALEAVGLPDPEevLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 1063 VDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQlfGTGILLITHDLGVVARIADEVAVMDDGRI 204
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1909-2121 |
1.02e-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: 90.91 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFlnknSIL------SNIH 1982
Cdd:COG1119 1 DPLLELRNVT--VRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDV----RLFgerrggEDVW 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1983 EVHQNMGYC-PQF-DAITELLTGREHVE--FFA---LLRGVPEKEVGKVGEWaIRKLGLLKYGEKYAGNYSGGNKRKLST 2055
Cdd:COG1119 75 ELRKRIGLVsPALqLRFPRDETVLDVVLsgFFDsigLYREPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRVLI 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSII--KEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG1119 154 ARALVKDPELLILDEPTAGLDLGARELLLA-LLDKLaaEGAPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
909-1108 |
1.03e-19 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.82 E-value: 1.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCP--QHNVLFD 986
Cdd:PRK11300 14 RFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MLTVEEHIwfyaclkgLSEKHVKVEM---------------EQMALD--------VGLPPSKLKSkTSQLSGGMQRKLSV 1043
Cdd:PRK11300 94 EMTVIENL--------LVAQHQQLKTglfsgllktpafrraESEALDraatwlerVGLLEHANRQ-AGNLAYGQQRRLEI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1912-2123 |
1.06e-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: 90.19 E-value: 1.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHE-VHQNMG 1989
Cdd:cd03224 1 LEVENLNAGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGlPPHErARAGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAITELLTGREHVE--FFALLRGVPEKEVgkvgEWAIRKLGLLKygEKY---AGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:cd03224 79 YVPEGRRIFPELTVEENLLlgAYARRRAKRKARL----ERVYELFPRLK--ERRkqlAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2065 VVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFR 2123
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVV 211
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
885-1109 |
1.28e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.13 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 885 EIRMEEEPthlKLG---VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILG 961
Cdd:COG0488 302 EIRFPPPE---RLGkkvLELEGLSKSYGD--KTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLG 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 962 KDIRsemstirqnLGVCPQHNVLFDM-LTVEEHIWFYAclKGLSEKHVKVEMEQMaldvGLPPSKLKSKTSQLSGGMQRK 1040
Cdd:COG0488 376 ETVK---------IGYFDQHQEELDPdKTVLDELRDGA--PGGTEQEVRGYLGRF----LFSGDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYrQGrTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGV 507
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1912-2122 |
1.48e-19 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 89.10 E-value: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:COG4619 1 LELEGLS--FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQ----FDAitellTGREHVEFFALLRGVPEKEvGKVGEWaIRKLGL-LKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:COG4619 79 VPQepalWGG-----TVRDNLPFPFQLRERKFDR-ERALEL-LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDV 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:COG4619 152 LLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
909-1109 |
3.21e-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: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsemSTIRQNLGVCPqhnvlfdML 988
Cdd:cd03220 31 EVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVS----SLLGLGGGFNP-------EL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWFYACLKGLSEKhvkvEMEQMALDV----GLPPSkLKSKTSQLSGGMQRKL--SVALAFvgGSKVVILDEPTAG 1062
Cdd:cd03220 100 TGRENIYLNGRLLGLSRK----EIDEKIDEIiefsELGDF-IDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLAV 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507682765 1063 VDPYSRRGIWELLL-KYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03220 173 GDAAFQEKCQRRLReLLKQGKTVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
899-1109 |
4.25e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 89.69 E-value: 4.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMST 970
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMvlseetvwDVRRQVGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 IRQNlgvcPQHNvlFDMLTVEEHIWFyaclkGLSEKHVK----VEMEQMALD-VGLpPSKLKSKTSQLSGGmqRKLSVAL 1045
Cdd:PRK13635 86 VFQN----PDNQ--FVGATVQDDVAF-----GLENIGVPreemVERVDQALRqVGM-EDFLNREPHRLSGG--QKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1046 AFVGGS--KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:PRK13635 152 AGVLALqpDIIILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1911-2133 |
4.71e-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: 88.50 E-value: 4.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKiyRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL----SNIHEVHQ 1986
Cdd:COG1127 5 MIEVRNLTK--SFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQ----FDAitelLTGREHVEFFalLR---GVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1127 83 RIGMLFQggalFDS----LTVFENVAFP--LRehtDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2060 IGGPPVVFLDEPTTGMDPK-ARRFlwnCALsiIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:COG1127 157 ALDPEILLYDEPTAGLDPItSAVI---DEL--IRElrdelGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
900-1105 |
7.94e-19 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 88.77 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTiRqnlGV 977
Cdd:COG4525 5 TVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIWFYACLKGLSekhvKVEMEQMALD----VGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:COG4525 81 VFQKDALLPWLNVLDNVAFGLRLRGVP----KAERRARAEEllalVGLADFA-RRRIWQLSGGMRQRVGIARALAADPRF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIIS 1105
Cdd:COG4525 156 LLMDEPFGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
925-1109 |
8.76e-19 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 87.35 E-value: 8.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 925 EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK-----DIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFyaC 999
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRENLAF--G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1000 LKGLSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LK 1077
Cdd:cd03297 100 LKRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELkqIK 178
|
170 180 190
....*....|....*....|....*....|..
gi 507682765 1078 YRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:cd03297 179 KNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1909-2128 |
8.94e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.83 E-value: 8.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYR--------------------RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRG 1968
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrrtrREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1969 NAFLNKN--SILsnihEVhqNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGK----VGEWAirklGLLKYGEKYA 2042
Cdd:COG1134 82 RVEVNGRvsALL----EL--GAGFHPE-------LTGRENIYLNGRLLGLSRKEIDEkfdeIVEFA----ELGDFIDQPV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2043 GNYSGGNKRKL--STAMALigGPPVVFLDEPTTGMDP----KARRFLwncaLSIIKEGRSVVLTSHSMEECEALCTRMAI 2116
Cdd:COG1134 145 KTYSSGMRARLafAVATAV--DPDILLVDEVLAVGDAafqkKCLARI----RELRESGRTVIFVSHSMGAVRRLCDRAIW 218
|
250
....*....|..
gi 507682765 2117 MVNGKFRCLGSV 2128
Cdd:COG1134 219 LEKGRLVMDGDP 230
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1915-2121 |
1.19e-18 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.07 E-value: 1.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1915 KELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTV--TRGNAFLN-KNSILSNIHEVhqnMGYC 1991
Cdd:cd03213 11 VTVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINgRPLDKRSFRKI---IGYV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVpekevgkvgewairklgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03213 88 PQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSM-EECEALCTRMAIMVNGK 2121
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGR 189
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
909-1132 |
1.40e-18 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.48 E-value: 1.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTI-RQNLGVCPQHNV 983
Cdd:PRK10070 37 KTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVrRKKIAMVFQSFA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 984 LFDMLTVEEHIWFYACLKGLSEKhvkvEMEQMALD----VGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:PRK10070 117 LMPHMTVLDNTAFGMELAGINAE----ERREKALDalrqVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1060 TAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYLTLVK 1132
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFR 266
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
914-1094 |
1.47e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.75 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 914 VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDirsemstirqNLGVCPQHNVLFDML--TVE 991
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 992 E--------HIWFYACLKGLSEKHVKVEMEQMALDvGLPPSKLksktSQLSGG-MQRKLsVALAFVGGSKVVILDEPTAG 1062
Cdd:NF040873 76 DlvamgrwaRRGLWRRLTRDDRAAVDDALERVGLA-DLAGRQL----GELSGGqRQRAL-LAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|...
gi 507682765 1063 VDPYSRRGIWELLLKY-RQGRTIILSTHHMDEA 1094
Cdd:NF040873 150 LDAESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1908-2121 |
1.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI---LSNIHEV 1984
Cdd:PRK13636 2 EDYILKVEELNYNYSDGTH-ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK13636 81 RESVGMVFQ-DPDNQLFSASvyQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2063 PPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGR 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1911-2131 |
1.62e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 87.94 E-value: 1.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL-SNIHEVHQNMG 1989
Cdd:PRK13652 3 LIETRDLCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQF--DAITELlTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:PRK13652 82 LVFQNpdDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2068 LDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
1912-2121 |
2.07e-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: 84.93 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN---KNSILSNIHEVHQNM 1988
Cdd:cd03229 1 LELKNVSKRY--GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDgedLTDLEDELPPLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAITELLTGREHVEFfallrgvpekevgkvgewairklGLlkygekyagnySGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03229 79 GMVFQDFALFPHLTVLENIAL-----------------------GL-----------SGGQQQRVALARALAMDPDVLLL 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2069 DEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03229 125 DEPTSALDPITRREV----RALLKSlqaqlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
899-1109 |
2.11e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 86.47 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK10908 2 IRFEHVSKAYLGG-RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQ-HNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQmALD-VGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK10908 81 IGMIFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSA-ALDkVGLL-DKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
899-1114 |
2.24e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.75 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMK---VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI----LGKDIRSEMSTI 971
Cdd:PRK13631 22 LRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 972 -------------RQNLGVC---PQHNVLFDmlTVEEHIWFYACLKGLSE----KHVKVEMEQMaldvGLPPSKLKSKTS 1031
Cdd:PRK13631 102 npyskkiknfkelRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKseakKLAKFYLNKM----GLDDSYLERSPF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1032 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGKLC 1110
Cdd:PRK13631 176 GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKaNNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
....
gi 507682765 1111 CVGS 1114
Cdd:PRK13631 256 KTGT 259
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
899-1114 |
2.49e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.55 E-value: 2.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS---GTAYILGKDIRSE-MSTIRQN 974
Cdd:PRK13640 6 VEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQH-NVLFDMLTVEEHIWFyaclkGLSEKHV-KVEM----EQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK13640 86 VGIVFQNpDNQFVGATVGDDVAF-----GLENRAVpRPEMikivRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGS 1114
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGS 226
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
892-1109 |
3.07e-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: 85.99 E-value: 3.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 892 PTHLKLGVSIQNLVKVYRDGMKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMS 969
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNLGVCPQHNVLFDMlTVEEHIWF------YACLKGLSEK-HVKVEMEQMAL----DVGlppsklkSKTSQLSGGMQ 1038
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAYglqscsFECVKEAAQKaHAHSFISELASgydtEVG-------EKGSQLSGGQK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKL 1109
Cdd:cd03248 157 QRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1911-2168 |
3.13e-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: 88.62 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIhEVHQ-NMG 1989
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-TGL-PPEKrNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAiteL---LTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:COG3842 81 MVFQDYA---LfphLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL----KNRFgdgyti 2141
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIyerpATRF------ 231
|
250 260
....*....|....*....|....*....
gi 507682765 2142 vvriagsnpdlkpVQEFFGLA--FPGSVL 2168
Cdd:COG3842 232 -------------VADFIGEAnlLPGTVL 247
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
1912-2129 |
3.56e-18 |
|
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: 85.85 E-value: 3.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpaVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIHEVHQNMGYC 1991
Cdd:cd03299 1 LKVENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVG-KVGEWAiRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIErKVLEIA-EMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2071 PTTGMDPKARRFLWNCALSIIKEGRSVVL-TSHSMEECEALCTRMAIMVNGKFRCLGSVQ 2129
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1909-2121 |
3.58e-18 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 85.87 E-value: 3.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYRRK--RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-------LS 1979
Cdd:COG1136 2 SPLLELRNLTKSYGTGegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIsslsereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHevHQNMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG1136 82 RLR--RRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSmEECEALCTRMAIMVNGK 2121
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGR 221
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
912-1089 |
6.54e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.54 E-value: 6.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 912 MKVAVDGLA-----------LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR-SEMSTIRQNLGv 977
Cdd:PRK13539 1 MMLEGEDLAcvrggrvlfsgLSFTlaAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 cpQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEqmalDVGLPP-SKLKSKTsqLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13539 80 --HRNAMKPALTVAENLEFWAAFLGGEELDIAAALE----AVGLAPlAHLPFGY--LSAGQKRRVALARLLVSNRPIWIL 151
|
170 180 190
....*....|....*....|....*....|....
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTH 1089
Cdd:PRK13539 152 DEPTAALDAAAVALFAELIRAHLaQGGIVIAATH 185
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1912-2121 |
6.75e-18 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 84.56 E-value: 6.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIH--EVHQNMG 1989
Cdd:cd03245 3 IEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI-RQLDpaDLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQ-----FDAITELLT-GREHVEFFALLRGVpekEVGKVGEWAIR-KLGL-LKYGEKYAGnYSGGNKRKLSTAMALIG 2061
Cdd:cd03245 82 YVPQdvtlfYGTLRDNITlGAPLADDERILRAA---ELAGVTDFVNKhPNGLdLQIGERGRG-LSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2062 GPPVVFLDEPTTGMDPKA-RRFLWNcaLSIIKEGRSVVLTSH--SMEEceaLCTRMAIMVNGK 2121
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGR 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
915-1109 |
7.44e-18 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 89.31 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCP---QHNVLFDMLT 989
Cdd:COG1129 267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 VEEHIWF-----YACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKlsVALA--FVGGSKVVILDEPTAG 1062
Cdd:COG1129 347 IRENITLasldrLSRGGLLDRRRERALAEEYIKRLRIKTPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRG 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 1063 VDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1109
Cdd:COG1129 425 IDVGAKAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
909-1090 |
8.97e-18 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 83.95 E-value: 8.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 988
Cdd:TIGR01189 10 RGE-RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWFYACLKGLSEKHVKVEMEQMALD--VGLPpsklkskTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:TIGR01189 89 SALENLHFWAAIHGGAQRTIEDALAAVGLTgfEDLP-------AAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
|
170 180
....*....|....*....|....*
gi 507682765 1067 SRRGIWELLLKY-RQGRTIILSTHH 1090
Cdd:TIGR01189 162 GVALLAGLLRAHlARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
899-1109 |
1.03e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 85.55 E-value: 1.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNL-VKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--------DIRSEMS 969
Cdd:PRK13650 5 IEVKNLtFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDllteenvwDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNlgvcPQHNvlFDMLTVEEHIWFYACLKGLSEKHVKVEMEQmALD-VGLPPSKLKsKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK13650 85 MVFQN----PDNQ--FVGATVEDDVAFGLENKGIPHEEMKERVNE-ALElVGMQDFKER-EPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEV-ALSDRVLVMKNGQV 218
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
913-1107 |
1.07e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.14 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---SEMSTIRQNLGVCPQHNVLfdmlt 989
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEgpgAERGVVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 veEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRR 1069
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAE-KRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTRE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507682765 1070 GIWELLLK--YRQGRTIILSTHHMDEADILGDRIAIISHG 1107
Cdd:PRK11248 166 QMQTLLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
899-1150 |
1.11e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLG-- 976
Cdd:PRK09700 6 ISMAGIGKSF--GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGig 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFDMLTVEEHIWFYACLKG-------LSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGMQRKLSVALAFVG 1049
Cdd:PRK09700 84 IIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1050 GSKVVILDEPTAGVdpySRRGIWELLLKYRQ----GRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQlgtG 1125
Cdd:PRK09700 163 DAKVIIMDEPTSSL---TNKEVDYLFLIMNQlrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSND---D 236
|
250 260
....*....|....*....|....*
gi 507682765 1126 YYLTLVKKDVESSLGSCRNSSSTVS 1150
Cdd:PRK09700 237 IVRLMVGRELQNRFNAMKENVSNLA 261
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
900-1114 |
1.25e-17 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 84.78 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC- 978
Cdd:COG4674 12 YVEDLTVSF-DGFK-ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGr 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 ----PqhNVlFDMLTVEEHI---------WFyACLKGLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:COG4674 90 kfqkP--TV-FEELTVFENLelalkgdrgVF-ASLFARLTAEERDRIEEVLETIGL-TDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
928-1128 |
1.29e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.10 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 928 ITSFLGHNGAGKTTTMSILTGLFP------PTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYACL 1000
Cdd:PRK14246 38 IFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1001 KGLSEK-HVKVEMEQMALDVGLPPS---KLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLL 1076
Cdd:PRK14246 118 HGIKEKrEIKKIVEECLRKVGLWKEvydRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1077 KYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS--LFL--KNQLGTGYYL 1128
Cdd:PRK14246 198 ELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSneIFTspKNELTEKYVI 253
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1911-2181 |
1.61e-17 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 87.20 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSiLSNIHEVHQNMGY 1990
Cdd:PRK11607 19 LLEIRNLTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2071 PTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKnrfgdgytivvriagSN 2149
Cdd:PRK11607 176 PMGALDKKLRDRMQLEVVDILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---------------EH 240
|
250 260 270
....*....|....*....|....*....|....
gi 507682765 2150 PDLKPVQEFFGLA--FPGsVLKEKHRNMLQYQLP 2181
Cdd:PRK11607 241 PTTRYSAEFIGSVnvFEG-VLKERQEDGLVIDSP 273
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
901-1109 |
1.69e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYRDG-MKVAV-DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR-Q 973
Cdd:PRK10535 7 LKDIRRSYPSGeEQVEVlKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVatldADALAQLRrE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 974 NLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10535 87 HFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPSQLSGGQQQRVSIARALMNGGQV 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADiLGDRIAIISHGKL 1109
Cdd:PRK10535 166 ILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1911-2121 |
1.73e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 85.13 E-value: 1.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI---LSNIHEVHQN 1987
Cdd:PRK13639 1 ILETRDLKYSYP-DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYCPQfDAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13639 80 VGIVFQ-NPDDQLFapTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGK 214
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
908-1109 |
1.74e-17 |
|
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: 83.82 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 986
Cdd:cd03253 10 YDPGRPV-LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MlTVEEHIwFYACLKGLSEkhvkvEMEQMALD-------VGLP---PSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:cd03253 89 D-TIGYNI-RYGRPDATDE-----EVIEAAKAaqihdkiMRFPdgyDTIVGERGLKLSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRI 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
918-1089 |
1.80e-17 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 83.67 E-value: 1.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMSTirQNLGVCPQHNVLFDMLTV 990
Cdd:PRK10584 28 GVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdeeaRAKLRA--KHVGFVFQSFMLIPTLNA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 991 EEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDK 184
|
170 180
....*....|....*....|.
gi 507682765 1071 IWELL--LKYRQGRTIILSTH 1089
Cdd:PRK10584 185 IADLLfsLNREHGTTLILVTH 205
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1912-2128 |
1.83e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 85.10 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRK---RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS---NIHEVH 1985
Cdd:PRK13637 3 IKIENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNMG----YcPQFDAITEllTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL--LKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:PRK13637 83 KKVGlvfqY-PEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSV 2128
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1911-2105 |
2.05e-17 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 83.56 E-value: 2.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkPAVDRICVGIPRGE-CFgLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSN--IHEVH 1985
Cdd:COG2884 1 MIRFENVSKRYPGGR-EALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrLKRreIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNMGYCPQ-FdaitELLTGR---EHVEFFALLRGVPEKEVGK-VGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:COG2884 79 RRIGVVFQdF----RLLPDRtvyENVALPLRVTGKSRKEIRRrVRE-VLDLVGLSDKAKALPHELSGGEQQRVAIARALV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507682765 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSME 2105
Cdd:COG2884 154 NRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1911-2122 |
2.07e-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: 82.09 E-value: 2.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTkiyrrkRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHEVHQN-M 1988
Cdd:cd03215 4 VLEVRGLS------VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtRRSPRDAIRAgI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYcpqfdaitelltgrehveffallrgVPE--KEVGKVGEWAIRK---LGLLkygekyagnYSGGNKRKLSTAMALIGGP 2063
Cdd:cd03215 78 AY-------------------------VPEdrKREGLVLDLSVAEniaLSSL---------LSGGNQQKVVLARWLARDP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2064 PVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:cd03215 124 RVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
1912-2121 |
2.25e-17 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 81.66 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQfdaitelltgreHVEFFAllrgvpekevGKVGEwairklGLLkygekyagnySGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:cd03228 81 VPQ------------DPFLFS----------GTIRE------NIL----------SGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2071 PTTGMDPKARRFLWNcALSIIKEGRSVVLTSHSMEECEaLCTRMAIMVNGK 2121
Cdd:cd03228 123 ATSALDPETEALILE-ALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
901-1114 |
3.08e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.91 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrsEMSTIRQ---NLGV 977
Cdd:PRK11231 5 TENLTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI--SMLSSRQlarRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEE--------HIWFYACLKGLSEKHVKVEMEQMALDvglppsKLKSK-TSQLSGGMQRKLSVALAFV 1048
Cdd:PRK11231 81 LPQHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQTRIN------HLADRrLTDLSGGQRQRAFLAMVLA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK11231 155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTqGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
899-1109 |
4.17e-17 |
|
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: 83.70 E-value: 4.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGM-------KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSE 967
Cdd:TIGR02769 3 LEVRDVTHTYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 MSTIRQNL---------GVCPQHNVLFDMLTVEEHiwfyacLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQ 1038
Cdd:TIGR02769 83 RRAFRRDVqlvfqdspsAVNPRMTVRQIIGEPLRH------LTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1039 RKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:TIGR02769 157 QRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
915-1131 |
4.58e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 87.87 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD------- 986
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSgsilenl 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGlppSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:TIGR01193 569 LLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQ---TELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1067 SRRGIWELLLKYrQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1131
Cdd:TIGR01193 646 TEKKIVNNLLNL-QDKTIIFVAHRLSVAK-QSDKIIVLDHGKIIEQGSHDELLDR--NGFYASLI 706
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
915-1109 |
5.28e-17 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 82.62 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST--IRQNLGVCPQHNVLFDMLTVEE 992
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIVPEGRRVFSRMTVEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 993 HI---WFYACLKGLSEKHVKVemeqmaldVGLPPsKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK11614 100 NLamgGFFAERDQFQERIKWV--------YELFP-RLHERRIQragtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507682765 1066 YSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK11614 171 IIIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
917-1090 |
5.56e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 5.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 917 DGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWF 996
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTALENLRF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 997 YACLKGLsekhVKVEMEQMALD-VGL------PpsklkskTSQLSGGMQRKlsVALA--FVGGSKVVILDEP-----TAG 1062
Cdd:PRK13538 98 YQRLHGP----GDDEALWEALAqVGLagfedvP-------VRQLSAGQQRR--VALArlWLTRAPLWILDEPftaidKQG 164
|
170 180
....*....|....*....|....*...
gi 507682765 1063 VDPYSRRgiweLLLKYRQGRTIILSTHH 1090
Cdd:PRK13538 165 VARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
1912-2121 |
5.78e-17 |
|
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: 82.07 E-value: 5.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKrKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSiLSNIHE-----VHQ 1986
Cdd:cd03292 1 IEFINVTKTYPNG-TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD-VSDLRGraipyLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGK 213
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1890-2142 |
6.57e-17 |
|
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: 87.20 E-value: 6.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1890 DEDEDVRRERQRILDGGgqndiLEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGN 1969
Cdd:COG2274 457 EREEGRSKLSLPRLKGD-----IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1970 AFLNKNSILS-NIHEVHQNMGYCPQfDaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGLLKY--------- 2037
Cdd:COG2274 532 ILIDGIDLRQiDPASLRRQIGVVLQ-D--VFLFSGtiRENITLGD--PDATDEEI----IEAARLAGLHDFiealpmgyd 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2038 ---GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSHSMeECEALCTRM 2114
Cdd:COG2274 603 tvvGEG-GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILE-NLRRLLKGRTVIIIAHRL-STIRLADRI 679
|
250 260
....*....|....*....|....*...
gi 507682765 2115 AIMVNGKFRCLGSVQHLKNRFGDGYTIV 2142
Cdd:COG2274 680 IVLDKGRIVEDGTHEELLARKGLYAELV 707
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
900-1109 |
6.71e-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: 80.34 E-value: 6.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVC 978
Cdd:cd03246 2 EVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMlTVEEHIwfyaclkglsekhvkvemeqmaldvglppsklksktsqLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03246 82 PQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMdEADILGDRIAIISHGKL 1109
Cdd:cd03246 123 PNSHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1912-2136 |
6.95e-17 |
|
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: 86.74 E-value: 6.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:COG4987 334 LELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQ----FDA-ITE-LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL-LKYGEkYAGNYSGGNKRKLSTAMA 2058
Cdd:COG4987 414 VPQrphlFDTtLREnLRLARPDAtdeELWAALERV------GLGDW-LAALpdGLdTWLGE-GGRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGKFRCLGSVQHLKNRFG 2136
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLA-DLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
878-1127 |
1.05e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.03 E-value: 1.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 878 SSQKGVSEIrMEEEP------THL----KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILT 947
Cdd:PRK11160 309 ASARRINEI-TEQKPevtfptTSTaaadQVSLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLT 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 948 GLFPPTSGTAYILGKDIR--SEmSTIRQNLGVCPQHNVLF-----DMLTVeehiwfyACLKGLSEKhvkveMEQMALDVG 1020
Cdd:PRK11160 388 RAWDPQQGEILLNGQPIAdySE-AALRQAISVVSQRVHLFsatlrDNLLL-------AAPNASDEA-----LIEVLQQVG 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1021 LppSKLKSKTS-----------QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTH 1089
Cdd:PRK11160 455 L--EKLLEDDKglnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITH 532
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 507682765 1090 ------HMdeadilgDRIAIISHGKLCCVGSSLFLKNQLGtGYY 1127
Cdd:PRK11160 533 rltgleQF-------DRICVMDNGQIIEQGTHQELLAQQG-RYY 568
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1909-2108 |
1.06e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 82.93 E-value: 1.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG--------DTTVTRGNAFLNKNSILsN 1980
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllpddnpNSKITVDGITLTAKTVW-D 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1981 IHE----VHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLS 2054
Cdd:PRK13640 82 IREkvgiVFQN----PdnQFVGATV----GDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2055 TAMALIGGPPVVFLDEPTTGMDPKARrflwNCALSIIKE-----GRSVVLTSHSMEECE 2108
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGK----EQILKLIRKlkkknNLTVISITHDIDEAN 208
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1909-2121 |
1.18e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYRR----KRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNK--NSILSNIH 1982
Cdd:PRK13633 2 NEMIKCKNVSYKYESneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGldTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1983 EVHQNMGYCPQ------FDAITElltgrEHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYgEKYAGN-YSGGNKRKLST 2055
Cdd:PRK13633 82 DIRNKAGMVFQnpdnqiVATIVE-----EDVAFGPENLGIPPEEIRERVDESLKKVGMYEY-RRHAPHlLSGGQKQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECeALCTRMAIMVNGK 2121
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGK 221
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1912-2102 |
1.47e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 80.10 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:TIGR01189 1 LAARNLA--CSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:TIGR01189 79 GHLPGLKPELSALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEP 154
|
170 180 190
....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:TIGR01189 155 TTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1911-2121 |
1.49e-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: 81.18 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHE-VHQNM 1988
Cdd:COG0410 3 MLEVENLHAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlPPHRiARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKevgkvGEWAIRK-LGL---LKygEK---YAGNYSGGNKRKLSTAMALIG 2061
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAE-----VRADLERvYELfprLK--ERrrqRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
899-1108 |
1.69e-16 |
|
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: 81.12 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIWFYAclKGLSEKHVKVEMEQ-------MALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03251 81 VSQDVFLFND-TVAENIAYGR--PGATREEVEEAARAanahefiMELPEGYD-TVIGERGVKLSGGQRQRIAIARALLKD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTII-----LSThhMDEAdilgDRIAIISHGK 1108
Cdd:cd03251 157 PPILILDEATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
899-1109 |
1.86e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 82.06 E-value: 1.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLG 976
Cdd:PRK13642 5 LEVENLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQH-NVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKsKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK13642 85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTR-EPARLSGGQKQRVAVAGIIALRPEIII 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1056 LDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
908-1128 |
2.15e-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: 80.99 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFD 986
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MlTVEEHIwfyACLKGLSEKHVKVEMEQMA----LDVGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEP 1059
Cdd:cd03252 90 R-SIRDNI---ALADPGMSMERVIEAAKLAgahdFISELPEgydTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEA 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1060 TAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKLCCVGSSLFLKNQLGTGYYL 1128
Cdd:cd03252 166 TSALDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYL 233
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
899-1109 |
2.28e-16 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 85.15 E-value: 2.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVAL 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIwFYACLKGLSEKHVKvEMEQMA--------LDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVG 1049
Cdd:TIGR02203 411 VSQDVVLFND-TIANNI-AYGRTEQADRAEIE-RALAAAyaqdfvdkLPLGLD-TPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdeADILG-DRIAIISHGKL 1109
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRL--STIEKaDRIVVMDDGRI 545
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
898-1123 |
2.52e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 82.86 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAgktttmSILTGLFPptsgtAYILGKDIR----------SE 967
Cdd:NF000106 13 AVEVRGLVKHF--GEVKAVDGVDLDVREGTVLGVLGP*GA------A**RGALP-----AHV*GPDAGrrpwrf*twcAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 MSTIRQNLGVC-PQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSkTSQLSGGMQRKLSVALA 1046
Cdd:NF000106 80 RRALRRTIG*HrPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRA-AAKYSGGMRRRLDLAAS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIW-ELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKNQLG 1123
Cdd:NF000106 159 MIGRPAVLYLDEPTTGLDPRTRNEVWdEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
909-1090 |
3.45e-16 |
|
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: 79.46 E-value: 3.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDML 988
Cdd:cd03231 10 RDG-RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWFYACLkglsekHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR 1068
Cdd:cd03231 89 SVLENLRFWHAD------HSDEQVEEALARVGLNGFE-DRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGV 161
|
170 180
....*....|....*....|...
gi 507682765 1069 RGIWELLLKY-RQGRTIILSTHH 1090
Cdd:cd03231 162 ARFAEAMAGHcARGGMVVLTTHQ 184
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
916-1115 |
5.85e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 79.96 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLFDMLT 989
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 VEEHIWFYACLKGLS------EKHVKVEMEQMAL--DVglpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLwdEV---KDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1062 GVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSS 1115
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPT 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1934-2139 |
5.85e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 82.39 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1934 VGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL----SNIHEVH-QNMGYCPQFDAITELLTGREHVE 2008
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2009 FFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2089 SI-IKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGDGY 2139
Cdd:PRK10070 209 KLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1911-2117 |
5.98e-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: 79.40 E-value: 5.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYR-----RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNI---- 1981
Cdd:COG4778 4 LLEVENLSKTFTlhlqgGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1982 -HEVH----QNMGYCPQFdaiteL-----LTGREHVEFFALLRGVPEKE-VGKVGEWairkLGLLKYGEK----YAGNYS 2046
Cdd:COG4778 84 pREILalrrRTIGYVSQF-----LrviprVSALDVVAEPLLERGVDREEaRARAREL----LARLNLPERlwdlPPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2047 GGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRflwnCALSIIKE----GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEakarGTAIIGIFHDEEVREAVADRVVDV 225
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
903-1098 |
6.51e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 79.47 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 903 NLVKVYRDGmKVAVDGL---ALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIR-----QN 974
Cdd:PRK11629 10 NLCKRYQEG-SVQTDVLhnvSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQ-HNVLFDmLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK11629 89 LGFIYQfHHLLPD-FTALENVAMPLLIGKKKPAEINSRALEMLAAVGLE-HRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILG 1098
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
912-1113 |
6.94e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 79.89 E-value: 6.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 912 MKVAVDGLALNFYEGQ---------------ITSFLGHNGAGKTTTMSILTGLF-----PPTSGTAYILGKDIRSEMST- 970
Cdd:PRK14267 1 MKFAIETVNLRVYYGSnhvikgvdlkipqngVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPDVDp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 --IRQNLGVCPQHNVLFDMLTVEEHIWFYACLKGLS------EKHVKVEMEQMAL--DVglpPSKLKSKTSQLSGGMQRK 1040
Cdd:PRK14267 81 ieVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVkskkelDERVEWALKKAALwdEV---KDRLNDYPSNLSGGQRQR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:PRK14267 158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
899-1109 |
7.26e-16 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 79.37 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG---KDIRSEMSTIRQNL 975
Cdd:PRK09493 2 IEFKNVSKHF--GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGlkvNDPKVDERLIRQEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQHNVLFDMLTVEEHIWFYAC-LKGLSekhvKVEMEQMALD----VGLPpSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:PRK09493 80 GMVFQQFYLFPHLTALENVMFGPLrVRGAS----KEEAEKQAREllakVGLA-ERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1051 SKVVILDEPTAGVDPYSRRgiwELLLKYR----QGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRH---EVLKVMQdlaeEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
1909-2134 |
7.30e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.16 E-value: 7.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHEVHQN 1987
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYCPQfDAITELLTGR--EHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13647 81 VGLVFQ-DPDDQVFSSTvwDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNR 2134
Cdd:PRK13647 160 IVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1912-2121 |
1.01e-15 |
|
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: 76.70 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGnaflnknSILSNIHEVHqnmgyc 1991
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSG-------EILVDGKEVS------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 pqFDAITElltgrehveffALLRGVpekevgkvgeWAIRKLgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03216 66 --FASPRD-----------ARRAGI----------AMVYQL-------------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGR 159
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
923-1114 |
1.01e-15 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 83.17 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 923 FYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDIRSEMstIRQNLGVCPQHNVLFDMLTVEEHIWFYAC 999
Cdd:TIGR00955 48 AKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKE--MRAISAYVQQDDLFIPTLTVREHLMFQAH 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1000 LK---GLSEKHVKVEMEQMALDVGL---------PPSKLKSktsqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYS 1067
Cdd:TIGR00955 126 LRmprRVTKKEKRERVDEVLQALGLrkcantrigVPGRVKG----LSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 1068 RRGIWELLLKYRQGRTIILSTHHMDEADI--LGDRIAIISHGKLCCVGS 1114
Cdd:TIGR00955 202 AYSVVQVLKGLAQKGKTIICTIHQPSSELfeLFDKIILMAEGRVAYLGS 250
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
916-1110 |
1.03e-15 |
|
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: 82.57 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPT-SGTAYILGK--DIRSEMSTIRQNLGVCPQ----HNVLFDMl 988
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrHGIVPIL- 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWFyACLKGLSEK-HVKVEMEQMALDVGLppSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:TIGR02633 355 GVGKNITL-SVLKSFCFKmRIDAAAELQIIGSAI--QRLKVKTAspflpigRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1061 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLC 1110
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLaQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
899-1123 |
1.29e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 80.92 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKvyRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemSTIrQNLGVC 978
Cdd:PRK11432 7 VVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSI-QQRDIC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 P--QHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEM-EQMALdVGLppSKLKSK-TSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:PRK11432 82 MvfQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVkEALEL-VDL--AGFEDRyVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1055 ILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS---------SLFLKNQLG 1123
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSpqelyrqpaSRFMASFMG 238
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1911-2127 |
1.43e-15 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 1.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHE-VHQNM 1988
Cdd:PRK10895 3 TLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsLLPLHArARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKV-GEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVF 2067
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDrANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2068 LDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGS 2127
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
916-1110 |
1.53e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 81.97 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemstirqnlgVCPQ--------------- 980
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVT----------RSPQdglangivyisedrk 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLFDMLTVEEHIWFYAcLKGLSEKHVKV--EMEQMALD--VGLPPSKLKSKTSQ---LSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK10762 338 RDGLVLGMSVKENMSLTA-LRYFSRAGGSLkhADEQQAVSdfIRLFNIKTPSMEQAiglLSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEadILG--DRIAIISHGKLC 1110
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRIS 474
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1913-2121 |
1.58e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 1.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFL--------NKNSILSNIHEV 1984
Cdd:PRK13632 9 KVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIdgitiskeNLKEIRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNmgycP--QFDAITelltgrehVE---FFALL-RGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:PRK13632 89 FQN----PdnQFIGAT--------VEddiAFGLEnKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNGK 2121
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGK 219
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1912-2127 |
2.12e-15 |
|
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: 78.15 E-value: 2.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIHEVHQNMGYC 1991
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGV----PEKEV-GKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRserpPEAEIrAKVHE-LLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGS 2127
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
918-1154 |
2.25e-15 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 78.51 E-value: 2.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----------RSEMSTIRQNlgvcPQHNVLFDm 987
Cdd:PRK13638 19 GLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskrgllalRQQVATVFQD----PEQQIFYT- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 988 lTVEEHIWFYACLKGLSEKHVKVEMEQmALDVgLPPSKLKSKTSQ-LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:PRK13638 94 -DIDSDIAFSLRNLGVPEAEITRRVDE-ALTL-VDAQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1067 SRRGIWELLLK-YRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS--SLFLKNQLGTGYYLT---LVKKDVESSLG 1140
Cdd:PRK13638 171 GRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGApgEVFACTEAMEQAGLTqpwLVKLHTQLGLP 250
|
250
....*....|....
gi 507682765 1141 SCRNSSSTVSNLKK 1154
Cdd:PRK13638 251 LCKTETEFFHRMQK 264
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
911-1109 |
4.65e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 80.73 E-value: 4.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--SEMSTIRQNLGVCPQHNVLFDML 988
Cdd:PRK11288 16 GVK-ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIW-------FYACLKGLSEKHVKVEMEQMALDVGlPPSKLKSktsqLSGGMQRKLSVALAFVGGSKVVILDEPTA 1061
Cdd:PRK11288 95 TVAENLYlgqlphkGGIVNRRLLNYEAREQLEHLGVDID-PDTPLKY----LSIGQRQMVEIAKALARNARVIAFDEPTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1062 GVdpySRRGIwELLLKY-----RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK11288 170 SL---SAREI-EQLFRVirelrAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
899-1114 |
5.38e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.04 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYR------DGMK--------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY 958
Cdd:COG1134 5 IEVENVSKSYRlyhepsRSLKelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 959 ILGKdirseMSTIrqnLGVcpqhNVLFDM-LTVEEHIWFYACLKGLSEKhvkvEMEQM------------ALDvgLPpsk 1025
Cdd:COG1134 85 VNGR-----VSAL---LEL----GAGFHPeLTGRENIYLNGRLLGLSRK----EIDEKfdeivefaelgdFID--QP--- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1026 LKSktsqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY----SRRGIWELLlkyRQGRTIILSTHHMDEADILGDRI 1101
Cdd:COG1134 144 VKT----YSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIRELR---ESGRTVIFVSHSMGAVRRLCDRA 216
|
250
....*....|...
gi 507682765 1102 AIISHGKLCCVGS 1114
Cdd:COG1134 217 IWLEKGRLVMDGD 229
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
1912-2121 |
6.11e-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: 76.45 E-value: 6.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGNAFL---NKNSILSNIHE 1983
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLdgkDIYDLDVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 VHQNMGYCPQ----FDAitellTGREHVEFFALLRGV-PEKEVGKVGEWAIRKLGLLKYGEK--YAGNYSGGNKRKLSTA 2056
Cdd:cd03260 79 LRRRVGMVFQkpnpFPG-----SIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEE-LIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGR 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
918-1131 |
8.19e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 8.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwF 996
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SVRENI-A 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 997 YACLKGLSEKHVKVEMEQMALD--VGLPP---SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGI 1071
Cdd:TIGR00958 577 YGLTDTPDEEIMAAAKAANAHDfiMEFPNgydTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLL 656
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1072 WEllLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKNQlgTGYYLTLV 1131
Cdd:TIGR00958 657 QE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSVVEMGTHKQLMED--QGCYKHLV 711
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
899-1121 |
1.30e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 76.20 E-value: 1.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMkvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP----PTSGTAYI---------LGKDIR 965
Cdd:PRK09984 5 IRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvqregrLARDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 966 SEmstiRQNLGVCPQHNVLFDMLTVEEHI---------WFYACLKGLSEKHvKVEMEQMALDVGLPPSKlKSKTSQLSGG 1036
Cdd:PRK09984 83 KS----RANTGYIFQQFNLVNRLSVLENVligalgstpFWRTCFSWFTREQ-KQRALQALTRVGMVHFA-HQRVSTLSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1037 MQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....*..
gi 507682765 1115 SLFLKNQ 1121
Cdd:PRK09984 237 SQQFDNE 243
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1936-2106 |
1.57e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.70 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAiTELL--TGREHVE 2008
Cdd:PRK13643 29 VKKGSYTALIGHTGSGKSTLLQHLNGllqptEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPE-SQLFeeTVLKDVA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2009 FFALLRGVPEKEVGKVGEWAIRKLGLLK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCA 2087
Cdd:PRK13643 108 FGPQNFGIPKEKAEKIAAEKLEMVGLADeFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLF 187
|
170
....*....|....*....
gi 507682765 2088 LSIIKEGRSVVLTSHSMEE 2106
Cdd:PRK13643 188 ESIHQSGQTVVLVTHLMDD 206
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
899-1114 |
1.63e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 77.43 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGVC 978
Cdd:PRK10851 3 IEIANIKKSF-GRTQVLND-ISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQHNVLFDMLTVEEHIWFyaclkGLS-----------EKHVKV----EMEQMALDVGLPPsklksktSQLSGGMQRKLSV 1043
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAF-----GLTvlprrerpnaaAIKAKVtqllEMVQLAHLADRYP-------AQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELL------LKYrqgrTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLrqlheeLKF----TSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1944-2102 |
1.69e-14 |
|
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: 74.20 E-value: 1.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1944 LLGVNGAGKSSTFKMLTGDTT--VTRGNAFLNKNSILSNIHEVhqnMGYCPQFDAITELLTGREHVEFFALLRGVpekev 2021
Cdd:cd03232 38 LMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNFQRS---TGYVEQQDVHSPNLTVREALRFSALLRGL----- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2022 gkvgewairklgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCALSiikeGRSV 2097
Cdd:cd03232 110 ------------------------SVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAynivRFLKKLADS----GQAI 161
|
....*
gi 507682765 2098 VLTSH 2102
Cdd:cd03232 162 LCTIH 166
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
899-1114 |
1.74e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 76.18 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLG 976
Cdd:PRK13644 2 IRLENVSYSYPDGTP-ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQH-NVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK13644 81 IVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKT-LSGGQGQCVALAGILTMEPECLI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLK-YRQGRTIILSTHHMDEADIlGDRIAIISHGKLCCVGS 1114
Cdd:PRK13644 160 FDEVTSMLDPDSGIAVLERIKKlHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
903-1120 |
1.77e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 75.96 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 903 NLVKV----YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQN 974
Cdd:PRK11831 6 NLVDMrgvsFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMLTVEEHIWFyaclkGLSEK--------HVKVEMEQMAldVGLPPSKlKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAY-----PLREHtqlpapllHSTVMMKLEA--VGLRGAA-KLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFLKN 1120
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLIseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
909-1109 |
1.81e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 75.78 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR--------------SEMSTIRQN 974
Cdd:PRK10619 14 RYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMLTVEEHIwFYACLK--GLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:PRK10619 94 LTMVFQHFNLWSHMTVLENV-MEAPIQvlGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPE 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1912-2129 |
2.27e-14 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 75.19 E-value: 2.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:PRK13548 3 LEARNLS--VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALI------GGPP 2064
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2065 VVFLDEPTTGMDPK--------ARRFLWNCALSIIkegrsVVLtsHSMEECEALCTRMAIMVNGKFRCLGSVQ 2129
Cdd:PRK13548 161 WLLLDEPTSALDLAhqhhvlrlARQLAHERGLAVI-----VVL--HDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
911-1108 |
2.31e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 78.51 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR---------SEMSTIRQNLGVCPQh 981
Cdd:PRK10762 16 GVK-ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpkssqeAGIGIIHQELNLIPQ- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 982 nvlfdmLTVEEHIW----FYACLKGLSEKHVKVEMEQMALDVGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILD 1057
Cdd:PRK10762 94 ------LTIAENIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSS-DKLVGELSIGEQQMVEIAKVLSFESKVIIMD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1058 EPT-AGVDPYSR---RGIWELllkYRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK10762 167 EPTdALTDTETEslfRVIREL---KSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1890-2131 |
2.45e-14 |
|
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: 78.65 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1890 DEDEDVRRERQRILDGGGQNDIlEIKELTKIYRrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGN 1969
Cdd:COG4988 316 DAPEPAAPAGTAPLPAAGPPSI-ELEDVSFSYP-GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1970 AFLNKNSILS-NIHEVHQNMGYCPQFdaiTELLTG--REHVEFFAllRGVPEKEVgkvgEWAIRKLGLLKY--------- 2037
Cdd:COG4988 394 ILINGVDLSDlDPASWRRQIAWVPQN---PYLFAGtiRENLRLGR--PDASDEEL----EAALEAAGLDEFvaalpdgld 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2038 ---GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSHSMEECeALCTRM 2114
Cdd:COG4988 465 tplGEG-GRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQ-ALRRLAKGRTVILITHRLALL-AQADRI 541
|
250
....*....|....*..
gi 507682765 2115 AIMVNGKFRCLGSVQHL 2131
Cdd:COG4988 542 LVLDDGRIVEQGTHEEL 558
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
901-1109 |
2.45e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 78.18 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyILGKDIRsemstirqnLGVCPQ 980
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-SIPKGLR---------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLFDMLTVEEHIwfyacLKGLSE-KHVKVEMEQM----------------------ALD--------------VGLPP 1023
Cdd:COG0488 69 EPPLDDDLTVLDTV-----LDGDAElRALEAELEELeaklaepdedlerlaelqeefeALGgweaearaeeilsgLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1024 SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRgiW--ELLLKYRqGrTIILSTHhmDEA--DILGD 1099
Cdd:COG0488 144 EDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNYP-G-TVLVVSH--DRYflDRVAT 217
|
250
....*....|
gi 507682765 1100 RIAIISHGKL 1109
Cdd:COG0488 218 RILELDRGKL 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1928-2133 |
2.99e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 2.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN---------KNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINninynkldhKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1999 ELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2078
Cdd:PRK09700 100 NLYIGRHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNK 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2079 ARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:PRK09700 180 EVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
902-1102 |
3.60e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 74.82 E-value: 3.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSI---LTGLFPP--TSGTAYILGKDI---RSEMSTIRQ 973
Cdd:PRK14243 14 ENLNVYY--GSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLyapDVDPVEVRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 974 NLGVCPQHNVLFDMlTVEEHIWFYACL---KGLSEKHVKVEMEQMAL--DVglpPSKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK14243 92 RIGMVFQKPNPFPK-SIYDNIAYGARIngyKGDMDELVERSLRQAALwdEV---KDKLKQSGLSLSGGQQQRLCIARAIA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIA 1102
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
899-1109 |
3.73e-14 |
|
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: 74.48 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTA-YILGKDIRSEMSTI------ 971
Cdd:TIGR02323 4 LQVSGLSKSY--GGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTAtYIMRSGAELELYQLseaerr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 972 ---RQNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKH---VKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:TIGR02323 82 rlmRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARHygnIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIAR 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:TIGR02323 162 NLVTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
888-1109 |
3.79e-14 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 74.69 E-value: 3.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 888 MEEEPTHLKLGVSIQNLvKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTT---TMSILTGLFPP--TSGTAYILGK 962
Cdd:COG1117 1 MTAPASTLEPKIEVRNL-NVYYGD-KQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 963 DIRS---EMSTIRQNLGVCPQHNVLFDMlTVEEHIWFYACLKGLSEKHVKVEMEQMAL-DVGLPP---SKLKSKTSQLSG 1035
Cdd:COG1117 79 DIYDpdvDVVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLrKAALWDevkDRLKKSALGLSG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1036 GMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGEL 231
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
899-1109 |
3.85e-14 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 74.40 E-value: 3.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI------LGKDIRSEMSTIR 972
Cdd:PRK11264 4 IEVKNLVKKFHG--QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 ---QNLGVCPQHNVLFDMLTVEEHIwfyacLKG--LSEKHVKVEMEQMALD----VGLPpSKLKSKTSQLSGGMQRKLSV 1043
Cdd:PRK11264 82 qlrQHVGFVFQNFNLFPHRTVLENI-----IEGpvIVKGEPKEEATARAREllakVGLA-GKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPysrRGIWELLLKYRQ----GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDP---ELVGEVLNTIRQlaqeKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1912-2102 |
4.53e-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: 73.30 E-value: 4.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03231 1 LEADELT--CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQVEE------ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 507682765 2072 TTGMDPK-----ARRFLWNCAlsiikEGRSVVLTSH 2102
Cdd:cd03231 153 TTALDKAgvarfAEAMAGHCA-----RGGMVVLTTH 183
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
898-1117 |
4.61e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 74.35 E-value: 4.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLVkVYRDGmkVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP----TSGTAYILGK-----DIRSEM 968
Cdd:PRK10418 4 QIELRNIA-LQAAQ--PLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKpvapcALRGRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 -STIRQNlgvcPQH--NVLFDMLT--VEEhiwfyacLKGLSEKHVKVEMEQMALDVGL--PPSKLKSKTSQLSGGMQRKL 1041
Cdd:PRK10418 81 iATIMQN----PRSafNPLHTMHThaRET-------CLALGKPADDATLTAALEAVGLenAARVLKLYPFEMSGGMLQRM 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1042 SVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL--CCVGSSLF 1117
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIveQGDVETLF 229
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
918-1109 |
5.06e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 77.40 E-value: 5.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 918 GLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGV--CPQHNVLFDMLTVEEHIW 995
Cdd:PRK15439 29 GIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIylVPQEPLLFPNLSVKENIL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 996 FyaclkGLSEKHVKVE-MEQM--ALDVGLppsKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR---- 1068
Cdd:PRK15439 109 F-----GLPKRQASMQkMKQLlaALGCQL---DLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETerlf 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 1069 RGIWELLlkyRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK15439 181 SRIRELL---AQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1911-2117 |
5.47e-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: 75.47 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG---DTTVTRGNAFLNKNSILS----NI 1981
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLKlsekEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1982 HEV-HQNMGYCPQfDAITEL---LTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGlLKYGEKYAGNY----SGGNKRK 2052
Cdd:COG0444 81 RKIrGREIQMIFQ-DPMTSLnpvMTVGDQIaEPLRIHGGLSKAEARERAIELLERVG-LPDPERRLDRYphelSGGMRQR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2053 LSTAMALIGGPPVVFLDEPTTGMDP--KARrflwncALSIIKE-----GRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVtiQAQ------ILNLLKDlqrelGLAILFITHDLGVVAEIADRVAVM 224
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1910-2180 |
5.63e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 74.77 E-value: 5.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1910 DILEIKELTKIYRR-KRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFL--------NKNSILSN 1980
Cdd:PRK13650 3 NIIEVKNLTFKYKEdQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIdgdllteeNVWDIRHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1981 IHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:PRK13650 83 IGMVFQN----PdnQFVGATV----EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECeALCTRMAIMVNGKFRCLGSVQHLKNRFGD 2137
Cdd:PRK13650 155 VAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGND 233
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 507682765 2138 GYTIVVRIAGSNPDLKPVQEfFGLAFPGSVLKEKHrnmLQYQL 2180
Cdd:PRK13650 234 LLQLGLDIPFTTSLVQSLRQ-NGYDLPEGYLTEKE---LEEQL 272
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1926-2072 |
5.94e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.03 E-value: 5.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsilSNIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:COG0488 11 RPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG---LRIGYLPQEPPLDDDLTVLDTVLDGDA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2006 HV-----EFFALLRGVPE-----KEVGKV-------GEWAIR--------KLGL-LKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:COG0488 88 ELraleaELEELEAKLAEpdedlERLAELqeefealGGWEAEaraeeilsGLGFpEEDLDRPVSELSGGWRRRVALARAL 167
|
170
....*....|...
gi 507682765 2060 IGGPPVVFLDEPT 2072
Cdd:COG0488 168 LSEPDLLLLDEPT 180
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
901-1109 |
7.38e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 76.75 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKvyRDGMKVAVDGLALNfyEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTIRQNLGVC 978
Cdd:PRK09700 268 VRNVTS--RDRKKVRDISFSVC--RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 PQH---NVLFDMLTVEEHIWFYACLK--------GL-SEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK09700 344 TESrrdNGFFPNFSIAQNMAISRSLKdggykgamGLfHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1913-2128 |
7.71e-14 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 75.22 E-value: 7.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSN--IHEVHQ 1986
Cdd:PRK11153 3 ELKNISKVFPQGGRTihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtaLSEkeLRKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQ-FDaiteLLTGREHVEFFAL---LRGVPEKEVGK-VGEwairkL----GLLKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:PRK11153 83 QIGMIFQhFN----LLSSRTVFDNVALpleLAGTPKAEIKArVTE-----LlelvGLSDKADRYPAQLSGGQKQRVAIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2058 ALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSV 2128
Cdd:PRK11153 154 ALASNPKVLLCDEATSALDPATTRSI----LELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTV 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
899-1109 |
9.74e-14 |
|
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: 72.85 E-value: 9.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVY--RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIR 972
Cdd:COG4181 9 IELRGLTKTVgtGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldEDARARLR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 973 -QNLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEkhvkveMEQMALD----VGL-------PpsklksktSQLSGGMQRK 1040
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRD------ARARARAllerVGLghrldhyP--------AQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDEADIL-GDRIAIISHGKL 1109
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLDAATGEQIIDLLfeLNRERGTTLVLVTH--DPALAArCDRVLRLRAGRL 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1912-2122 |
1.11e-13 |
|
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: 71.19 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQfdaitelltgREHVeFFALLRgvpeKEVGKvgewairklgllkygekyagNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03247 81 NQ----------RPYL-FDTTLR----NNLGR--------------------RFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEgRSVVLTSHSMEECEALcTRMAIMVNGKF 2122
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1939-2121 |
1.20e-13 |
|
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: 72.33 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN--------KNSILSniheVHQ-NMGYCPQFDAITELLTGREHVEF 2009
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfdsrKKINLP----PQQrKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2010 fALLRGVPEKEVGKVGEWAIRkLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2089
Cdd:cd03297 99 -GLKRKRNREDRISVDELLDL-LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQ 176
|
170 180 190
....*....|....*....|....*....|...
gi 507682765 2090 IIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03297 177 IKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGR 209
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
910-1109 |
1.30e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.15 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMl 988
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIW----------FYACLKgLSEKHVKVEMEQMALD--VGlppsklkSKTSQLSGGMQRKLSVALAFVGGSKVVIL 1056
Cdd:PRK13657 424 SIEDNIRvgrpdatdeeMRAAAE-RAQAHDFIERKPDGYDtvVG-------ERGRQLSGGERQRLAIARALLKDPPILIL 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1057 DEPTAGVDPYSRRGIWELLLKYRQGRT--II---LSThhMDEAdilgDRIAIISHGKL 1109
Cdd:PRK13657 496 DEATSALDVETEAKVKAALDELMKGRTtfIIahrLST--VRNA----DRILVFDNGRV 547
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
908-1107 |
1.45e-13 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 72.44 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMS--TIRQNLGVCPQHNVLF 985
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDI-STLKpeIYRQQVSYCAQTPTLF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DMlTVEEHIWFYACLkglseKHVKVEMEQMALDV---GLPPSKLKSKTSQLSGGMQRKLSVA--LAFVggSKVVILDEPT 1060
Cdd:PRK10247 94 GD-TVYDNLIFPWQI-----RNQQPDPAIFLDDLerfALPDTILTKNIAELSGGEKQRISLIrnLQFM--PKVLLLDEIT 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 1061 AGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHG 1107
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
885-1109 |
1.90e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 75.45 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 885 EIRMEEEPTHLKLG---VSIQNLVkVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG 961
Cdd:COG3845 241 EVLLRVEKAPAEPGevvLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 962 KDI---------RSEMSTI---RQNLGVCPqhnvlfDMlTVEEHIWF-------YACLKGLSEKHVKVEMEQM--ALDVg 1020
Cdd:COG3845 320 EDItglsprerrRLGVAYIpedRLGRGLVP------DM-SVAENLILgryrrppFSRGGFLDRKAIRAFAEELieEFDV- 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1021 LPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGD 1099
Cdd:COG3845 392 RTPG-PDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSD 470
|
250
....*....|
gi 507682765 1100 RIAIISHGKL 1109
Cdd:COG3845 471 RIAVMYEGRI 480
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
932-1109 |
2.12e-13 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 71.92 E-value: 2.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 932 LGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSeMSTIRQNLGVCPQHNVLFDMLTVEEHIWF--YACLKgLSEKHvK 1009
Cdd:PRK10771 31 LGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTT-TPPSRRPVSMLFQENNLFSHLTVAQNIGLglNPGLK-LNAAQ-R 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1010 VEMEQMALDVGLpPSKLKSKTSQLSGGmQRKlSVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TII 1085
Cdd:PRK10771 108 EKLHAIARQMGI-EDLLARLPGQLSGG-QRQ-RVALArcLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERqlTLL 184
|
170 180
....*....|....*....|....
gi 507682765 1086 LSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK10771 185 MVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
900-1114 |
2.13e-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: 71.02 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFP---PTSGTAYILGKDIrSEMST---IRQ 973
Cdd:cd03217 2 EIKDL-HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLPPeerARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 974 NLGVCPQHNVLFDMLTVEEHIWFyaclkglsekhvkvemeqmaLDVGLppsklksktsqlSGGMQRKLSVALAFVGGSKV 1053
Cdd:cd03217 78 GIFLAFQYPPEIPGVKNADFLRY--------------------VNEGF------------SGGEKKRNEILQLLLLEPDL 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEAD-ILGDRIAIISHGKLCCVGS 1114
Cdd:cd03217 126 AILDEPDSGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDyIKPDRVHVLYDGRIVKSGD 188
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
899-1113 |
2.57e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 74.49 E-value: 2.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVkVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMS-TIRQNLGV 977
Cdd:PRK09536 4 IDVSDLS-VEFGDTTV-LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSArAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVL---FDMLTVEE-----HIWFYACLKGLSEKHVKVEMEQmaldVGLPPSKLKSKTSqLSGGMQRKLSVALAFVG 1049
Cdd:PRK09536 82 VPQDTSLsfeFDVRQVVEmgrtpHRSRFDTWTETDRAAVERAMER----TGVAQFADRPVTS-LSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1050 GSKVVILDEPTAGVDpySRRGIWELLLKYR---QGRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:PRK09536 157 ATPVLLLDEPTASLD--INHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
915-1109 |
2.85e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.48 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQH--------NVLF 985
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHIGIVFQNpdnqfvgsIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DM-LTVEEHIwfyaclkgLSEKHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PRK13648 104 DVaFGLENHA--------VPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 1065 PYSRRGIWELLLKYRQGR--TIILSTHHMDEAdILGDRIAIISHGKL 1109
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTV 220
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1908-2121 |
3.13e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 72.36 E-value: 3.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGNAFLNKNS---ILS 1979
Cdd:PRK13635 2 KEEIIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlllpeAGTITVGGMVLSEETvwdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHEVHQNmgycP--QFDAITElltgREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:PRK13635 82 QVGMVFQN----PdnQFVGATV----QDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2058 ALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNGK 2121
Cdd:PRK13635 154 VLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGE 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1911-2145 |
3.88e-13 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 71.97 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFK----MLTGDTTVTR-----GNAFLNKNSILSNI 1981
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGShiellGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1982 HEVHQNMGYCPQFDAITELLTGREHVEFFAL---------LRGVPEKEVGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRK 2052
Cdd:PRK09984 82 RKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2053 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIK-EGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240
|
250
....*....|....*
gi 507682765 2132 KN-RFGDGYTIVVRI 2145
Cdd:PRK09984 241 DNeRFDHLYRSINRV 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
898-1102 |
4.78e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.61 E-value: 4.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLvKVYRDGMKVaVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTS-----GTAYILGKDI---RSEMS 969
Cdd:PRK14258 7 AIKVNNL-SFYYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNLG-VCPQHNvLFDMlTVEEHIWFYACLKGLsekHVKVEM----EQMALDVGL---PPSKLKSKTSQLSGGMQRKL 1041
Cdd:PRK14258 85 RLRRQVSmVHPKPN-LFPM-SVYDNVAYGVKIVGW---RPKLEIddivESALKDADLwdeIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1042 SVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIA 1102
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
1912-2104 |
5.03e-13 |
|
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: 70.25 E-value: 5.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS---NIHEVHQNM 1988
Cdd:cd03262 1 IEIKNLHKSF--GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQ----------FDAITELLTgrehveffaLLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:cd03262 79 GMVFQqfnlfphltvLENITLAPI---------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSM 2104
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEM 195
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
900-1109 |
5.58e-13 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 71.64 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDG-------MKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEM 968
Cdd:PRK10419 5 NVSGLSHHYAHGglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 STIRQNL---------GVCPQHNVLFDMLTVEEHiwfyacLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQR 1039
Cdd:PRK10419 85 KAFRRDIqmvfqdsisAVNPRKTVREIIREPLRH------LLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1040 KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
911-1108 |
5.78e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 74.00 E-value: 5.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI---------RSEMSTIRQNLGVCPQH 981
Cdd:PRK10982 10 GVK-ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksskealENGISMVHQELNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 982 NVLfdmltveEHIWF--YAcLKGLSEKHVKVEMEQMA----LDVGLPPsklKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK10982 89 SVM-------DNMWLgrYP-TKGMFVDQDKMYRDTKAifdeLDIDIDP---RAKVATLSVSQMQMIEIAKAFSYNAKIVI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK10982 158 MDEPTSSLTEKEVNHLFTIIRKLKeRGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
899-1108 |
5.97e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 74.37 E-value: 5.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:PRK10790 341 IDIDNVSFAYRDDNLVLQN-INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNV-----LFDMLTVEEHIwfyaclkglSEKHV--KVEMEQMALDV-GLPP---SKLKSKTSQLSGGMQRKLSVALA 1046
Cdd:PRK10790 420 VQQDPVvladtFLANVTLGRDI---------SEEQVwqALETVQLAELArSLPDglyTPLGEQGNNLSVGQKQLLALARV 490
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1047 FVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMD---EAdilgDRIAIISHGK 1108
Cdd:PRK10790 491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQ 551
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
899-1108 |
7.31e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 73.71 E-value: 7.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDI--RSEMSTIRQN 974
Cdd:TIGR02633 2 LEMKGIVKTF-GGVK-ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLkaSNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLFDMLTVEEHIWF--YACLKG--LSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLgnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIrdLK-AHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1911-2121 |
7.51e-13 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 72.03 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSN--IHEV 1984
Cdd:COG1135 1 MIELENLSKTFPTKGGPvtALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtaLSEreLRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQ-FDaiteLLTGR---EHVEfFAL-LRGVPEKEV-GKVGEwairkL----GLLKYGEKYAGNYSGGNKRKLS 2054
Cdd:COG1135 81 RRKIGMIFQhFN----LLSSRtvaENVA-LPLeIAGVPKAEIrKRVAE-----LlelvGLSDKADAYPSQLSGGQKQRVG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2055 TAMALIGGPPVVFLDEPTTGMDPKARRflwncalSI---IKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTR-------SIldlLKDinrelGLTIVLITHEMDVVRRICDRVAVLENGR 218
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1911-2121 |
7.69e-13 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 70.51 E-value: 7.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKiyRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS---NIHEVHQN 1987
Cdd:PRK09493 1 MIEFKNVSK--HFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYC-PQFDAITELlTGREHVEFFAL-LRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK09493 79 AGMVfQQFYLFPHL-TALENVMFGPLrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGR 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1908-2120 |
8.38e-13 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 8.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAflnknSIL--SNIHEVH 1985
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILgqPTRQALQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNM-GYCPQ-------FDAITE--LLTGRE-HVeffALLRgVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLS 2054
Cdd:PRK15056 77 KNLvAYVPQseevdwsFPVLVEdvVMMGRYgHM---GWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2055 TAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTrMAIMVNG 2120
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1928-2108 |
8.91e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 8.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIH--EVHQNMGYCPQfdaitEL----- 2000
Cdd:NF033858 16 ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHrrAVCPRIAYMPQ-----GLgknly 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2001 --LTGREHVEFFALLRGVPEKEvgkvGEWAIRKL----GLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2074
Cdd:NF033858 91 ptLSVFENLDFFGRLFGQDAAE----RRRRIDELlratGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTG 166
|
170 180 190
....*....|....*....|....*....|....*....
gi 507682765 2075 MDPKARRFLWncALsI--IKEGR---SVVLTSHSMEECE 2108
Cdd:NF033858 167 VDPLSRRQFW--EL-IdrIRAERpgmSVLVATAYMEEAE 202
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
926-1089 |
1.19e-12 |
|
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: 68.81 E-value: 1.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSIL-----TGLfppTSGTAYILGKDIRSemsTIRQNLGVCPQHNVLFDMLTVEEHIWFYACL 1000
Cdd:cd03232 33 GTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLDK---NFQRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1001 KGLSekhvkVEmeqmaldvglppsklksktsqlsggmQRK-LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY- 1078
Cdd:cd03232 107 RGLS-----VE--------------------------QRKrLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLa 155
|
170
....*....|.
gi 507682765 1079 RQGRTIILSTH 1089
Cdd:cd03232 156 DSGQAILCTIH 166
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1929-2120 |
1.61e-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: 1.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1929 VDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHE---VHQNMGYCPqfdaiteLLTGRE 2005
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDrmvVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2006 HVEFF--ALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2083
Cdd:TIGR01184 74 NIALAvdRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 2084 WNCALSIIKEGR-SVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:TIGR01184 154 QEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
913-1109 |
1.70e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 70.12 E-value: 1.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAY-----ILGKDIRS--EMSTIRQNLGVCPQHNVLF 985
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYsgdvlLGGRSIFNyrDVLEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DMLTVEEHIWFYACLKGLSEKHVKVEMEQMALDVGL---PPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 1063 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1911-2121 |
1.83e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 72.36 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTkiyrrkRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHE-VHQNM 1988
Cdd:COG1129 256 VLEVEGLS------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVrIRSPRDaIRAGI 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQ-------------FDAITelLTGREHVEFFALLRgvpEKEVGKVGEWAIRKLGLlKYG--EKYAGNYSGGNKRKL 2053
Cdd:COG1129 330 AYVPEdrkgeglvldlsiRENIT--LASLDRLSRGGLLD---RRRERALAEEYIKRLRI-KTPspEQPVGNLSGGNQQKV 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2054 STAMALIGGPPVVFLDEPTTGMDPKAR----RFLWNCAlsiiKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG1129 404 VLAKWLATDPKVLILDEPTRGIDVGAKaeiyRLIRELA----AEGKAVIVISSELPELLGLSDRILVMREGR 471
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1926-2140 |
2.07e-12 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 69.34 E-value: 2.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHE---VHQNMGYCPQFDAItellt 2002
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAErgvVFQNEGLLPWRNVQ----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2003 grEHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2082
Cdd:PRK11248 89 --DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2083 LWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRClgsVQHLKNRFGDGYT 2140
Cdd:PRK11248 167 MQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPGPGRV---VERLPLNFARRFV 222
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
914-1114 |
2.18e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.19 E-value: 2.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 914 VAVDG----LALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIR----SEMSTIRQNLgvCPQHNVLF 985
Cdd:PRK03695 6 VAVSTrlgpLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEawsaAELARHRAYL--SQQQTPPF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 DMltveeHIWFYACL---KGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGG-MQRklsVALAFV---------GGSK 1052
Cdd:PRK03695 83 AM-----PVFQYLTLhqpDKTRTEAVASALNEVAEALGLDD-KLGRSVNQLSGGeWQR---VRLAAVvlqvwpdinPAGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK03695 154 LLLLDEPMNSLDVAQQAALDRLLSELcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGR 216
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1911-2122 |
2.24e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 71.97 E-value: 2.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrkrkPAV---DRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHE--- 1983
Cdd:COG1129 4 LLEMRGISKSF-----GGVkalDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrFRSPRDaqa 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 -----VHQNMGYCPQFDaITE-LLTGREhveffallrgvpekevgkvgewaIRKLGLLKYGEKYA--------------- 2042
Cdd:COG1129 79 agiaiIHQELNLVPNLS-VAEnIFLGRE-----------------------PRRGGLIDWRAMRRrarellarlgldidp 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2043 ----GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIK----EGRSVVLTSHSMEECEALCTRM 2114
Cdd:COG1129 135 dtpvGDLSVAQQQLVEIARALSRDARVLILDEPTASLTEREVERL----FRIIRrlkaQGVAIIYISHRLDEVFEIADRV 210
|
....*...
gi 507682765 2115 AIMVNGKF 2122
Cdd:COG1129 211 TVLRDGRL 218
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1928-2121 |
2.27e-12 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 69.25 E-value: 2.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSNiHEV--------HQNMGYCPQFDAI 1997
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPG-HQIarmgvvrtFQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1998 TELLTGR-EHVE--FFALLRGVP-----EKE-VGKVGEWaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:PRK11300 99 ENLLVAQhQQLKtgLFSGLLKTPafrraESEaLDRAATW-LERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2069 DEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11300 178 DEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1927-2103 |
2.86e-12 |
|
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: 71.62 E-value: 2.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIH-EVHQNMGYCPQ----FDA-ITE- 1999
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQdEVRRRVSVCAQdahlFDTtVREn 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2000 LLTGREHV---EFFALLRGVpekevgKVGEWaIRKL--GL-LKYGEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTT 2073
Cdd:TIGR02868 429 LRLARPDAtdeELWAALERV------GLADW-LRALpdGLdTVLGEG-GARLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|
gi 507682765 2074 GMDPKARRFLWNCALSIIkEGRSVVLTSHS 2103
Cdd:TIGR02868 501 HLDAETADELLEDLLAAL-SGRTVVLITHH 529
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1879-2121 |
3.02e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.74 E-value: 3.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1879 RAVKTKFLPLNDEDEDVRRERqrildgggqndILEIKELTkiyRRKRKPAVDrICVGIPRGECFGLLGVNGAGKSSTFKM 1958
Cdd:PRK09700 244 RELQNRFNAMKENVSNLAHET-----------VFEVRNVT---SRDRKKVRD-ISFSVCRGEILGFAGLVGSGRTELMNC 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1959 LTGDTTVTRGNAFLN--KNSILSNIHEVHQNMGYcpqfdaITElltGREHVEFF---------ALLRGVpeKEVGKVGEW 2027
Cdd:PRK09700 309 LFGVDKRAGGEIRLNgkDISPRSPLDAVKKGMAY------ITE---SRRDNGFFpnfsiaqnmAISRSL--KDGGYKGAM 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2028 AI-------------RKLGLLKYG--EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIK 2092
Cdd:PRK09700 378 GLfhevdeqrtaenqRELLALKCHsvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLAD 457
|
250 260
....*....|....*....|....*....
gi 507682765 2093 EGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK09700 458 DGKVILMVSSELPEIITVCDRIAVFCEGR 486
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1912-2117 |
3.15e-12 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 69.12 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIY--RRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHE---VHQ 1986
Cdd:COG4525 4 LTVRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADrgvVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NmgycpqfDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:COG4525 84 K-------DALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSI-IKEGRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:COG4525 157 LMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1939-2125 |
3.32e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTtvtRGNAFLNKnsILSN----IHEVHQNMGYCPQFDAITELLTGREHVEFFALLR 2014
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRI---QGNNFTGT--ILANnrkpTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2015 ---GVPEKEVGKVGEWAIRKLGLLKYGEKYAGN-----YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNC 2086
Cdd:PLN03211 169 lpkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 2087 ALSIIKEGRSVVLtshSMEECEALCTRM--AIMVNGKFRCL 2125
Cdd:PLN03211 249 LGSLAQKGKTIVT---SMHQPSSRVYQMfdSVLVLSEGRCL 286
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1911-2121 |
3.34e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.89 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMG 1989
Cdd:PRK11231 2 TLRTENLTVGYGTKR--ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDAITELLTGREHVE--------FFALLRGVPEKEVgkvgEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK11231 80 LLPQHHLTPEGITVRELVAygrspwlsLWGRLSAEDNARV----NQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11231 156 DTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGH 215
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1907-2119 |
3.34e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 69.01 E-value: 3.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1907 GQNDILEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI----LSNIH 1982
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAItddnFEKLR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1983 E----VHQN-----MGYCPQFDaitelltgrehVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKL 2053
Cdd:PRK13648 83 KhigiVFQNpdnqfVGSIVKYD-----------VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2054 STAMALIGGPPVVFLDEPTTGMDPKARRFLWNCaLSIIKEGRSVVLTSHSMEECEALCTRMAIMVN 2119
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDL-VRKVKSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1912-2102 |
3.55e-12 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.52 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIyrRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYC 1991
Cdd:PRK13538 2 LEARNLACE--RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFALLRGVPEKEVgkvgEW-AIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:PRK13538 80 GHQPGIKTELTALENLRFYQRLHGPGDDEA----LWeALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 507682765 2071 PTTGMDPKA-----RRFLWNCAlsiikEGRSVVLTSH 2102
Cdd:PRK13538 156 PFTAIDKQGvarleALLAQHAE-----QGGMVILTTH 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1883-2102 |
3.58e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 72.45 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1883 TKFLPLNDEDEDVRRERQRILDGGGqnDILEIKELT---KIYRRKRK--PAVDRICvgIPrGECFGLLGVNGAGKSSTFK 1957
Cdd:TIGR00956 733 LGSTDLTDESDDVNDEKDMEKESGE--DIFHWRNLTyevKIKKEKRVilNNVDGWV--KP-GTLTALMGASGAGKTTLLN 807
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1958 MLTGDTT---VTRGNAFLNKNSILSNIHevhQNMGYCPQFDAITELLTGREHVEFFALLR---GVPEKEVGKVGEWAIRK 2031
Cdd:TIGR00956 808 VLAERVTtgvITGGDRLVNGRPLDSSFQ---RSIGYVQQQDLHLPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKL 884
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2032 LGLLKYGEKYAGNYSGG----NKRKLSTAMALIGGPP-VVFLDEPTTGMDPKArrflwncALSIIK-------EGRSVVL 2099
Cdd:TIGR00956 885 LEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQT-------AWSICKlmrkladHGQAILC 957
|
...
gi 507682765 2100 TSH 2102
Cdd:TIGR00956 958 TIH 960
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1927-2191 |
5.31e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 68.86 E-value: 5.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN--KNSILSNIHEVHQNMGYCPQfDAITELL--T 2002
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgiDTGDFSKLQGIRKLVGIVFQ-NPETQFVgrT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2003 GREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2082
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2083 LWNCALSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGKFRCLGSVQHLKnrfgdgytivvriagSNPDLKpvqeFFGLA 2162
Cdd:PRK13644 175 VLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENVL---------------SDVSLQ----TLGLT 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 507682765 2163 FPGSV-LKE---KHRNMLQYQLPSSLSSLA----RIF 2191
Cdd:PRK13644 235 PPSLIeLAEnlkMHGVVIPWENTSSPSSFAeeicRLF 271
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1911-2135 |
5.50e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 69.98 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS------NIHEV 1984
Cdd:PRK09452 14 LVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaenrHVNTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPP 2064
Cdd:PRK09452 92 FQSYALFPH-------MTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2065 VVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL----KNRF 2135
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
898-1118 |
6.74e-12 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.67 E-value: 6.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLVKVYrDGMKVAVDgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 977
Cdd:PRK11000 3 SVTLRNVTKAY-GDVVISKD-INLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIWFYACLKGLSEKHVKVEMEQMA--LDVGlppSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVI 1055
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAevLQLA---HLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1056 LDEPTAGVDPYSR---RgIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFL 1118
Cdd:PRK11000 157 LDEPLSNLDAALRvqmR-IEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1909-2123 |
6.78e-12 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 70.48 E-value: 6.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDT-----TVTRGnaflnknsilsniHE 1983
Cdd:COG0488 313 KKVLELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELepdsgTVKLG-------------ET 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 VHqnMGYCPQ-FDAITELLTGREHVEffALLRGVPEKEVGKVgewairkLG-LLKYGE---KYAGNYSGGNKRKLSTAMA 2058
Cdd:COG0488 378 VK--IGYFDQhQEELDPDKTVLDELR--DGAPGGTEQEVRGY-------LGrFLFSGDdafKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRflwncAL--SIIK-EGrSVVLTSHSMEECEALCTRMAIMVNGKFR 2123
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLE-----ALeeALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
902-1108 |
7.56e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 70.34 E-value: 7.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYrDGMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP--PTSGTAYILGKDIR------SE---MST 970
Cdd:PRK13549 9 KNITKTF-GGVK-ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhgTYEGEIIFEGEELQasnirdTEragIAI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 IRQNLGVCPQhnvlfdmLTVEEHI-----WFYACLKGLSEKHVKVE--MEQMALDVglPPSklkSKTSQLSGGMQRKLSV 1043
Cdd:PRK13549 87 IHQELALVKE-------LSVLENIflgneITPGGIMDYDAMYLRAQklLAQLKLDI--NPA---TPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIrdLK-AHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1923-2102 |
9.70e-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: 66.87 E-value: 9.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1923 RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQfDAIteLL 2001
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQ-DTF--LF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2002 TG--REHVEFFALLrgVPEKEVGKVGEWA-----IRKL--GLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:cd03254 90 SGtiMENIRLGRPN--ATDEEVIEAAKEAgahdfIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEAT 167
|
170 180 190
....*....|....*....|....*....|
gi 507682765 2073 TGMDPKARRFLWNcALSIIKEGRSVVLTSH 2102
Cdd:cd03254 168 SNIDTETEKLIQE-ALEKLMKGRTSIIIAH 196
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
888-1118 |
1.10e-11 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 888 MEEEPTHLKLGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE 967
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVS--FRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 MS-TIRQNLGVCPQHNVLFDMLTVEEHI------WFYACLKGLSEKHVKVEmEQMALdVGLPPSKLKSKTSqLSGGMQRK 1040
Cdd:PRK10575 79 SSkAFARKVAYLPQQLPAAEGMTVRELVaigrypWHGALGRFGAADREKVE-EAISL-VGLKPLAHRLVDS-LSGGERQR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGSSLFL 1118
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
1922-2141 |
1.10e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 70.08 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1922 RRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-DTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAITEL 2000
Cdd:TIGR00955 34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2001 LTGREHVEFFALLR---GVPEKEVGKVGEWAIRKLGLLKYGEKYAG------NYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:TIGR00955 114 LTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGvpgrvkGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2072 TTGMDPkarrFLWNCALSIIKE----GRSVVLTSH--SMEECEaLCTRMAIMVNGKFRCLGSVQHLKNRFGD-GYTI 2141
Cdd:TIGR00955 194 TSGLDS----FMAYSVVQVLKGlaqkGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1912-2121 |
1.36e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 67.80 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRK---PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG------------------DTTVTRGNA 1970
Cdd:PRK13651 3 IKVKNIVKIFNKKLPtelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1971 FLNKNSI-------LSNIHEVHQNMGYCPQFdAITELL--TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL-LKYGEK 2040
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQF-AEYQLFeqTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2041 YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDG 241
|
.
gi 507682765 2121 K 2121
Cdd:PRK13651 242 K 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
916-1109 |
1.84e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.19 E-value: 1.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYILGK--DIRSEMSTIRQNLGVCP----QHNVLFDMl 988
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkRDGIVPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHIWFyACLKGLSE-KHVKVEMEQMALDVGLppSKLKSKTS-------QLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK13549 357 GVGKNITL-AALDRFTGgSRIDDAAELKTILESI--QRLKVKTAspelaiaRLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1061 AGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1109
Cdd:PRK13549 434 RGIDVGAKYEIYKLINQLvQQGVAIIVISSELPE--VLGlsDRVLVMHEGKL 483
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
640-841 |
2.48e-11 |
|
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: 67.80 E-value: 2.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 640 MPLFMTLAWIYSVAVIIKGIVYEKEARLKETMRIMGLDNGILWFSWFISSLIPLLVSASLLVVILkLGNLLPYSDPSVVF 719
Cdd:pfam12698 164 VGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLL-FGIGIPFGNLGLLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 720 VFLSVFAVVTILQCFLLSTLFSRANLAAACGGILYFILYLPYVLcVAWQDYVGFNLKVFASLLSPVAFGFGceyfalFEE 799
Cdd:pfam12698 243 LLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGG-LFPLEDPPSFLQWIFSIIPFFSPIDG------LLR 315
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507682765 800 QGIGVQWDNLFESLVegdgfnlttsvsMMLFDTFIYGVMTWY 841
Cdd:pfam12698 316 LIYGDSLWEIAPSLI------------ILLLFAVVLLLLALL 345
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1936-2123 |
2.83e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 2.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSiLSNIHEVH------QNMGYCPQFDAITELLTGREHVEF 2009
Cdd:PRK10584 33 VKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQP-LHQMDEEAraklraKHVGFVFQSFMLIPTLNALENVEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2010 FALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALS 2089
Cdd:PRK10584 112 PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFS 191
|
170 180 190
....*....|....*....|....*....|....*
gi 507682765 2090 IIKE-GRSVVLTSHSmEECEALCTRMAIMVNGKFR 2123
Cdd:PRK10584 192 LNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
899-1108 |
2.89e-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: 63.24 E-value: 2.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRsemstirqnlgvc 978
Cdd:cd03221 1 IELENLSKTYGG--KLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-VTWGSTVK------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 pqhnvlfdmltveehIWFYAclkglsekhvkvemeqmaldvglppsklksktsQLSGGMQRKLSVALAFVGGSKVVILDE 1058
Cdd:cd03221 65 ---------------IGYFE---------------------------------QLSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1059 PTAGVDPYSRRGIWELLLKYRqgRTIILSTHhmDEA--DILGDRIAIISHGK 1108
Cdd:cd03221 97 PTNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1912-2105 |
3.36e-11 |
|
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: 68.47 E-value: 3.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:TIGR02857 322 LEFSGVSVAYPGRR-PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQFDAITELlTGREHVEFFAllRGVPEKEVgkvgEWAIRKLGLL------------KYGEKYAGnYSGGNKRKLSTAMA 2058
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLAR--PDASDAEI----REALERAGLDefvaalpqgldtPIGEGGAG-LSGGQAQRLALARA 472
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLwNCALSIIKEGRSVVLTSHSME 2105
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEV-LEALRALAQGRTVLLVTHRLA 518
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
889-1109 |
3.38e-11 |
|
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: 68.62 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 889 EEEPTHL---KLGVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR 965
Cdd:COG4618 318 EPERMPLprpKGRLSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 966 S-EMSTIRQNLGVCPQHNVLFDMlTVEEHIwfyACLKGLSEKHVkVEMEQMA----LDVGLP---PSKLKSKTSQLSGG- 1036
Cdd:COG4618 398 QwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKV-VAAAKLAgvheMILRLPdgyDTRIGEGGARLSGGq 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1037 MQRklsVALA--FVGGSKVVILDEPTAGVDPYSRRGIWELL--LKyRQGRTIILSTHHMdeaDILG--DRIAIISHGKL 1109
Cdd:COG4618 473 RQR---IGLAraLYGDPRLVVLDEPNSNLDDEGEAALAAAIraLK-ARGATVVVITHRP---SLLAavDKLLVLRDGRV 544
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
900-1108 |
3.70e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 65.72 E-value: 3.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKD---------------- 963
Cdd:PRK11701 8 SVRGLTKLY--GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyalseaerrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 964 -IRSEMSTIRQN------LGVCPQHNVlfdmltVEEhiwfyacLKGLSEKHVKvEMEQMALD----VGLPPSKLKSKTSQ 1032
Cdd:PRK11701 86 lLRTEWGFVHQHprdglrMQVSAGGNI------GER-------LMAVGARHYG-DIRATAGDwlerVEIDAARIDDLPTT 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1033 LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK11701 152 FSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
897-1109 |
5.22e-11 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 65.03 E-value: 5.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-------RSEMS 969
Cdd:COG4161 1 MSIQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 970 TIRQNLGVCPQHNVLFDMLTVEEHIWFYAC-LKGLSEKHVKVEMEQMALDVGLPPsKLKSKTSQLSGGMQRKLSVALAFV 1048
Cdd:COG4161 79 LLRQKVGMVFQQYNLWPHLTVMENLIEAPCkVLGLSKEQAREKAMKLLARLRLTD-KADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1049 GGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1927-2106 |
5.90e-11 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 63.79 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGNaflnknsilsnihevHQNMGYCPQFDAITELL 2001
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGvlrptSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2002 --TGREHVE--FFA---LLRGvPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2074
Cdd:NF040873 71 plTVRDLVAmgRWArrgLWRR-LTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
|
170 180 190
....*....|....*....|....*....|....*.
gi 507682765 2075 MDPKARRFLwncaLSIIKE----GRSVVLTSHSMEE 2106
Cdd:NF040873 150 LDAESRERI----IALLAEeharGATVVVVTHDLEL 181
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1936-2121 |
5.98e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 65.25 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GNAFLNKNSILS---NIHEVHQNMGYCPQFDAITELLTGREHV 2007
Cdd:PRK14267 27 IPQNGVFALMGPSGCGKSTllrTFNRLLELNEEARveGEVRLFGRNIYSpdvDPIEVRREVGMVFQYPNPFPHLTIYDNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2008 EFFALLRGV--PEKEVGKVGEWAIRKLGLLKYGEK----YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK14267 107 AIGVKLNGLvkSKKELDERVEWALKKAALWDEVKDrlndYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTA 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507682765 2082 FLWNCALSiIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK14267 187 KIEELLFE-LKKEYTIVLVTHSPAQAARVSDYVAFLYLGK 225
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
908-1107 |
7.01e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 64.21 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG--LFPPTSGTAYILGKDIRSEMSTIrqnlgvcpqhnvlf 985
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalKGTPVAGCVDVPDNQFGREASLI-------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 986 dmltveEHIWfyaclkglSEKHVKVEMEQMAlDVGL--PPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:COG2401 104 ------DAIG--------RKGDFKDAVELLN-AVGLsdAVL-WLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 507682765 1064 DP-YSRRG--IWELLLKyRQGRTIILSTHHMD-EADILGDRIAIISHG 1107
Cdd:COG2401 168 DRqTAKRVarNLQKLAR-RAGITLVVATHHYDvIDDLQPDLLIFVGYG 214
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
915-1064 |
8.83e-11 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 65.88 E-value: 8.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNLGVCPQHNV--LFDML 988
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWRAVRSDIQMIFQDPLasLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 989 TVEEHI-----WFYAclkGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PRK15079 116 TIGEIIaeplrTYHP---KLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
.
gi 507682765 1064 D 1064
Cdd:PRK15079 193 D 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1908-2081 |
9.21e-11 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 65.90 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTKiyRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN-----KNSIlsnih 1982
Cdd:PRK11432 3 QKNFVVLKNITK--RFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDgedvtHRSI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1983 evhQNMGYCPQFD--AITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALI 2060
Cdd:PRK11432 76 ---QQRDICMVFQsyALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180
....*....|....*....|.
gi 507682765 2061 GGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRR 173
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1911-2121 |
1.05e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 64.72 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKR---KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL--------S 1979
Cdd:COG1101 1 MLELKNLSKTFNPGTvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTklpeykraK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHEVHQN--MGYCPQfdaitelLTGREHV-------EFFALLRGVPEKEVGKVGEW-AIRKLGLlkygEKY----AGNY 2045
Cdd:COG1101 81 YIGRVFQDpmMGTAPS-------MTIEENLalayrrgKRRGLRRGLTKKRRELFRELlATLGLGL----ENRldtkVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2046 SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRsvvLTS----HSMEECEALCTRMAIMVNGK 2121
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1926-2121 |
1.10e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 64.85 E-value: 1.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFK-----MLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAiTEL 2000
Cdd:PRK13641 20 KKGLDNISFELEEGSFVALVGHTGSGKSTLMQhfnalLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQFPE-AQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2001 L--TGREHVEFFALLRGVPEKEV-GKVGEWaIRKLGLLK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK13641 99 FenTVLKDVEFGPKNFGFSEDEAkEKALKW-LKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507682765 2077 PKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGK 222
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
1912-2121 |
1.13e-10 |
|
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: 62.62 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNkNSILSNIHEVH--QNMG 1989
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLD-GADISQWDPNElgDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQFDaitELLTGrehveffallrgvpekevgkvgewAIrklgllkygekyAGN-YSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:cd03246 80 YLPQDD---ELFSG------------------------SI------------AENiLSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2069 DEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGK 2121
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGR 172
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1912-2129 |
1.57e-10 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 63.98 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-------LSNIHEV 1984
Cdd:COG4559 2 LEAENLS--VRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLaawspweLARRRAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HqnmgycPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKyagNY---SGGNKRKLSTAMALI- 2060
Cdd:COG4559 80 L------PQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGR---SYqtlSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2061 ------GGPPVVFLDEPTTGMDPK--------ARRFLwncalsiiKEGRSVV-------LTSHsmeeceaLCTRMAIMVN 2119
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAhqhavlrlARQLA--------RRGGGVVavlhdlnLAAQ-------YADRILLLHQ 215
|
250
....*....|
gi 507682765 2120 GKFRCLGSVQ 2129
Cdd:COG4559 216 GRLVAQGTPE 225
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1938-2130 |
1.83e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.70 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1938 RGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN--KNSILSNIHEVHQNMGYCPQ---FDAITELLTGRE------- 2005
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDgkPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADninisar 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2006 --HVEFFALLRGVPEKEVgkvgewAIRKLGLLKY----GEKYAGNYSGGNKRK------LSTAMAliggppVVFLDEPTT 2073
Cdd:PRK11288 358 rhHLRAGCLINNRWEAEN------ADRFIRSLNIktpsREQLIMNLSGGNQQKailgrwLSEDMK------VILLDEPTR 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2074 GMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGkfRCLGSVQH 2130
Cdd:PRK11288 426 GIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREG--RIAGELAR 480
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1926-2141 |
1.87e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 63.91 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLT-------GDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrlieiydSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1999 ELLTGREHVEFFALLRGVPEK-EVGKVGEWAIRKLGLLKygEKY------AGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLWK--EVYdrlnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2072 TTGMDPKARRFLWNCALSIIKEgRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL----KNRFGDGYTI 2141
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1912-2121 |
1.89e-10 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 63.24 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKpavdRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHE------- 1983
Cdd:COG3840 2 LRLDDLTYRYGDFPL----RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAlPPAErpvsmlf 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 ----------VHQNMGycpqfdaitelltgrehvefFAL---LR-GVPEKEvgKVgEWAIRKLGLLKYGEKYAGNYSGGN 2049
Cdd:COG3840 78 qennlfphltVAQNIG--------------------LGLrpgLKlTAEQRA--QV-EQALERVGLAGLLDRLPGQLSGGQ 134
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2050 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG3840 135 RQRVALARCLVRKRPILLLDEPFSALDPALRQEM----LDLVDElcrerGLTVLMVTHDPEDAARIADRVLLVADGR 207
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
1916-2121 |
2.34e-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: 62.51 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1916 ELTKIYRRKRKPAVDRICVgIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN-------------------KNS 1976
Cdd:cd03298 2 RLDKIRFSYGEQPMHFDLT-FAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINgvdvtaappadrpvsmlfqENN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1977 ILSNIhEVHQNMGYCpqfdaitelLTGREHveffalLRGVPEKEVGKvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:cd03298 81 LFAHL-TVEQNVGLG---------LSPGLK------LTAEDRQAIEV----ALARVGLAGLEKRLPGELSGGERQRVALA 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGR 206
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1939-2103 |
2.35e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 62.58 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN-KNSILSNIHEV-----HQNmgycpqfdAITELLTGREHVEFFAL 2012
Cdd:PRK13539 28 GEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDgGDIDDPDVAEAchylgHRN--------AMKPALTVAENLEFWAA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2013 LRGVPEKEVgkvgEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIK 2092
Cdd:PRK13539 100 FLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAHLA 175
|
170
....*....|.
gi 507682765 2093 EGRSVVLTSHS 2103
Cdd:PRK13539 176 QGGIVIAATHI 186
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1925-2121 |
2.43e-10 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 62.10 E-value: 2.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1925 RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsilsnihevhqnMGYCPQFDAItelLTG- 2003
Cdd:cd03250 17 TSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQEPWI---QNGt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2004 -REHVEFfallrGVPEKEvgkvgEW---AIRKLGLLK------------YGEKyaG-NYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03250 82 iRENILF-----GKPFDE-----ERyekVIKACALEPdleilpdgdlteIGEK--GiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2067 FLDEPTTGMDPKARRFLW-NCALSIIKEGRSVVLTSHSMEECEAlCTRMAIMVNGK 2121
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
916-1107 |
2.70e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 66.29 E-value: 2.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLalnFYEGQITSFLGHNGAGKTTTMSILTGlfppTSGTAYILGKDI----RSEMSTIRQNLGVCPQHNVLFDMLTVE 991
Cdd:TIGR00956 782 VDGW---VKPGTLTALMGASGAGKTTLLNVLAE----RVTTGVITGGDRlvngRPLDSSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 992 EHIWFYACLK-----GLSEKHVKV-------EMEQMAlD--VGLPPSKLKSKtsqlsggmQRK-LSVALAFVGGSKVVI- 1055
Cdd:TIGR00956 855 ESLRFSAYLRqpksvSKSEKMEYVeevikllEMESYA-DavVGVPGEGLNVE--------QRKrLTIGVELVAKPKLLLf 925
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKY-RQGRTiILSTHHMDEADILG--DRIAIISHG 1107
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQA-ILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1911-2121 |
2.89e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 65.43 E-value: 2.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrkrkPAV---DRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN---------KNSIL 1978
Cdd:COG3845 5 ALELRGITKRF-----GGVvanDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgkpvrirspRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1979 SNIHEVHQN-MgycpQFDAIT--E-LLTGREHVEFFALLRGVPEKEVGKVGEwairklgllKYG-----EKYAGNYSGGN 2049
Cdd:COG3845 80 LGIGMVHQHfM----LVPNLTvaEnIVLGLEPTKGGRLDRKAARARIRELSE---------RYGldvdpDAKVEDLSVGE 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2050 KRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIK----EGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG3845 147 QQRVEILKALYRGARILILDEPTAVLTPQEADEL----FEILRrlaaEGKSIIFITHKLREVMAIADRVTVLRRGK 218
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
899-1065 |
4.13e-10 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 62.34 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG-----------KDIRSe 967
Cdd:PRK11124 3 IQLNGINCFY--GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIRE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 mstIRQNLGVCPQHNVLFDMLTVEEHIWFYAC-LKGLSEKHVKVEMEQMaldvgLPPSKLKSKTS----QLSGGMQRKLS 1042
Cdd:PRK11124 80 ---LRRNVGMVFQQYNLWPHLTVQQNLIEAPCrVLGLSKDQALARAEKL-----LERLRLKPYADrfplHLSGGQQQRVA 151
|
170 180
....*....|....*....|...
gi 507682765 1043 VALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK11124 152 IARALMMEPQVLLFDEPTAALDP 174
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1927-2121 |
4.15e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 63.22 E-value: 4.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-----NIHEVHQNMGYCPQFdAITELL 2001
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQF-PESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2002 --TGREHVEFFALLRGVPEKEVGKVgewAIRKLGLLKYGE----KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2075
Cdd:PRK13649 100 eeTVLKDVAFGPQNFGVSQEEAEAL---AREKLALVGISEslfeKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507682765 2076 DPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGK 222
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1927-2150 |
4.47e-10 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 64.09 E-value: 4.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:PRK09536 17 TVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVASVPQDTSLSFEFDVRQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2006 HVEFFA---LLRGVPEKEVGK-VGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD-PKAR 2080
Cdd:PRK09536 97 VVEMGRtphRSRFDTWTETDRaAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQV 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2081 RFLwNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG------SVQHLKNRFgDGYTIVvriaGSNP 2150
Cdd:PRK09536 177 RTL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGppadvlTADTLRAAF-DARTAV----GTDP 246
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1911-2121 |
4.81e-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: 62.52 E-value: 4.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYR-------RKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAF--------LNKN 1975
Cdd:TIGR02769 2 LLEVRDVTHTYRtgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1976 SILSNIHEVHQNMGYCPqfDAITELLTGREHV-EFFALLRGVPEKEVGKVGEWAIRKLGL-LKYGEKYAGNYSGGNKRKL 2053
Cdd:TIGR02769 82 QRRAFRRDVQLVFQDSP--SAVNPRMTVRQIIgEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2054 STAMALIGGPPVVFLDEPTTGMDpkarRFLWNCALSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:TIGR02769 160 NIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
1909-2121 |
5.08e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 62.80 E-value: 5.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELtkIYRRKRKPAVDR---ICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEV 1984
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAeNVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 HQNMGYCPQF-DAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2064 PVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLT-SHSMEECeALCTRMAIMVNGK 2121
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGE 217
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1932-2131 |
5.95e-10 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 62.73 E-value: 5.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1932 ICVGIPRGECFGLLGVNGAGKSSTFKMLTG-----DTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFdaiTELLTGREH 2006
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGllqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQF---PEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2007 VE----FFALLRGVPEKEVGKVGEWAIRKLGL-LKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR 2081
Cdd:PRK13634 103 VEkdicFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2082 FLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:PRK13634 183 EMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
926-1109 |
6.30e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK--DIRSEMSTIRQNLGVCPQ---HNVLFDMLTVEE-------- 992
Cdd:PRK11288 279 GEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADninisarr 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 993 -HIWFYACLKG-----LSEKHVKvemeqmaldvglppsKLKSKTS-------QLSGGMQRK--LSVALAfvGGSKVVILD 1057
Cdd:PRK11288 359 hHLRAGCLINNrweaeNADRFIR---------------SLNIKTPsreqlimNLSGGNQQKaiLGRWLS--EDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHhmDEADILG--DRIAIISHGKL 1109
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELaAQGVAVLFVSS--DLPEVLGvaDRIVVMREGRI 474
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
892-1109 |
7.09e-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: 60.89 E-value: 7.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 892 PTHLKlgVSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMST 970
Cdd:cd03369 2 PEHGE--IEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 IRQNLGVCPQHNVLFdMLTVEEHIWFYaclkglsEKHVKVEMEQmALDVglppsklKSKTSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03369 80 LRSSLTIIPQDPTLF-SGTIRSNLDPF-------DEYSDEEIYG-ALRV-------SEGGLNLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDE-ADIlgDRIAIISHGKL 1109
Cdd:cd03369 144 PRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEV 201
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
1909-2126 |
9.49e-10 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 61.76 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYR--RKRKP----------------AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNa 1970
Cdd:PRK13546 2 NVSVNIKNVTKEYRiyRTNKErmkdalipkhknktffALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1971 fLNKNSILSNIhevHQNMGYCPQfdaitelLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNK 2050
Cdd:PRK13546 81 -VDRNGEVSVI---AISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2051 RKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNCALSI--IKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLG 2126
Cdd:PRK13546 150 AKLGFSINITVNPDILVIDEALSVGD---QTFAQKCLDKIyeFKEqNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
900-1109 |
1.01e-09 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 63.55 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYR--DGMKVAVDGLALNFYEGQITSFLGHNGAGKT-TTMSILtGLFPP----TSGTAYILGKDI----RSEM 968
Cdd:COG4172 8 SVEDLSVAFGqgGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSIL-RLLPDpaahPSGSILFDGQDLlglsEREL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 STIRQN------------LgvcpqhNVLFdmlTVEEHIwfYACL---KGLSEKHVKVEMEQMALDVGLPP--SKLKSKTS 1031
Cdd:COG4172 87 RRIRGNriamifqepmtsL------NPLH---TIGKQI--AEVLrlhRGLSGAAARARALELLERVGIPDpeRRLDAYPH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1032 QLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHhmDeadiLG------DRIAI 1103
Cdd:COG4172 156 QLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLkdLQRELGMALLLITH--D----LGvvrrfaDRVAV 229
|
....*.
gi 507682765 1104 ISHGKL 1109
Cdd:COG4172 230 MRQGEI 235
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
928-1194 |
1.06e-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: 62.82 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 928 ITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-----EMSTIRQNLGVCPQHNVLFDMLTVEEHIWFyaclkG 1002
Cdd:TIGR02142 25 VTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgiFLPPEKRRIGYVFQEARLFPHLSVRGNLRY-----G 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1003 LseKHVKVEMEQMALD-----VGLPPSkLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK 1077
Cdd:TIGR02142 100 M--KRARPSERRISFErvielLGIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLER 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1078 YRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVGS----------SLFLKNQLGTGYYLTLVKKDVESSLGSCR-N 1144
Cdd:TIGR02142 177 LHAefGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPiaevwaspdlPWLAREDQGSLIEGVVAEHDQHYGLTALRlG 256
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1145 SSSTVSNLKKEDSVSQ-----SSSDAGLGSDHESDTltidvsAISNLIRKHVAEA 1194
Cdd:TIGR02142 257 GGHLWVPENLGPTGARlrlrvPARDVSLALQKPEAT------SIRNILPARVVEI 305
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
898-1091 |
1.17e-09 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 61.44 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSemsTIRQNL-G 976
Cdd:PRK15056 6 GIVVNDVTVTWRNG-HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVL---FDMLtVEEHIWF--YACLKGL--SEKHVKVEMEQMALDVGLPPSKLKsKTSQLSGGMQRKLSVALAFVG 1049
Cdd:PRK15056 82 YVPQSEEVdwsFPVL-VEDVVMMgrYGHMGWLrrAKKRDRQIVTAALARVDMVEFRHR-QIGELSGGQKKRVFLARAIAQ 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507682765 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHM 1091
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
899-1204 |
1.32e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 63.81 E-value: 1.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVc 978
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL- 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 pQHNVLFDmltveehiwfyaclKGLSEKHVKVEMEQMAL--DVGLPPS----KLKSKTSQLSGGMQRKLSVALAFVGGSK 1052
Cdd:TIGR00957 716 -RENILFG--------------KALNEKYYQQVLEACALlpDLEILPSgdrtEIGEKGVNLSGGQKQRVSLARAVYSNAD 780
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1053 VVILDEPTAGVDPYSRRGIWELLLKYR---QGRTIILSTHHMDEADILgDRIAIISHGKLCCVGSslflknqlgtgyYLT 1129
Cdd:TIGR00957 781 IYLFDDPLSAVDAHVGKHIFEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS------------YQE 847
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1130 LVKKDvESSLGSCRNSSSTVSNLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVAEARLVEDIGHEL 1204
Cdd:TIGR00957 848 LLQRD-GAFAEFLRTYAPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHH 921
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1944-2102 |
1.40e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.71 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1944 LLGVNGAGKSSTFKMLTGDTT------VTRGNAFLNKNSILSNIHevhqnmGYCPQFDAITELLTGREHVEFFALLRgVP 2017
Cdd:PLN03140 911 LMGVSGAGKTTLMDVLAGRKTggyiegDIRISGFPKKQETFARIS------GYCEQNDIHSPQVTVRESLIYSAFLR-LP 983
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2018 eKEVGK------VGEWA-IRKLGLLK---YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCA 2087
Cdd:PLN03140 984 -KEVSKeekmmfVDEVMeLVELDNLKdaiVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV 1062
|
170
....*....|....*
gi 507682765 2088 LSIIKEGRSVVLTSH 2102
Cdd:PLN03140 1063 RNTVDTGRTVVCTIH 1077
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
883-1109 |
1.51e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 63.33 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 883 VSEIRMEEEPTHLKLGVSI--QNLVKVYRDGmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGlFPPTSGTAYIL 960
Cdd:PRK11174 332 LAHPQQGEKELASNDPVTIeaEDLEILSPDG-KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGSLKIN 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 961 GKDIRS-EMSTIRQNL---GVCPQ--HNVLFDMLTV------EEHIWFYACLKGLSEKhvkVEMEQMALDvglppSKLKS 1028
Cdd:PRK11174 410 GIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLgnpdasDEQLQQALENAWVSEF---LPLLPQGLD-----TPIGD 481
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1029 KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILgDRIAIISHGK 1108
Cdd:PRK11174 482 QAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
|
.
gi 507682765 1109 L 1109
Cdd:PRK11174 561 I 561
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
926-1090 |
1.57e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.96 E-value: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVCPQHNVLFDMLTVEEHiwfyaCLKGLSE 1005
Cdd:PRK13540 27 GGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLREN-----CLYDIHF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1006 KHVKVEMEQMALDVGLpPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTI 1084
Cdd:PRK13540 102 SPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRaKGGAV 180
|
....*.
gi 507682765 1085 ILSTHH 1090
Cdd:PRK13540 181 LLTSHQ 186
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
919-1109 |
1.77e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTIRQNLGVC------PQHNVLFDM----- 987
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 988 ---LTVEEHIWFyacLKGLSEKHVkveMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PRK15439 362 vcaLTHNRRGFW---IKPARENAV---LERYRRALNIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 507682765 1065 PYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1912-2121 |
1.91e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.71 E-value: 1.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKiyrrkrkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSN----------- 1980
Cdd:PRK10762 258 LKVDNLSG-------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangiv 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1981 -IHE------------VHQNMGYCpqfdAITEL--LTGRehveffalLRGVPEKEVgkVGEWaIRKLGLLKYG-EKYAGN 2044
Cdd:PRK10762 331 yISEdrkrdglvlgmsVKENMSLT----ALRYFsrAGGS--------LKHADEQQA--VSDF-IRLFNIKTPSmEQAIGL 395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2045 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
911-1114 |
2.10e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 60.77 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST-IRQNLGVCPQHNVLFDMLT 989
Cdd:PRK10253 18 GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKeVARRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 990 VEE--------HIWFYACLKGLSEKHVKVEMEQMALdvglppSKLKSKT-SQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK10253 98 VQElvargrypHQPLFTRWRKEDEEAVTKAMQATGI------THLADQSvDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1061 AGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK10253 172 TWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
900-1112 |
2.20e-09 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 62.42 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 900 SIQNLVKVYRDGMKV--AVDGLALNFYEGQITSFLGHNGAGKT-TTMSILTGLfpPTSGTAYILGkDIR----------- 965
Cdd:PRK15134 7 AIENLSVAFRQQQTVrtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLL--PSPPVVYPSG-DIRfhgesllhase 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 966 --------SEMSTIRQNLGVC--PQHNV---LFDMLTVEehiwfyaclKGLSEKHVKVEMEQMALDVGL--PPSKLKSKT 1030
Cdd:PRK15134 84 qtlrgvrgNKIAMIFQEPMVSlnPLHTLekqLYEVLSLH---------RGMRREAARGEILNCLDRVGIrqAAKRLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1031 SQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:PRK15134 155 HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234
|
....
gi 507682765 1109 lcCV 1112
Cdd:PRK15134 235 --CV 236
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1909-2123 |
2.87e-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: 62.15 E-value: 2.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIY----RRKRkpaVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGD-TTVTRGNAFLNKNSI------ 1977
Cdd:TIGR02633 255 DVILEARNLTCWDvinpHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdirnpa 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1978 ------LSNIHEVHQNMGYCPQFdAITELLTGREHVEFFALLRGVPEKEVGKVGEwAIRKLGLLKYGEKYA-GNYSGGNK 2050
Cdd:TIGR02633 332 qairagIAMVPEDRKRHGIVPIL-GVGKNITLSVLKSFCFKMRIDAAAELQIIGS-AIQRLKVKTASPFLPiGRLSGGNQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2051 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFR 2123
Cdd:TIGR02633 410 QKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1939-2122 |
3.08e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 3.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI--LSNIHEVHQNMGYCPQ--------FDA-----ITELLTG 2003
Cdd:PRK15439 289 GEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPEdrqssglyLDAplawnVCALTHN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2004 RehVEFFalLRgvPEKEvGKVGEWAIRKLGL-LKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRF 2082
Cdd:PRK15439 369 R--RGFW--IK--PARE-NAVLERYRRALNIkFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARND 441
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507682765 2083 LWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:PRK15439 442 IYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1932-2133 |
3.60e-09 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 59.64 E-value: 3.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1932 ICVGIPRGECFGLLGVNGAGKSSTFKML-------TGDTTVTrGNAF-LNKNSILSNIHEVHQNMGYCPQFDAITELLTG 2003
Cdd:PRK11124 21 ITLDCPQGETLVLLGPSGAGKSSLLRVLnllemprSGTLNIA-GNHFdFSKTPSDKAIRELRRNVGMVFQQYNLWPHLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2004 REH-VEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrf 2082
Cdd:PRK11124 100 QQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE---- 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2083 LWNCALSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKN 2133
Cdd:PRK11124 176 ITAQIVSIIRElaetGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1915-2120 |
3.87e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 60.18 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1915 KELTKIYRRK---RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSN-----IHEVHQ 1986
Cdd:PRK13646 6 DNVSYTYQKGtpyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKtkdkyIRPVRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQF--DAITELLTGREhVEFFALLRGVPEKEVGkvgEWAIRKLGLLKYG----EKYAGNYSGGNKRKLSTAMALI 2060
Cdd:PRK13646 86 RIGMVFQFpeSQLFEDTVERE-IIFGPKNFKMNLDEVK---NYAHRLLMDLGFSrdvmSQSPFQMSGGQMRKIAIVSILA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2061 GGPPVVFLDEPTTGMDPKARRFLWNCALSI-IKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK13646 162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEG 222
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
899-1109 |
4.21e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 59.83 E-value: 4.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYR------DGMK------------VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyil 960
Cdd:PRK13546 5 VNIKNVTKEYRiyrtnkERMKdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 961 gkDIRSEMSTIRQNLGVCPQhnvlfdmLTVEEHIWFYACLKGLSEKHVKVEMEQMaldvgLPPSKLKSKTSQ----LSGG 1036
Cdd:PRK13546 82 --DRNGEVSVIAISAGLSGQ-------LTGIENIEFKMLCMGFKRKEIKAMTPKI-----IEFSELGEFIYQpvkkYSSG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1037 MQRKLSVALAFVGGSKVVILDEP-TAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK13546 148 MRAKLGFSINITVNPDILVIDEAlSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
1912-2102 |
4.93e-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: 4.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsilsnihevhQNMGYC 1991
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST----------VKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFdaitelltgrehveffallrgvpekevgkvgewairklgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:cd03221 69 EQL---------------------------------------------------SGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190
....*....|....*....|....*....|.
gi 507682765 2072 TTGMDPKARRFLWNcalSIIKEGRSVVLTSH 2102
Cdd:cd03221 98 TNHLDLESIEALEE---ALKEYPGTVILVSH 125
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
915-1123 |
5.67e-09 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 61.19 E-value: 5.67e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLFDMlTVEEH 993
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVSQNVHLFND-TIANN 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 994 IwFYAClkglSEKHVKVEMEQMA-----------LDVGLPPSKLKSKTSqLSGGMQRKLSVALAFVGGSKVVILDEPTAG 1062
Cdd:PRK11176 437 I-AYAR----TEQYSREQIEEAArmayamdfinkMDNGLDTVIGENGVL-LSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1063 VDPYSRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSLFLKNQLG 1123
Cdd:PRK11176 511 LDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHAELLAQNG 570
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
923-1064 |
6.07e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 61.79 E-value: 6.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 923 FYEGQITSFLGHNGAGKTTTMSILTGlfPPTSGtaYILGkDIRSEMSTIRQNL-----GVCPQHNVLFDMLTVEEHIWFY 997
Cdd:PLN03140 903 FRPGVLTALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRISGFPKKQETfarisGYCEQNDIHSPQVTVRESLIYS 977
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 998 ACLK-----GLSEKHVKVE--MEQMALD------VGLPpsklksKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PLN03140 978 AFLRlpkevSKEEKMMFVDevMELVELDnlkdaiVGLP------GVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
890-1109 |
7.98e-09 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 58.92 E-value: 7.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 890 EEPTHLKLG--VSIQNLVKVYrdGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGtAYILGkdiRSE 967
Cdd:PRK11247 2 MNTARLNQGtpLLLNAVSKRY--GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---TAP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 968 MSTIRQNLGVCPQHNVLFDMLTVEEHIwfyaclkGLSEK-HVKVEMEQmALD-VGLPpSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:PRK11247 76 LAEAREDTRLMFQDARLLPWKKVIDNV-------GLGLKgQWRDAALQ-ALAaVGLA-DRANEWPAALSGGQKQRVALAR 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1046 AFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1909-2121 |
8.57e-09 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 59.48 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1909 NDILEIKELTKIYRRKRK---PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNA----FLNKNSILSNI 1981
Cdd:PRK13631 19 DIILRVKNLYCVFDEKQEnelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1982 HEVHQNMGYCPQFDAITELL--------------TGREHVEFFALLRGVPEKEVGKVGEWAIRKLGL-LKYGEKYAGNYS 2046
Cdd:PRK13631 99 LITNPYSKKIKNFKELRRRVsmvfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2047 GGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
921-1181 |
8.62e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.15 E-value: 8.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYACL 1000
Cdd:PLN03232 638 LEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRENILFGSDF 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1001 KglSEKHVK-VEMEQMALDVGLPP----SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL 1075
Cdd:PLN03232 706 E--SERYWRaIDVTALQHDLDLLPgrdlTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDSC 783
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1076 LKYR-QGRTIILSTHHMDEADILgDRIAIISHGKLCCVGSSLFL-KNQlgtgyylTLVKKDVESSlgscrnssstvsnLK 1153
Cdd:PLN03232 784 MKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELsKSG-------SLFKKLMENA-------------GK 842
|
250 260
....*....|....*....|....*...
gi 507682765 1154 KEDSVSQSSSDAGLgsDHESDTLTIDVS 1181
Cdd:PLN03232 843 MDATQEVNTNDENI--LKLGPTVTIDVS 868
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
921-1089 |
9.72e-09 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.58 E-value: 9.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 921 LNFYEGQITsFL-GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--------RSEMSTIRQNlgvcpQHnvLFDMLtve 991
Cdd:COG4615 353 LTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtadnreayRQLFSAVFSD-----FH--LFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 992 ehiwfYACLKGLSEKHVKVEMEQMALDvglppSKLKSK-----TSQLSGGmQRK-LSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:COG4615 422 -----LGLDGEADPARARELLERLELD-----HKVSVEdgrfsTTDLSQG-QRKrLALLVALLEDRPILVFDEWAADQDP 490
|
170 180
....*....|....*....|....*....
gi 507682765 1066 YSRRgiW---ELL--LKyRQGRTIILSTH 1089
Cdd:COG4615 491 EFRR--VfytELLpeLK-ARGKTVIAISH 516
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1936-2134 |
9.91e-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: 59.74 E-value: 9.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN--------KNSILSnIHE-----VHQNMGYCPQFDAITELLT 2002
Cdd:TIGR02142 20 LPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNgrtlfdsrKGIFLP-PEKrrigyVFQEARLFPHLSVRGNLRY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2003 GREHVEffALLRGVPEKEVgkvgewaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR- 2081
Cdd:TIGR02142 99 GMKRAR--PSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYe 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2082 ---FLWNCALSIikeGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNR 2134
Cdd:TIGR02142 170 ilpYLERLHAEF---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1926-2134 |
1.12e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 58.17 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSST----FKMLTGDTTVTRGNAFLNKNSILSN------IHEVHQNmgycPQfD 1995
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCalrgrkIATIMQN----PR-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1996 AITELLTGREHVEFFALLRGVPEKEVGKVGewAIRKLGL---LKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK10418 91 AFNPLHTMHTHARETCLALGKPADDATLTA--ALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2073 TGMDPKAR-RFLwNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNR 2134
Cdd:PRK10418 169 TDLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1936-2076 |
1.38e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.90 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAF-----LNKNSILSNIHEVHQNMGYCPQFDAITELLTGREHVEFF 2010
Cdd:PRK11629 32 IGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIfngqpMSKLSSAAKAELRNQKLGFIYQFHHLLPDFTALENVAMP 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2011 ALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK11629 112 LLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
899-1110 |
1.53e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--------RSEMST 970
Cdd:PRK10522 323 LELRNVTFAYQD-NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaeqpedyRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 971 IRQNLgvcpqHnvLFDMLTVEE---------HIWfyacLKGLSEKHvKVEMEQMALdvglppsklksKTSQLSGGMQRKL 1041
Cdd:PRK10522 402 VFTDF-----H--LFDQLLGPEgkpanpalvEKW----LERLKMAH-KLELEDGRI-----------SNLKLSKGQKKRL 458
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 1042 SVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHmDEADILGDRIAIISHGKLC 1110
Cdd:PRK10522 459 ALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQemGKTIFAISHD-DHYFIHADRLLEMRNGQLS 528
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1911-2121 |
1.61e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKiyrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL-SNIHEVHQNmg 1989
Cdd:PRK10982 250 ILEVRNLTS----LRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnHNANEAINH-- 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 ycpQFDAITEL-----LTGREHVEFFALLRGVpEKEVGKVG-----------EWAIRKLGLLKYGEKYA-GNYSGGNKRK 2052
Cdd:PRK10982 324 ---GFALVTEErrstgIYAYLDIGFNSLISNI-RNYKNKVGlldnsrmksdtQWVIDSMRVKTPGHRTQiGSLSGGNQQK 399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2053 LSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGL 468
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
1928-2137 |
1.68e-08 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.52 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEvhqnmgycpqfdAITELLTGREHV 2007
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS------------GLNGQLTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2008 EFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDpkaRRFLWNC- 2086
Cdd:PRK13545 107 ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKKCl 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2087 -ALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRFGD 2137
Cdd:PRK13545 184 dKMNEFKEqGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDE 236
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
1883-2076 |
1.68e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 59.56 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1883 TKFLPLNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKML 1959
Cdd:TIGR03719 291 ARYEELLSQEFQKRNETAEIYIPPGPrlgDKVIEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMI 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1960 TGDTTVTRGnaflnknSIlsNIHE-VHqnMGYCPQFdaiTELLTGREHVeFFALLRGVPEKEVGKVgEWAIRK-LGLLKY 2037
Cdd:TIGR03719 369 TGQEQPDSG-------TI--EIGEtVK--LAYVDQS---RDALDPNKTV-WEEISGGLDIIKLGKR-EIPSRAyVGRFNF 432
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507682765 2038 G----EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:TIGR03719 433 KgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1924-2127 |
1.81e-08 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 58.10 E-value: 1.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1924 KRKP----AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQ------NMGYC-- 1991
Cdd:PRK13645 18 KKTPfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEvkrlrkEIGLVfq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 -PQFDAITEllTGREHVEFFALLRGVPEKEV-GKVGEWairkLGLLKYGEKYAG----NYSGGNKRKLSTAMALIGGPPV 2065
Cdd:PRK13645 98 fPEYQLFQE--TIEKDIAFGPVNLGENKQEAyKKVPEL----LKLVQLPEDYVKrspfELSGGQKRRVALAGIIAMDGNT 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGS 2127
Cdd:PRK13645 172 LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1912-2131 |
2.04e-08 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 59.45 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIHE--VHQNMG 1989
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQfdaitelltgREHVeFFALLR-----GVPEKEVGKVGEwAIRKLGLLKYGEKYAG----------NYSGGNKRKLS 2054
Cdd:PRK11160 418 VVSQ----------RVHL-FSATLRdnlllAAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLG 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2055 TAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE---GRSVVLTSH---SMEECEALCtrmaIMVNGKFRCLGSV 2128
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQI----LELLAEhaqNKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTH 557
|
...
gi 507682765 2129 QHL 2131
Cdd:PRK11160 558 QEL 560
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1921-2105 |
2.21e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 57.71 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1921 YRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAF-------LNKNSILSniheVHQNMGYCPQ 1993
Cdd:PRK13638 9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLwqgkpldYSKRGLLA----LRQQVATVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1994 FDAITELLTGREHVEFFALLR-GVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK13638 85 DPEQQIFYTDIDSDIAFSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190
....*....|....*....|....*....|...
gi 507682765 2073 TGMDPKARRFLWNCALSIIKEGRSVVLTSHSME 2105
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDID 197
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
911-1108 |
2.44e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKvAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIL--G-----KDIR-SE---MSTIRQNLGVCP 979
Cdd:NF040905 13 GVK-ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSYEGEILfdGevcrfKDIRdSEalgIVIIHQELALIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 980 QhnvlfdmLTVEEHIWfyaclkgLSEKHVK----------VEMEQMALDVGL--PPSklkSKTSQLSGGMQRKLSVALAF 1047
Cdd:NF040905 92 Y-------LSIAENIF-------LGNERAKrgvidwnetnRRARELLAKVGLdeSPD---TLVTDIGVGKQQLVEIAKAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMDEADILGDRIAIISHGK 1108
Cdd:NF040905 155 SKDVKLLILDEPTAALNEEDSAALLDLLLELKaQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
901-1107 |
2.49e-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: 56.67 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKVY----RDGMK-VAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILgkdIRSEMSTIrqNL 975
Cdd:COG4778 7 VENLSKTFtlhlQGGKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS--IL---VRHDGGWV--DL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQHnvlfDMLTVEEHIWFY-----------ACL---------KGLSEKHVKVEMEQM--ALDV-----GLPPSklks 1028
Cdd:COG4778 80 AQASPR----EILALRRRTIGYvsqflrviprvSALdvvaeplleRGVDREEARARARELlaRLNLperlwDLPPA---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1029 kTsqLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEADILGDRIAIISHG 1107
Cdd:COG4778 152 -T--FSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
926-1090 |
2.74e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 59.12 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDiRSEMSTIRQNLGVCPQHNVLFDMLTVEEHIWFYACL---KG 1002
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKS 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1003 LSEKHVKVEMEQMALDVGLPPSKL----KSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSR-RGIWELLLK 1077
Cdd:PLN03211 173 LTKQEKILVAESVISELGLTKCENtiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLTLGSL 252
|
170
....*....|...
gi 507682765 1078 YRQGRTIILSTHH 1090
Cdd:PLN03211 253 AQKGKTIVTSMHQ 265
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1937-2076 |
3.29e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 57.10 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1937 PRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF------ 2009
Cdd:PRK10575 35 PAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIgrypwh 114
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2010 FALLR-GVPEKEvgKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK10575 115 GALGRfGAADRE--KVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALD 179
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1911-2122 |
3.47e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 58.48 E-value: 3.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYrrkrkP---AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGN-AFLNKNSILSN------ 1980
Cdd:PRK10762 4 LLQLKGIDKAF-----PgvkALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSiLYLGKEVTFNGpkssqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1981 --IHEVHQNMGYCPQFDAITELLTGREHVEFFAllrGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMA 2058
Cdd:PRK10762 79 agIGIIHQELNLIPQLTIAENIFLGREFVNRFG---RIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 507682765 2059 LIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:PRK10762 156 LSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1912-2135 |
3.63e-08 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 58.66 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGnaflnknsilsnihEVHQNMG 1989
Cdd:TIGR03269 1 IEVKNLTKKFDGKE--VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSG--------------RIIYHVA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 YCPQF-------------------------------DAITELLTGREHVEF---FAL------LRGVPE--KEVGKVGEW 2027
Cdd:TIGR03269 65 LCEKCgyverpskvgepcpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLqrtFALygddtvLDNVLEalEEIGYEGKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2028 AI-RKLGLLKYGE------KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVVL 2099
Cdd:TIGR03269 145 AVgRAVDLIEMVQlshritHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVL 224
|
250 260 270
....*....|....*....|....*....|....*.
gi 507682765 2100 TSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRF 2135
Cdd:TIGR03269 225 TSHWPEVIEDLSDKAIWLENGEIKEEGTPDEVVAVF 260
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1912-2121 |
3.63e-08 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 56.68 E-value: 3.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLT------------GDTTVTRGNAFLNKNSILS 1979
Cdd:PRK11264 4 IEVKNLVKKF--HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINlleqpeagtirvGDITIDTARSLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHE----VHQNMGYCPQFDAITELLTGRehveffALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLST 2055
Cdd:PRK11264 82 QLRQhvgfVFQNFNLFPHRTVLENIIEGP------VIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGR 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
921-1108 |
3.69e-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: 55.94 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 921 LNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKD--------IRSEmsTIRQNlgvcpqhnVLFDMLTVEE 992
Cdd:cd03250 26 LEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIayvsqepwIQNG--TIREN--------ILFGKPFDEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 993 hiwFY-----AClkglsekHVKVEMEQMAL----DVGlppsklkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:cd03250 96 ---RYekvikAC-------ALEPDLEILPDgdltEIG-------EKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 507682765 1064 DPYSRRGIWELLL--KYRQGRTIILSTHHMD---EAdilgDRIAIISHGK 1108
Cdd:cd03250 159 DAHVGRHIFENCIlgLLLNNKTRILVTHQLQllpHA----DQIVVLDNGR 204
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
1912-2128 |
3.87e-08 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 55.61 E-value: 3.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGNAFLNKNSILS-NIHEvHQNM 1988
Cdd:cd03217 1 LEIKDLH--VSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDlPPEE-RARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 G------YCPQFDAITelltgrehVEFFalLRGVPEkevgkvgewairklgllkygekyagNYSGGNKRKLSTAMALIGG 2062
Cdd:cd03217 78 GiflafqYPPEIPGVK--------NADF--LRYVNE-------------------------GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2063 PPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEAL-CTRMAIMVNGKFRCLGSV 2128
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDK 189
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
919-1089 |
6.44e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.88 E-value: 6.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI----RSEMSTIRQNLGVCPQhnvlfdmLTVEEHI 994
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInniaKPYCTYIGHNLGLKLE-------MTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 995 WFYaclkglSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWEL 1074
Cdd:PRK13541 92 KFW------SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNL 165
|
170
....*....|....*.
gi 507682765 1075 L-LKYRQGRTIILSTH 1089
Cdd:PRK13541 166 IvMKANSGGIVLLSSH 181
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1908-2121 |
6.74e-08 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 55.66 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS--NIHEVH 1985
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1986 QNMGYCPQFDAITELLTGREHVE---FFALlRGVPEKEVGKVGEWAIRklgLLKYGEKYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK11614 80 EAVAIVPEGRRVFSRMTVEENLAmggFFAE-RDQFQERIKWVYELFPR---LHERRIQRAGTMSGGEQQMLAIGRALMSQ 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2063 PPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11614 156 PRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGH 214
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1928-2122 |
6.87e-08 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 57.61 E-value: 6.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLN---------KNSILSNIHEVHQNMGYCPQFDAIT 1998
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDgqemrfastTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1999 ELLTGREHVEFFALLRGVPEKEVGKvgewAIRKLGL-------LKYgekyagnYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:PRK11288 99 NLYLGQLPHKGGIVNRRLLNYEARE----QLEHLGVdidpdtpLKY-------LSIGQRQMVEIAKALARNARVIAFDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2072 TTGMDPKARRFLWncalSIIK----EGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:PRK11288 168 TSSLSAREIEQLF----RVIRelraEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
871-1109 |
6.90e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 871 DEKSHPGSSQKGVSEIRMEEepTHLKlgvsiqnlvkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLF 950
Cdd:PLN03232 1220 IENNRPVSGWPSRGSIKFED--VHLR-----------YRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIV 1286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 951 PPTSGTAYILGKDI-RSEMSTIRQNLGVCPQHNVLF------DMLTVEEH----IWfyaclKGLSEKHVK--VEMEQMAL 1017
Cdd:PLN03232 1287 ELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFsgtvrfNIDPFSEHndadLW-----EALERAHIKdvIDRNPFGL 1361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1018 DvglppSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEAdIL 1097
Cdd:PLN03232 1362 D-----AEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTI-ID 1435
|
250
....*....|..
gi 507682765 1098 GDRIAIISHGKL 1109
Cdd:PLN03232 1436 CDKILVLSSGQV 1447
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1921-2136 |
1.01e-07 |
|
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: 55.18 E-value: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1921 YRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHEVHQNMGYCPQfdaiTE 1999
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQ----EN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2000 LLTGREHVEFFALLR-GVPEKEVGKVGEWA-----IRKLGLlKY----GEKYAGnYSGGNKRKLSTAMALIGGPPVVFLD 2069
Cdd:cd03252 86 VLFNRSIRDNIALADpGMSMERVIEAAKLAgahdfISELPE-GYdtivGEQGAG-LSGGQRQRIAIARALIHNPRILIFD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 2070 EPTTGMDPKARRFLWNCALSIIKeGRSVVLTSHSMEECEAlCTRMAIMVNGKFRCLGSVQHLKNRFG 2136
Cdd:cd03252 164 EATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1913-2102 |
1.02e-07 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.47 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1913 EIKELTKIYRRKrkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYC 1991
Cdd:COG4604 3 EIKNVSKRYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEF--FALLRGVPEKE-VGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFL 2068
Cdd:COG4604 81 RQENHINSRLTVRELVAFgrFPYSKGRLTAEdREIIDE-AIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507682765 2069 DEPTTGMDPKArrflwncALSIIK--------EGRSVVLTSH 2102
Cdd:COG4604 160 DEPLNNLDMKH-------SVQMMKllrrladeLGKTVVIVLH 194
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
901-1115 |
1.12e-07 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 55.57 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 901 IQNLVKV--YRDGM-----KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGK-----DIRSEM 968
Cdd:PRK15112 7 VRNLSKTfrYRTGWfrrqtVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 969 STIRQ-----NLGVCPQHNV--LFDM-------LTVEEHiwfyaclkglsEKHVKVEMEQmaldVGLPPSKLKSKTSQLS 1034
Cdd:PRK15112 87 QRIRMifqdpSTSLNPRQRIsqILDFplrlntdLEPEQR-----------EKQIIETLRQ----VGLLPDHASYYPHMLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1035 GGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKY--RQGRTIILSTHHMDEADILGDRIAIISHGKLCCV 1112
Cdd:PRK15112 152 PGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVER 231
|
...
gi 507682765 1113 GSS 1115
Cdd:PRK15112 232 GST 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1939-2105 |
1.14e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 55.36 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNsilsNIHEVHQNMGYCPQFDAIT-ELLTGR-----EHV---EF 2009
Cdd:PRK10619 31 GDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQ----TINLVRDKDGQLKVADKNQlRLLRTRltmvfQHFnlwSH 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2010 FALLRGVPEKEVGKVG-------EWAIRKLGLLKYGEKYAGNY----SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPK 2078
Cdd:PRK10619 107 MTVLENVMEAPIQVLGlskqearERAVKYLAKVGIDERAQGKYpvhlSGGQQQRVSIARALAMEPEVLLFDEPTSALDPE 186
|
170 180
....*....|....*....|....*..
gi 507682765 2079 ARRFLWNCALSIIKEGRSVVLTSHSME 2105
Cdd:PRK10619 187 LVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1032-1089 |
1.33e-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: 53.13 E-value: 1.33e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1032 QLSGGMQRKLSVALAF----VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ-GRTIILSTH 1089
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVkGAQVIVITH 139
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1911-2121 |
1.45e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 56.76 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGNAFLNKNSI----LS 1979
Cdd:TIGR02633 1 LLEMKGIVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyphgtwDGEIYWSGSPLKASNIrdteRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHEVHQNMGYCPQFDAITELLTGREhveffALLRG--VPEKEVGKVGEWAIRKLGL-LKYGEKYAGNYSGGNKRKLSTA 2056
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGNE-----ITLPGgrMAYNAMYLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2057 MALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1912-2102 |
1.67e-07 |
|
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: 54.54 E-value: 1.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGY 1990
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQfDAIteLLTG--REHVEFFAllRGVPEKEVGKVGEWA-----IRKL--GL-LKYGEKyAGNYSGGNKRKLSTAMALI 2060
Cdd:cd03251 81 VSQ-DVF--LFNDtvAENIAYGR--PGATREEVEEAARAAnahefIMELpeGYdTVIGER-GVKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507682765 2061 GGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSH 2102
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQA-ALERLMKNRTTFVIAH 195
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1936-2102 |
1.74e-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: 54.68 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPR-GECFGLLGVNGAGKSSTFKMLTGdttvtrgnaflnknsilsnihEVHQNMG-YC--PQFDAITELLTGREHVEFFA 2011
Cdd:cd03236 22 VPReGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSELQNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2012 LLRG--------------VPEKEVGKVGE------------WAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPV 2065
Cdd:cd03236 81 KLLEgdvkvivkpqyvdlIPKAVKGKVGEllkkkdergkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 507682765 2066 VFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
899-1092 |
1.85e-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: 1.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIWFYaclkglsEKHVKVEMEQMALDVGLP------PSKLKSKTSQ----LSGGMQRKLSVALAF 1047
Cdd:TIGR01271 1297 IPQKVFIFSG-TFRKNLDPY-------EQWSDEEIWKVAEEVGLKsvieqfPDKLDFVLVDggyvLSNGHKQLMCLARSI 1368
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMD 1092
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
910-1089 |
1.91e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 55.50 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 910 DGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPP---TSGTAYILGKDI----RSEMSTIRQNlgvcpQHN 982
Cdd:PRK09473 26 DGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRAE-----QIS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 983 VLF-DMLT-------VEEHIWFYACL-KGLSEKHVKVEMEQMALDVGLPPSKLKSKT--SQLSGGMQRKLSVALAFVGGS 1051
Cdd:PRK09473 101 MIFqDPMTslnpymrVGEQLMEVLMLhKGMSKAEAFEESVRMLDAVKMPEARKRMKMypHEFSGGMRQRVMIAMALLCRP 180
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 507682765 1052 KVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTH 1089
Cdd:PRK09473 181 KLLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1927-2076 |
2.24e-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: 56.29 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1927 PAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNI--HEVHQNMGYCPQ----FD-AITE 1999
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL-KDIdrHTLRQFINYLPQepyiFSgSILE 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2000 -LLTGREhveffallRGVPEKEVGKVGEWA-IRK------LGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEP 2071
Cdd:TIGR01193 567 nLLLGAK--------ENVSQDEIWAACEIAeIKDdienmpLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDES 638
|
....*
gi 507682765 2072 TTGMD 2076
Cdd:TIGR01193 639 TSNLD 643
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
1939-2108 |
2.43e-07 |
|
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: 54.01 E-value: 2.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHE-------------------VHQNMGY----CPqFD 1995
Cdd:cd03248 40 GEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylhskvslvgqepvlfarsLQDNIAYglqsCS-FE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1996 AITELLTGREHVEFFALLRGVPEKEVGKVGewairklGLLkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGM 2075
Cdd:cd03248 119 CVKEAAQKAHAHSFISELASGYDTEVGEKG-------SQL----------SGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190
....*....|....*....|....*....|...
gi 507682765 2076 DPKARRFLwNCALSIIKEGRSVVLTSHSMEECE 2108
Cdd:cd03248 182 DAESEQQV-QQALYDWPERRTVLVIAHRLSTVE 213
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
1925-2126 |
2.71e-07 |
|
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: 55.91 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1925 RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI-LSNIHEVHQNMGYCPQfdaitelltg 2003
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsQWDREELGRHIGYLPQ---------- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2004 reHVEFF--------ALLRGV-PEKevgkVGEWA--------IRKL--GllkY----GEkyAGNY-SGGNKRKLSTAMAL 2059
Cdd:COG4618 414 --DVELFdgtiaeniARFGDAdPEK----VVAAAklagvhemILRLpdG---YdtriGE--GGARlSGGQRQRIGLARAL 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKARRFLwNCALSIIKE-GRSVVLTSHSMeecEAL--CTRMAIMVNGKFRCLG 2126
Cdd:COG4618 483 YGDPRLVVLDEPNSNLDDEGEAAL-AAAIRALKArGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1912-2129 |
2.73e-07 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 55.09 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIlSNIHEVHQNMGYC 1991
Cdd:PRK10851 3 IEIANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQFDAITELLTGREHVEFFalLRGVPEKEvgKVGEWAIRK--------LGLLKYGEKYAGNYSGGNKRKLSTAMALIGGP 2063
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAFG--LTVLPRRE--RPNAAAIKAkvtqllemVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2064 PVVFLDEPTTGMDPKARRFL--WNCALSIIKEGRSVVLTsHSMEECEALCTRMAIMVNGKFRCLGSVQ 2129
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELrrWLRQLHEELKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1887-2121 |
3.17e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 3.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1887 PLNDEDEDVRRERQRILDGGGQND-ILEIKELTKIY--------RRKRK-PAVDRICVGIPRGECFGLLGVNGAGKSSTF 1956
Cdd:PRK10261 288 PLISLEHPAKQEPPIEQDTVVDGEpILQVRNLVTRFplrsgllnRVTREvHAVEKVSFDLWPGETLSLVGESGSGKSTTG 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1957 KMLTGDTTVTRGNAFLNKNSI----LSNIHEVHQNMGYCPQ------------FDAITELLtgREHveffALLRGvpeKE 2020
Cdd:PRK10261 368 RALLRLVESQGGEIIFNGQRIdtlsPGKLQALRRDIQFIFQdpyasldprqtvGDSIMEPL--RVH----GLLPG---KA 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2021 VGKVGEWAIRKLGLL-KYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKE-GRSVV 2098
Cdd:PRK10261 439 AAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYL 518
|
250 260
....*....|....*....|...
gi 507682765 2099 LTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK10261 519 FISHDMAVVERISHRVAVMYLGQ 541
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
899-1114 |
3.19e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 55.63 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNL-VKVYRDGMKV-AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYI--------------LGK 962
Cdd:PRK10261 13 LAVENLnIAFMQEQQKIaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCdkmllrrrsrqvieLSE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 963 DIRSEMSTIR-QNLGVCPQHNV--LFDMLTVEEHIWFYACL-KGLSEKHVKVEMEQMALDVGLPPSK--LKSKTSQLSGG 1036
Cdd:PRK10261 93 QSAAQMRHVRgADMAMIFQEPMtsLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtiLSRYPHQLSGG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1037 MQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKYRQGRTIILSTHHMDEADILGDRIAIISHGKLCCVGS 1114
Cdd:PRK10261 173 MRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
911-1087 |
3.40e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 55.56 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYiLGKDIRsemstirqnLGVCPQHNVLFdmLTV 990
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG-LAKGIK---------LGYFAQHQLEF--LRA 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 991 EEhiwfyACLKGLSEKHVKvEMEQMALD----VGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY 1066
Cdd:PRK10636 391 DE-----SPLQHLARLAPQ-ELEQKLRDylggFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLD 464
|
170 180
....*....|....*....|.
gi 507682765 1067 SRRGIWELLLKYrQGRTIILS 1087
Cdd:PRK10636 465 MRQALTEALIDF-EGALVVVS 484
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
926-1091 |
3.59e-07 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 53.10 E-value: 3.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMSTI-----RQNLGVCPQHNVLFDMlTVEEHIWFYACL 1000
Cdd:cd03290 27 GQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSVAYAAQKPWLLNA-TVEENITFGSPF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1001 KGLSEKHVkVEMEQMALDVGLPP----SKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPY-SRRGIWELL 1075
Cdd:cd03290 106 NKQRYKAV-TDACSLQPDIDLLPfgdqTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHlSDHLMQEGI 184
|
170
....*....|....*...
gi 507682765 1076 LKYRQG--RTIILSTHHM 1091
Cdd:cd03290 185 LKFLQDdkRTLVLVTHKL 202
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1926-2102 |
4.41e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 52.64 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQNMGYCPQFDAITELLTGRE 2005
Cdd:PRK13540 14 QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2006 HVeFFALLRGVPEKEVGKVgewaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWN 2085
Cdd:PRK13540 94 NC-LYDIHFSPGAVGITEL----CRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIIT 168
|
170
....*....|....*..
gi 507682765 2086 CALSIIKEGRSVVLTSH 2102
Cdd:PRK13540 169 KIQEHRAKGGAVLLTSH 185
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
899-1109 |
4.46e-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: 53.70 E-value: 4.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPpTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMlTVEEHIWFYAClkglsekHVKVEMEQMALDVGLP------PSKLKSKTSQ----LSGGMQRKLSVALAF 1047
Cdd:cd03289 82 IPQKVFIFSG-TFRKNLDPYGK-------WSDEEIWKVAEEVGLKsvieqfPGQLDFVLVDggcvLSHGHKQLMCLARSV 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507682765 1048 VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKL 1109
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1912-2109 |
4.83e-07 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 52.87 E-value: 4.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTkIYRRKRkPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTT---VTRGNAFLNKNSILS-NIHEvhQN 1987
Cdd:COG4136 2 LSLENLT-ITLGGR-PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTAlPAEQ--RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1988 MGYCPQfdaiTELLtgrehveF----------FALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAM 2057
Cdd:COG4136 78 IGILFQ----DDLL-------FphlsvgenlaFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2058 ALIGGPPVVFLDEPTTGMDP----KARRFLWNcalSIIKEGRSVVLTSHSMEECEA 2109
Cdd:COG4136 147 ALLAEPRALLLDEPFSKLDAalraQFREFVFE---QIRQRGIPALLVTHDEEDAPA 199
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1911-2122 |
5.14e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 54.65 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTkIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI------------L 1978
Cdd:COG3845 257 VLEVENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItglsprerrrlgV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1979 SNIHEVHQNMGYCPQFDaITE--LLTGREHVEF--FALLRGvpekevGKVGEWAIRKLgllkygEKY----------AGN 2044
Cdd:COG3845 336 AYIPEDRLGRGLVPDMS-VAEnlILGRYRRPPFsrGGFLDR------KAIRAFAEELI------EEFdvrtpgpdtpARS 402
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2045 YSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKF 2122
Cdd:COG3845 403 LSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
1925-2076 |
6.36e-07 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 53.07 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1925 RKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNI-HEVHQNMGYCPQfDAIT----- 1998
Cdd:PRK10253 19 KYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYAsKEVARRIGLLAQ-NATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1999 --ELLT-GR-EHVEFFALLRGVPEKEVGKvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTG 2074
Cdd:PRK10253 98 vqELVArGRyPHQPLFTRWRKEDEEAVTK----AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
..
gi 507682765 2075 MD 2076
Cdd:PRK10253 174 LD 175
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1939-2076 |
8.76e-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: 51.88 E-value: 8.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTvtrGNAFLNkNSILSNIHEVHQNMG-------YCPQFDAITELLTGREHVEFFA 2011
Cdd:cd03233 33 GEMVLVLGRPGSGCSTLLKALANRTE---GNVSVE-GDIHYNGIPYKEFAEkypgeiiYVSEEDVHFPTLTVRETLDFAL 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2012 LLRGvpeKEVgkvgewaIRKLgllkygekyagnySGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:cd03233 109 RCKG---NEF-------VRGI-------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
1912-2121 |
1.07e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 52.37 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGnAFLNKNSILSNIHEVHQNMgyc 1991
Cdd:PRK11247 13 LLLNAVSKRYGERT--VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAGTAPLAEAREDTRLM--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 pqfdaitelltgrehvefFALLRGVPEKEV------GKVGEW------AIRKLGLLKYGEKYAGNYSGGNKRKLSTAMAL 2059
Cdd:PRK11247 87 ------------------FQDARLLPWKKVidnvglGLKGQWrdaalqALAAVGLADRANEWPAALSGGQKQRVALARAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2060 IGGPPVVFLDEPTTGMDPKAR-------RFLWNcalsiiKEGRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11247 149 IHRPGLLLLDEPLGALDALTRiemqdliESLWQ------QHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
933-1065 |
1.17e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 51.77 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 933 GHNGAGKTTTMSILTGLFPPTSGTAYILGKDI-RSEMSTIRQNLGVCPQhnvLFDMLTVEEHIWFyacLKGLSEKHVKvE 1011
Cdd:PRK13543 44 GDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtRGDRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAK-Q 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1012 MEQMALD-VGLPPSKlKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDP 1065
Cdd:PRK13543 117 MPGSALAiVGLAGYE-DTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1926-2131 |
1.34e-06 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.41 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSS---TFKMLTGDTTVTR--GNAFLNKNSILS--NIHEVHQNMGYCPQ----- 1993
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTflrTLNRMNDKVSGYRysGDVLLGGRSIFNyrDVLEFRRRVGMLFQrpnpf 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1994 -FDAITELLTG-REHV-----EFfallRGVPEKEVGKVGEWAIRKLGLlkygEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK14271 114 pMSIMDNVLAGvRAHKlvprkEF----RGVAQARLTEVGLWDAVKDRL----SDSPFRLSGGQQQLLCLARTLAVNPEVL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2067 FLDEPTTGMDP----KARRFLWNCALSIikegrSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHL 2131
Cdd:PRK14271 186 LLDEPTSALDPttteKIEEFIRSLADRL-----TVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
915-1089 |
1.46e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 52.82 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFP-PTSGTAYIL---GKDIR------------SEMSTIRQN--LG 976
Cdd:PRK11022 22 AVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPGRVMAEKLefnGQDLQrisekerrnlvgAEVAMIFQDpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 977 VCPQHNVLFD-MLTVEEHiwfyaclKGLSEKhvkvEMEQMALD----VGLP--PSKLKSKTSQLSGGMQRKLSVALAFVG 1049
Cdd:PRK11022 102 LNPCYTVGFQiMEAIKVH-------QGGNKK----TRRQRAIDllnqVGIPdpASRLDVYPHQLSGGMSQRVMIAMAIAC 170
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 507682765 1050 GSKVVILDEPTAGVDPYSRRGIWELLLKYRQGR--TIILSTH 1089
Cdd:PRK11022 171 RPKLLIADEPTTALDVTIQAQIIELLLELQQKEnmALVLITH 212
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1937-2121 |
1.65e-06 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 51.55 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1937 PRGECFGLLGVNGAGKSSTFKML-------TGDTTVTrGNAF-LNKNSILSNIHEVHQNMGYCPQFDAITELLTGREH-V 2007
Cdd:COG4161 26 PSGETLVLLGPSGAGKSSLLRVLnlletpdSGQLNIA-GHQFdFSQKPSEKAIRLLRQKVGMVFQQYNLWPHLTVMENlI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2008 EFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKarrfLWNCA 2087
Cdd:COG4161 105 EAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPE----ITAQV 180
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 2088 LSIIKE----GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:COG4161 181 VEIIRElsqtGITQVIVTHEVEFARKVASQVVYMEKGR 218
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
926-1088 |
2.14e-06 |
|
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: 52.90 E-value: 2.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGVCPQHNVLF-DmlTVEEHIWfYACLkGL 1003
Cdd:COG5265 384 GKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRP-DA 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1004 SEKHVkVEMEQMA-LD---VGLPpsK----------LKsktsqLSGG-MQRklsVALA--FVGGSKVVILDEPTAGVDPY 1066
Cdd:COG5265 460 SEEEV-EAAARAAqIHdfiESLP--DgydtrvgergLK-----LSGGeKQR---VAIArtLLKNPPILIFDEATSALDSR 528
|
170 180
....*....|....*....|....*..
gi 507682765 1067 SRRGIWELLLKYRQGRT--II---LST 1088
Cdd:COG5265 529 TERAIQAALREVARGRTtlVIahrLST 555
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
915-1113 |
2.34e-06 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 52.94 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 915 AVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIR----SEMSTIRQNL---------GVCPQH 981
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIqfifqdpyaSLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 982 NVLFDMLtveEHIWFYACLKG-LSEKHVKVEMEQmaldVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK10261 419 TVGDSIM---EPLRVHGLLPGkAAAARVAWLLER----VGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1061 AGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEADILGDRIAIISHGKLCCVG 1113
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1898-2136 |
2.37e-06 |
|
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: 53.41 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1898 ERQRILDGGGQNdiLEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLnKNSI 1977
Cdd:TIGR00957 625 ERRTIKPGEGNS--ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KGSV 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1978 lsnihevhqnmGYCP-----QFDAITE-LLTG--------REHVEFFALLrgvPEKEVGKVGEWAirklgllKYGEKyAG 2043
Cdd:TIGR00957 702 -----------AYVPqqawiQNDSLREnILFGkalnekyyQQVLEACALL---PDLEILPSGDRT-------EIGEK-GV 759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2044 NYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSI--IKEGRSVVLTSHSMEECEALcTRMAIMVNGK 2121
Cdd:TIGR00957 760 NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFEHVIGPegVLKNKTRILVTHGISYLPQV-DVIIVMSGGK 838
|
250
....*....|....*
gi 507682765 2122 FRCLGSVQHLKNRFG 2136
Cdd:TIGR00957 839 ISEMGSYQELLQRDG 853
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
899-1087 |
2.61e-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: 52.63 E-value: 2.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRseMSTIRQNlgvc 978
Cdd:TIGR03719 323 IEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETVK--LAYVDQS---- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 979 pqHNVLFDMLTVEEHIwfyacLKGLSEKHV-KVEMEQMALdVG---LPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKVV 1054
Cdd:TIGR03719 394 --RDALDPNKTVWEEI-----SGGLDIIKLgKREIPSRAY-VGrfnFKGSDQQKKVGQLSGGERNRVHLAKTLKSGGNVL 465
|
170 180 190
....*....|....*....|....*....|...
gi 507682765 1055 ILDEPTAGVDPYSRRGIWELLLKYrQGRTIILS 1087
Cdd:TIGR03719 466 LLDEPTNDLDVETLRALEEALLNF-AGCAVVIS 497
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1911-2123 |
3.46e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 52.24 E-value: 3.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIY----RRKRkpaVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGD-TTVTRGNAFLN--KNSILSNIHE 1983
Cdd:PRK13549 259 ILEVRNLTAWDpvnpHIKR---VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAyPGRWEGEIFIDgkPVKIRNPQQA 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 VHQNMGYCPQ---FDAITELLTGREHVEFFAL----LRGV--PEKEVGKVGEwAIRKLGLlkygeKYA------GNYSGG 2048
Cdd:PRK13549 336 IAQGIAMVPEdrkRDGIVPVMGVGKNITLAALdrftGGSRidDAAELKTILE-SIQRLKV-----KTAspelaiARLSGG 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2049 NKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRMAIMVNGKFR 2123
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
899-1064 |
3.67e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 3.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRS-EMSTIRQNLGV 977
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGI 1317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLF------DMLTVEEH----IWfyaclKGLSEKHVK--VEMEQMALDvglppSKLKSKTSQLSGGMQRKLSVAL 1045
Cdd:PLN03130 1318 IPQAPVLFsgtvrfNLDPFNEHndadLW-----ESLERAHLKdvIRRNSLGLD-----AEVSEAGENFSVGQRQLLSLAR 1387
|
170
....*....|....*....
gi 507682765 1046 AFVGGSKVVILDEPTAGVD 1064
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVD 1406
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1921-2114 |
3.71e-06 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 50.23 E-value: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1921 YRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNihEVHQNMGYCPQFDAITEL 2000
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG--DRSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2001 LTGREHVEFFALLRGV-PEKEVGKvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKA 2079
Cdd:PRK13543 97 LSTLENLHFLCGLHGRrAKQMPGS----ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEG 172
|
170 180 190
....*....|....*....|....*....|....*
gi 507682765 2080 RRFLWNCALSIIKEGRSVVLTSHSMEECEALCTRM 2114
Cdd:PRK13543 173 ITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRM 207
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1773-2105 |
4.31e-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: 50.85 E-value: 4.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1773 VNLFIGINGSVATFVLELFtnnklnnindilksvflifphfclgRGLIDMVKNQAMADALERFGENRFISPLSWDLvGRN 1852
Cdd:pfam13304 1 INVLIGPNGSGKSNLLEAL-------------------------RFLADFDALVIGLTDERSRNGGIGGIPSLLNG-IDP 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1853 LFAMAVEGVVFFLITVLIQYRFFIRPRAVKTKfLPLNDEDEDVRRERQRILDGGGQNDILEIKELTKIYRRKRKPAVDRI 1932
Cdd:pfam13304 55 KEPIEFEISEFLEDGVRYRYGLDLEREDVEEK-LSSKPTLLEKRLLLREDSEEREPKFPPEAEELRLGLDVEERIELSLS 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1933 CVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEVHQnmgYCPQFDAITELLTGREHVEFFAL 2012
Cdd:pfam13304 134 ELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQR---LVRGLKLADLNLSDLGEGIEKSL 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2013 LRGVPEKEVGKVgeWAIRKLGllkyGEKYAGNYSGGNKRKLSTAMALI---GGPPVVFLDEPTTGMDPKARRFLWNCALS 2089
Cdd:pfam13304 211 LVDDRLRERGLI--LLENGGG----GELPAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKE 284
|
330
....*....|....*.
gi 507682765 2090 IIKEGRSVVLTSHSME 2105
Cdd:pfam13304 285 LSRNGAQLILTTHSPL 300
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1908-2133 |
5.00e-06 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 50.53 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1908 QNDILEIKELTkiYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSI----LSNIHE 1983
Cdd:PRK11831 4 VANLVDMRGVS--FTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 VHQNMGYCPQFDAITELLTGREHVEFfallrgvPEKEVGKVGEWAIRKLGLLKY---GEKYAGN-----YSGGNKRKLST 2055
Cdd:PRK11831 82 VRKRMSMLFQSGALFTDMNVFDNVAY-------PLREHTQLPAPLLHSTVMMKLeavGLRGAAKlmpseLSGGMARRAAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2056 AMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE-----GRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQH 2130
Cdd:PRK11831 155 ARAIALEPDLIMFDEPFVGQDPITMGVL----VKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
...
gi 507682765 2131 LKN 2133
Cdd:PRK11831 231 LQA 233
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1939-2076 |
6.35e-06 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 50.49 E-value: 6.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTG---DTTVTRGNAFLNKNSILsNIHEVHQNMGYCPQF-----DAITEL----LTGREH 2006
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGllaANGRIGGSATFNGREIL-NLPEKELNKLRAEQIsmifqDPMTSLnpymRVGEQL 120
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2007 VEFFALLRGVPEKEVGkvgEWAIRKLGLLKYGEK------YAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK09473 121 MEVLMLHKGMSKAEAF---EESVRMLDAVKMPEArkrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALD 193
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1911-2120 |
6.45e-06 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 49.77 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLT--GD----TTVTrgnaflnkNSILSNIHEV 1984
Cdd:PRK14239 5 ILQVSDLSVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpeVTIT--------GSIVYNGHNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1985 hqnmgYCPQFDAItEL---------------LTGREHVEFFALLRGVPEKEV-GKVGEWAIRklGLLKYGE------KYA 2042
Cdd:PRK14239 75 -----YSPRTDTV-DLrkeigmvfqqpnpfpMSIYENVVYGLRLKGIKDKQVlDEAVEKSLK--GASIWDEvkdrlhDSA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 2043 GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSiIKEGRSVVLTSHSMEECEALCTRMAIMVNG 2120
Cdd:PRK14239 147 LGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLG-LKDDYTMLLVTRSMQQASRISDRTGFFLDG 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
899-1093 |
7.50e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.17 E-value: 7.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSEMST---IRQNL 975
Cdd:PRK10938 261 IVLNNGVVSYND--RPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLTLFGRRRGSGETiwdIKKHI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GV------------CPQHNVL----FDmltveeHIWFYaclKGLSEKHVKVEMEQMALdVGLPPSKLKSKTSQLSGGMQR 1039
Cdd:PRK10938 339 GYvssslhldyrvsTSVRNVIlsgfFD------SIGIY---QAVSDRQQKLAQQWLDI-LGIDKRTADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 507682765 1040 KLSVALAFVGGSKVVILDEPTAGVDPYSR---RGIWELLLkyRQGRTIILSTHHMDE 1093
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRqlvRRFVDVLI--SEGETQLLFVSHHAE 463
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
911-1114 |
7.78e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 49.73 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAyilgkdIRSEMSTIrqnlGVCPQhNVLFDM--- 987
Cdd:PRK09544 15 GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI------KRNGKLRI----GYVPQ-KLYLDTtlp 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 988 LTVEEhiwFYACLKGLSEKHVKVEME--QMALDVGLPPSKlksktsqLSGG-MQRKLsVALAFVGGSKVVILDEPTAGVD 1064
Cdd:PRK09544 84 LTVNR---FLRLRPGTKKEDILPALKrvQAGHLIDAPMQK-------LSGGeTQRVL-LARALLNRPQLLVLDEPTQGVD 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 507682765 1065 PYSRRGIWELLLKYRQ--GRTIILSTH--HMDEADIlgDRIAIISHgKLCCVGS 1114
Cdd:PRK09544 153 VNGQVALYDLIDQLRRelDCAVLMVSHdlHLVMAKT--DEVLCLNH-HICCSGT 203
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
923-1090 |
8.62e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 48.76 E-value: 8.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 923 FYEGqITSFLGHNGAGKTTTMS----ILTGLFPPTSGTAYILGKDIRSEMS----------------TIRQNLGV----- 977
Cdd:cd03240 20 FFSP-LTLIVGQNGAGKTTIIEalkyALTGELPPNSKGGAHDPKLIREGEVraqvklafenangkkyTITRSLAIlenvi 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 -CPQhnvlfdmltvEEHIWFyaclkglsekhvkveMEQMAldvglppsklksktSQLSGGMQRKLSV----ALAFVGGSK 1052
Cdd:cd03240 99 fCHQ----------GESNWP---------------LLDMR--------------GRCSGGEKVLASLiirlALAETFGSN 139
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507682765 1053 --VVILDEPTAGVDPYSRRGIWELLLKYRQG---RTIILSTHH 1090
Cdd:cd03240 140 cgILALDEPTTNLDEENIEESLAEIIEERKSqknFQLIVITHD 182
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1926-2102 |
1.30e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 50.55 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQfDAIteLLTG- 2003
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQ-DTF--LFSGt 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2004 -REHVEFFALlrGVPEKEVgkvgEWAIRKLGLLKY------------GEKyAGNYSGGNKRKLSTAMALIGGPPVVFLDE 2070
Cdd:COG1132 430 iRENIRYGRP--DATDEEV----EEAAKAAQAHEFiealpdgydtvvGER-GVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190
....*....|....*....|....*....|..
gi 507682765 2071 PTTGMDPKARRFLWNcALSIIKEGRSVVLTSH 2102
Cdd:COG1132 503 ATSALDTETEALIQE-ALERLMKGRTTIVIAH 533
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
897-1127 |
1.31e-05 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 50.48 E-value: 1.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 897 LGVSIQNLVkvYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTayILGKDI---RSEMSTIRQ 973
Cdd:PRK10789 314 LDVNIRQFT--YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGD--IRFHDIpltKLQLDSWRS 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 974 NLGVCPQHNVLFDMlTVEEHIWFyACLKGLSEkhvkvEMEQMAL------DV-GLPP---SKLKSKTSQLSGGMQRKLSV 1043
Cdd:PRK10789 390 RLAVVSQTPFLFSD-TVANNIAL-GRPDATQQ-----EIEHVARlasvhdDIlRLPQgydTEVGERGVMLSGGQKQRISI 462
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1044 ALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMdEADILGDRIAIISHGKLCCVGSSLFLKNQlg 1123
Cdd:PRK10789 463 ARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQ-- 539
|
....
gi 507682765 1124 TGYY 1127
Cdd:PRK10789 540 SGWY 543
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
913-1192 |
1.42e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.55 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 913 KVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYilgkdirSEMStirqnLGVCPQHNVLFDMlTVEE 992
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW-------AERS-----IAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 993 HIWFY-----ACLkglsekHVKVEMEQMALDVGLPPSKLKS----KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PTZ00243 740 NILFFdeedaARL------ADAVRVSQLEADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1064 DPY-SRRGIWELLLKYRQGRTIILSTHHMDEADiLGDRIAIISHGKLCCVGSSlflKNQLGTGYYLTL---VKKDVESSL 1139
Cdd:PTZ00243 814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVP-RADYVVALGDGRVEFSGSS---ADFMRTSLYATLaaeLKENKDSKE 889
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1140 GSCRNSSSTVSNLKKEDSVSQSSSDAGLGSDHESDTLTIDVSAISNLIRKHVA 1192
Cdd:PTZ00243 890 GDADAEVAEVDAAPGGAVDHEPPVAKQEGNAEGGDGAALDAAAGRLMTREEKA 942
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
1031-1089 |
1.48e-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: 49.31 E-value: 1.48e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1031 SQLSGGMQRKLSVALAF---VGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQGRT-IILSTH 1089
Cdd:pfam13304 235 FELSDGTKRLLALLAALlsaLPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAqLILTTH 297
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1936-2102 |
1.65e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPR-GECFGLLGVNGAGKSSTFKMLTG---------DTTVT--------RGNAFLNKNSILSN--IHEVHQnmgycPQF- 1994
Cdd:PRK13409 95 IPKeGKVTGILGPNGIGKTTAVKILSGelipnlgdyEEEPSwdevlkrfRGTELQNYFKKLYNgeIKVVHK-----PQYv 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1995 DAITELLTG--REhveffaLLRGVPEKevGKVGEwAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK13409 170 DLIPKVFKGkvRE------LLKKVDER--GKLDE-VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPT 240
|
170 180 190
....*....|....*....|....*....|..
gi 507682765 2073 TGMDPKARrflWNCALSI--IKEGRSVVLTSH 2102
Cdd:PRK13409 241 SYLDIRQR---LNVARLIreLAEGKYVLVVEH 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
933-1109 |
1.71e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 933 GHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRseMSTIRQNlgvcPQHNV---LFDMLT-----VEEHIWFYACLKGL- 1003
Cdd:PRK11147 36 GRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLI--VARLQQD----PPRNVegtVYDFVAegieeQAEYLKRYHDISHLv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1004 ----SEKHVKvEME--QMALD-----------------VGLPPSKlksKTSQLSGGMQRKLSVALAFVGGSKVVILDEPT 1060
Cdd:PRK11147 109 etdpSEKNLN-ELAklQEQLDhhnlwqlenrinevlaqLGLDPDA---ALSSLSGGWLRKAALGRALVSNPDVLLLDEPT 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1061 AGVDpysrrgI----W-ELLLKYRQGrTIILSTHhmDEADI--LGDRIAIISHGKL 1109
Cdd:PRK11147 185 NHLD------IetieWlEGFLKTFQG-SIIFISH--DRSFIrnMATRIVDLDRGKL 231
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1912-2077 |
1.83e-05 |
|
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: 48.26 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSST----FKMLtgdtTVTRGNAFLNKNSILS-NIHEVHQ 1986
Cdd:cd03244 3 IEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQfDAIteLLTG--REHVEFFALlrgVPEKEVgkvgeW-AIRKLGLLKYGEKYAG-----------NYSGGNKRK 2052
Cdd:cd03244 79 RISIIPQ-DPV--LFSGtiRSNLDPFGE---YSDEEL-----WqALERVGLKEFVESLPGgldtvveeggeNLSVGQRQL 147
|
170 180
....*....|....*....|....*
gi 507682765 2053 LSTAMALIGGPPVVFLDEPTTGMDP 2077
Cdd:cd03244 148 LCLARALLRKSKILVLDEATASVDP 172
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
926-1109 |
1.90e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.12 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 926 GQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYIlgkdirsemstIRQNLGVCPQHNVLFDMlTVEEHIWFYACLKGLS- 1004
Cdd:PLN03130 643 GSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDPERy 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1005 EKHVKVEMEQMALDVgLPPSKLKS---KTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-Q 1080
Cdd:PLN03130 711 ERAIDVTALQHDLDL-LPGGDLTEigeRGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190
....*....|....*....|....*....|..
gi 507682765 1081 GRTIILST---HHMDEAdilgDRIAIISHGKL 1109
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMI 817
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1926-2102 |
2.16e-05 |
|
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: 48.00 E-value: 2.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQ----FDAITE- 1999
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQdtvlFNDTIGy 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2000 -LLTGR-----EHVEFFA-------LLRGVPEKEVGKVGEwaiRKLGLlkygekyagnySGGNKRKLSTAMALIGGPPVV 2066
Cdd:cd03253 94 nIRYGRpdatdEEVIEAAkaaqihdKIMRFPDGYDTIVGE---RGLKL-----------SGGEKQRVAIARAILKNPPIL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKeGRSVVLTSH 2102
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAH 194
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1911-2104 |
4.02e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 47.18 E-value: 4.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSIL----SNIHEVHQ 1986
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITrlknREVPFLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1987 NMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVV 2066
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 2067 FLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSHSM 2104
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
905-1091 |
4.12e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 49.26 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 905 VKVYRDgmkvavdgLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILG----KDIrsEMSTIRQNLGVCPQ 980
Cdd:PTZ00265 398 VEIYKD--------LNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDI--NLKWWRSKIGVVSQ 467
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLF----------------DMLTVEEHI----------------WFYACLKGLSEK----------HVKVEMEQM--- 1015
Cdd:PTZ00265 468 DPLLFsnsiknnikyslyslkDLEALSNYYnedgndsqenknkrnsCRAKCAGDLNDMsnttdsneliEMRKNYQTIkds 547
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1016 -ALDV-----------GLP---PSKLKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELL--LKY 1078
Cdd:PTZ00265 548 eVVDVskkvlihdfvsALPdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTInnLKG 627
|
250
....*....|...
gi 507682765 1079 RQGRTIILSTHHM 1091
Cdd:PTZ00265 628 NENRITIIIAHRL 640
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2042-2122 |
4.23e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.63 E-value: 4.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2042 AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWncalSII----KEGRSVVLTSHSMEECEALCTRMAIM 2117
Cdd:NF040905 402 VGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIY----TIInelaAEGKGVIVISSELPELLGMCDRIYVM 477
|
....*
gi 507682765 2118 VNGKF 2122
Cdd:NF040905 478 NEGRI 482
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
919-1109 |
4.58e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDI--RSEMSTI----------RQNLGVCPQHNVLFD 986
Cdd:PRK10982 267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFN 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 MLTveEHIWFYACLKGL-SEKHVKVEMEQM--ALDVGLPPSKlkSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGV 1063
Cdd:PRK10982 347 SLI--SNIRNYKNKVGLlDNSRMKSDTQWVidSMRVKTPGHR--TQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGI 422
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 1064 DPYSRRGIWELLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1109
Cdd:PRK10982 423 DVGAKFEIYQLIAELaKKDKGIIIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1911-2121 |
5.45e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.39 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG-------DTTVTRGNAFLNKNSIL----S 1979
Cdd:PRK13549 5 LLEMKNITKTFGGVK--ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyphgtyEGEIIFEGEELQASNIRdterA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1980 NIHEVHQNMGYCPQFDAITELLTGREhveffallrgvpekevgkvgewaIRKLGLLKYGEKYA----------------- 2042
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNE-----------------------ITPGGIMDYDAMYLraqkllaqlkldinpat 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2043 --GNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLwncaLSIIKE----GRSVVLTSHSMEECEALCTRMAI 2116
Cdd:PRK13549 140 pvGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTESETAVL----LDIIRDlkahGIACIYISHKLNEVKAISDTICV 215
|
....*
gi 507682765 2117 MVNGK 2121
Cdd:PRK13549 216 IRDGR 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1912-2113 |
5.55e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 48.35 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYrrKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSilsnihevhqNMGYC 1991
Cdd:PRK15064 320 LEVENLTKGF--DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENA----------NIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 PQfdaitelltgrEHVEFFA----LLRGVPEKEVGKVGEWAIRK-LGLLKYGE----KYAGNYSGGNKRKLSTAMALIGG 2062
Cdd:PRK15064 388 AQ-----------DHAYDFEndltLFDWMSQWRQEGDDEQAVRGtLGRLLFSQddikKSVKVLSGGEKGRMLFGKLMMQK 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2063 PPVVFLDEPTTGMDPKARRFLwNCALSIIkEGrSVVLTSHSMEECEALCTR 2113
Cdd:PRK15064 457 PNVLVMDEPTNHMDMESIESL-NMALEKY-EG-TLIFVSHDREFVSSLATR 504
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1917-2076 |
6.73e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.57 E-value: 6.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1917 LTKIYRRKRKPAVD--RICVGIPR-GECFGLLGVNGAGKSSTFKMLTGDTTvtrGNAFLNKNSILSNIHEVHQNMG---- 1989
Cdd:TIGR00956 62 FRKLKKFRDTKTFDilKPMDGLIKpGELTVVLGRPGSGCSTLLKTIASNTD---GFHIGVEGVITYDGITPEEIKKhyrg 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1990 ---YCPQFDAITELLTGREHVEFFALLR-------GVPEKE-VGKVGEWAIRKLGL-----LKYGEKYAGNYSGGNKRKL 2053
Cdd:TIGR00956 139 dvvYNAETDVHFPHLTVGETLDFAARCKtpqnrpdGVSREEyAKHIADVYMATYGLshtrnTKVGNDFVRGVSGGERKRV 218
|
170 180
....*....|....*....|...
gi 507682765 2054 STAMALIGGPPVVFLDEPTTGMD 2076
Cdd:TIGR00956 219 SIAEASLGGAKIQCWDNATRGLD 241
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
911-1080 |
7.04e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 7.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 911 GMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFpPTSGTAYILGKDI----RSEMSTIRQNLGVCPQ--HNVL 984
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 985 FDMLTVEEHIwfyacLKGLS-----------EKHVKVEMEQmaldVGLPPSKLKSKTSQLSGGMQRKLSVALAFVGGSKV 1053
Cdd:PRK15134 376 NPRLNVLQII-----EEGLRvhqptlsaaqrEQQVIAVMEE----VGLDPETRHRYPAEFSGGQRQRIAIARALILKPSL 446
|
170 180
....*....|....*....|....*..
gi 507682765 1054 VILDEPTAGVDPYSRRGIWELLLKYRQ 1080
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQ 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
925-1104 |
7.58e-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: 47.86 E-value: 7.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 925 EGQITSFLGHNGAGKTTTMSILTGLF---------PPT--------SGTA---YIlgKDIRS-EMSTIRQnlgvcPQHnv 983
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkpnlgdydeEPSwdevlkrfRGTElqdYF--KKLANgEIKVAHK-----PQY-- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 984 lFDML------TVEEhiwfyaCLKGLSEKHVKVE-MEQMALDvglppSKLKSKTSQLSGG-MQRkLSVALAFVGGSKVVI 1055
Cdd:COG1245 169 -VDLIpkvfkgTVRE------LLEKVDERGKLDElAEKLGLE-----NILDRDISELSGGeLQR-VAIAAALLRDADFYF 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 507682765 1056 LDEPTAGVDPYSR----RGIWELLlkyRQGRTIILSTHHMDEADILGDRIAII 1104
Cdd:COG1245 236 FDEPSSYLDIYQRlnvaRLIRELA---EEGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
898-1107 |
7.66e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 47.53 E-value: 7.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 898 GVSIQNLVKVYrDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIrSEMSTIRQNLGV 977
Cdd:PRK11650 3 GLKLQAVRKSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVV-NELEPADRDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 CPQHNVLFDMLTVEEHIwFYAcLK--GLSEKHVKVEMEQMALDVGLPPSkLKSKTSQLSGGmQRKlSVAL--AFVGGSKV 1053
Cdd:PRK11650 81 VFQNYALYPHMSVRENM-AYG-LKirGMPKAEIEERVAEAARILELEPL-LDRKPRELSGG-QRQ-RVAMgrAIVREPAV 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 507682765 1054 VILDEPTAGVDPYSR---RgiWELL-LKYRQGRTIILSTHHMDEADILGDRIAIISHG 1107
Cdd:PRK11650 156 FLFDEPLSNLDAKLRvqmR--LEIQrLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGG 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
1944-2128 |
1.31e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 46.79 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1944 LLGVNGAGKSSTFKMLTGDTTVTRGNAFLNkNSILSNIHE-----VHQ-NMGYC-------------------------P 1992
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLN-GRVLFDAEKgiclpPEKrRIGYVfqdarlfphykvrgnlrygmaksmvA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1993 QFDAITELLtGREHveffallrgvpekevgkvgewairklgLLKygeKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPT 2072
Cdd:PRK11144 108 QFDKIVALL-GIEP---------------------------LLD---RYPGSLSGGEKQRVAIGRALLTAPELLLMDEPL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2073 TGMD-PKARRFL-WNCALSiiKEGRSVVL-TSHSMEECEALCTRMAIMVNGKFRCLGSV 2128
Cdd:PRK11144 157 ASLDlPRKRELLpYLERLA--REINIPILyVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
916-1109 |
1.84e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 46.71 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 916 VDGLALNFYEGQITSFLGHNGAGKT-TTMSILT---GLFppTSGTAYILGKDIRseMSTI--------------RQNLGV 977
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGrsyGRN--ISGTVFKDGKEVD--VSTVsdaidaglayvtedRKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 978 cpqhnVLFDmlTVEEHIWFyACLKGLSEKHVKVEMEQMALDVGLPpSKLKSKTS-------QLSGGMQRKlsVALA---F 1047
Cdd:NF040905 352 -----NLID--DIKRNITL-ANLGKVSRRGVIDENEEIKVAEEYR-KKMNIKTPsvfqkvgNLSGGNQQK--VVLSkwlF 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 1048 VGgSKVVILDEPTAGVDPYSRRGIWELLLKY-RQGRTIILSTHHMDEadILG--DRIAIISHGKL 1109
Cdd:NF040905 421 TD-PDVLILDEPTRGIDVGAKYEIYTIINELaAEGKGVIVISSELPE--LLGmcDRIYVMNEGRI 482
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1936-2121 |
2.03e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 45.29 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTV-----TRGNAFLNKNSILS-NIHEVHQNMGYCPQFDAITELLTGREHVEF 2009
Cdd:PRK14247 26 IPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNPIPNLSIFENVAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2010 -FALLRGVPEK-EVGKVGEWAIRKLGLLKYGEKY----AGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL 2083
Cdd:PRK14247 106 gLKLNRLVKSKkELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAKI 185
|
170 180 190
....*....|....*....|....*....|....*...
gi 507682765 2084 WNCALSIIKEgRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK14247 186 ESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQ 222
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
899-1064 |
2.17e-04 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTttmSILTGLF---PPTSGTAYILGKDI-RSEMSTIRQN 974
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKS---SLTLGLFrinESAEGEIIIDGLNIaKIGLHDLRFK 1361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 975 LGVCPQHNVLF--------DMLT--VEEHIWFyaclkglsekhvKVEMEQMALDVGLPPSKLKSKTSQ----LSGGMQRK 1040
Cdd:TIGR00957 1362 ITIIPQDPVLFsgslrmnlDPFSqySDEEVWW------------ALELAHLKTFVSALPDKLDHECAEggenLSVGQRQL 1429
|
170 180
....*....|....*....|....
gi 507682765 1041 LSVALAFVGGSKVVILDEPTAGVD 1064
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVD 1453
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
1014-1101 |
2.37e-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: 44.94 E-value: 2.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1014 QMALDVGLPPSKLKSKTSQLSGG-MQRklsVALAFVGGSKVV----ILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILS 1087
Cdd:cd03270 119 GFLVDVGLGYLTLSRSAPTLSGGeAQR---IRLATQIGSGLTgvlyVLDEPSIGLHPRDNDRLIETLKRLRdLGNTVLVV 195
|
90
....*....|....*
gi 507682765 1088 THhmDEADIL-GDRI 1101
Cdd:cd03270 196 EH--DEDTIRaADHV 208
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1912-2102 |
2.74e-04 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 46.25 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1912 LEIKELTKIYRRKrKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILSNIHEV-HQNMGY 1990
Cdd:PRK10790 341 IDIDNVSFAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1991 CPQ---------FDAITellTGR-----------EHVEFFALLRGVPEKEVGKVGEwairklgllkygekYAGNYSGGNK 2050
Cdd:PRK10790 420 VQQdpvvladtfLANVT---LGRdiseeqvwqalETVQLAELARSLPDGLYTPLGE--------------QGNNLSVGQK 482
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 507682765 2051 RKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNcALSIIKEGRSVVLTSH 2102
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSGTEQAIQQ-ALAAVREHTTLVVIAH 533
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
981-1092 |
2.77e-04 |
|
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: 44.91 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 981 HNVLfDMlTVEEHIWFYACLKGLSEKHvkvemeQMALDVGLPPSKLKSKTSQLSGG-MQR-KLSVALAF-VGGSKVVILD 1057
Cdd:cd03271 126 ADVL-DM-TVEEALEFFENIPKIARKL------QTLCDVGLGYIKLGQPATTLSGGeAQRiKLAKELSKrSTGKTLYILD 197
|
90 100 110
....*....|....*....|....*....|....*.
gi 507682765 1058 EPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHHMD 1092
Cdd:cd03271 198 EPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLD 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1905-2076 |
2.86e-04 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 45.49 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1905 GGGQNDILEIKELTKIY-------RRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKN 1975
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfGRTVGVvkAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1976 SILS-----------NIHEVHQNmgycPQ---------FDAITELLtgREHveffallRGVPEKEV-GKVGEwAIRKLGL 2034
Cdd:COG4608 81 DITGlsgrelrplrrRMQMVFQD----PYaslnprmtvGDIIAEPL--RIH-------GLASKAERrERVAE-LLELVGL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 507682765 2035 LK-YGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:COG4608 147 RPeHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
899-1106 |
2.86e-04 |
|
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: 43.68 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDGmKVAVDGLALNFYEGQ---ITsflGHNGAGKTTTMSILTGLFPPTSGTayilgkdirsemstirqnL 975
Cdd:cd03223 1 IELENLSLATPDG-RVLLKDLSFEIKPGDrllIT---GPSGTGKSSLFRALAGLWPWGSGR------------------I 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 976 GVCPQHNVLFdmltveehiwfyaclkglsekhvkveMEQMALdvgLPPSKLKSK-----TSQLSGGMQRKLSVALAFVGG 1050
Cdd:cd03223 59 GMPEGEDLLF--------------------------LPQRPY---LPLGTLREQliypwDDVLSGGEQQRLAFARLLLHK 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1051 SKVVILDEPTAGVDPYSRRGIWELLlkyRQGRTIILSTHHMDEADILGDRIAIISH 1106
Cdd:cd03223 110 PKFVFLDEATSALDEESEDRLYQLL---KELGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1936-2168 |
3.00e-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: 45.48 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNkNSILSNIHE-----VHQ-NMGYCPQfDAitEL---LTGREH 2006
Cdd:COG4148 22 LPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLG-GEVLQDSARgiflpPHRrRIGYVFQ-EA--RLfphLSVRGN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2007 VEFfALLRGVPEKEVGKVGEwAIRKLG---LLkygEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARR-- 2081
Cdd:COG4148 98 LLY-GRKRAPRAERRISFDE-VVELLGighLL---DRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAei 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2082 --FLwncaLSIIKEGR-SVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQHLKNRfgdgytivvriagsnPDLKPVQEF 2158
Cdd:COG4148 173 lpYL----ERLRDELDiPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR---------------PDLLPLAGG 233
|
250
....*....|
gi 507682765 2159 FGlafPGSVL 2168
Cdd:COG4148 234 EE---AGSVL 240
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
1936-2076 |
3.33e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKsSTF-KMLTGDTTVTRGnaflnknSILSNIhevhqNMGYCPQFdaitelLTGREHVEFFALLR 2014
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGK-TTFaKLLAGVLKPDEG-------EVDPEL-----KISYKPQY------IKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2015 GVPEK--------EVgkvgewaIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK13409 423 SITDDlgssyyksEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
1936-2076 |
3.36e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 45.93 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1936 IPRGECFGLLGVNGAGKsSTF-KMLTGDTTVTRGNafLNKNSILSnihevhqnmgYCPQFdaITELLTGRehVEFFalLR 2014
Cdd:COG1245 363 IREGEVLGIVGPNGIGK-TTFaKILAGVLKPDEGE--VDEDLKIS----------YKPQY--ISPDYDGT--VEEF--LR 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 2015 GVPEKEVGkvGEWA----IRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:COG1245 424 SANTDDFG--SSYYkteiIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1911-2121 |
3.87e-04 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 44.53 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIY-RRKrkpAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNA-FLNKNSILSNIHE----- 1983
Cdd:PRK11701 6 LLSVRGLTKLYgPRK---GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYAlseae 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1984 -----------VHQN--MGYCPQFDA---ITELL--TGREHvefFALLRGVPEKEVGKVgEWAIRKLGLLkygekyAGNY 2045
Cdd:PRK11701 83 rrrllrtewgfVHQHprDGLRMQVSAggnIGERLmaVGARH---YGDIRATAGDWLERV-EIDAARIDDL------PTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 2046 SGGNKRKLSTAMALIGGPPVVFLDEPTTGMD--PKARrfLWNCALSIIKE-GRSVVLTSHSMEECEALCTRMAIMVNGK 2121
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDvsVQAR--LLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
908-1114 |
3.89e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 45.93 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 908 YRDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKDIRSE-MSTIRQNLGVCPQHNVLFD 986
Cdd:PTZ00243 1318 YREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYgLRELRRQFSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 987 ---MLTVE-------EHIWFYACLKGLSEkHVKVEMEqmALDvglppSKLKSKTSQLSGGMQRKLSVALAFVG-GSKVVI 1055
Cdd:PTZ00243 1398 gtvRQNVDpfleassAEVWAALELVGLRE-RVASESE--GID-----SRVLEGGSNYSVGQRQLMCMARALLKkGSGFIL 1469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 507682765 1056 LDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILgDRIAIISHGKLCCVGS 1114
Cdd:PTZ00243 1470 MDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGS 1527
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1932-2104 |
4.77e-04 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 44.33 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1932 ICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGnaflnknsilSNIHEVHQNMGYCPQ---FDAITELLTGRehve 2008
Cdd:PRK09544 23 VSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG----------VIKRNGKLRIGYVPQklyLDTTLPLTVNR---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2009 FFALLRGVPEKEVGKvgewAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCAL 2088
Cdd:PRK09544 89 FLRLRPGTKKEDILP----ALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLID 164
|
170
....*....|....*..
gi 507682765 2089 SIIKE-GRSVVLTSHSM 2104
Cdd:PRK09544 165 QLRRElDCAVLMVSHDL 181
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
930-1109 |
5.06e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.24 E-value: 5.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 930 SFLGHNGAGKTTTMSILTGLFPPTSGTAYilgkdiRSemSTIRqnLGVCPQHNVLFDMLTVEEHIWFYACLKGLSEKHVK 1009
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF------RS--AKVR--MAVFSQHHVDGLDLSSNPLLYMMRCFPGVPEQKLR 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1010 VEMEQMALDVGLPPSKLKSktsqLSGGmqRKLSVALAFVGGSK--VVILDEPTAGVDPYSRRGIWELLLKYRQGrtIILS 1087
Cdd:PLN03073 609 AHLGSFGVTGNLALQPMYT----LSGG--QKSRVAFAKITFKKphILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMV 680
|
170 180
....*....|....*....|....
gi 507682765 1088 THhmDEADILG--DRIAIISHGKL 1109
Cdd:PLN03073 681 SH--DEHLISGsvDELWVVSEGKV 702
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
909-1109 |
5.20e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 909 RDGMKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTG---------LFP---------------PTSGTAYILGKDi 964
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNeisadggsyTFPgnwqlawvnqetpalPQPALEYVIDGD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 965 rSEMSTIRQNLGVCPQHNVLFDMLTVeehiwfYACLKGLSEKHVKVEMEQMALDVGLPPSKLKSKTSQLSGGMQRKLSVA 1044
Cdd:PRK10636 89 -REYRQLEAQLHDANERNDGHAIATI------HGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507682765 1045 LAFVGGSKVVILDEPTAGVDPYSRrgIW-ELLLKYRQGrTIILSTHHMDEADILGDRIAIISHGKL 1109
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAV--IWlEKWLKSYQG-TLILISHDRDFLDPIVDKIIHIEQQSL 224
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1911-2102 |
5.73e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 43.86 E-value: 5.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKiyRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG--DTTVTRGNAFLNKNSILSNIHEVHQNM 1988
Cdd:CHL00131 7 ILEIKNLHA--SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1989 GYCPQFDAITElLTGREHVEFFAL-------LRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNY-----SGGNKRK---L 2053
Cdd:CHL00131 85 GIFLAFQYPIE-IPGVSNADFLRLaynskrkFQGLPELDPLEFLEIINEKLKLVGMDPSFLSRNvnegfSGGEKKRneiL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 507682765 2054 StaMALIgGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:CHL00131 164 Q--MALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1911-2102 |
5.84e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1911 ILEIKELTKIYRRKRKP--AVDRICVGIPRGECFGLLGVNGAGKSSTFKML-------TGDTTVTRGNAFLNKNSILSNI 1981
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldkptSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1982 HEVHqnMGYCPQFDAITELLTGREHVEFFALLRGVPEKEVGKVGEWAIRKLGLLKYGEKYAGNYSGGNKRKLSTAMALIG 2061
Cdd:PRK10535 84 RREH--FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 2062 GPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1934-2103 |
6.31e-04 |
|
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: 42.70 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1934 VGIPRGECFGLLGVNGAGKSStfkmLTGDTTVTRGNAFLNKNSilsnihevhqnmgycPQFDaitelltgREHVEFFALL 2013
Cdd:cd03238 16 VSIPLNVLVVVTGVSGSGKST----LVNEGLYASGKARLISFL---------------PKFS--------RNKLIFIDQL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2014 rgvpeKEVGKVGewairkLGLLKYGEKyAGNYSGGNKRKLSTAMALIGGP-PVVF-LDEPTTGMDPKARRFLWNCALSII 2091
Cdd:cd03238 69 -----QFLIDVG------LGYLTLGQK-LSTLSGGELQRVKLASELFSEPpGTLFiLDEPSTGLHQQDINQLLEVIKGLI 136
|
170
....*....|..
gi 507682765 2092 KEGRSVVLTSHS 2103
Cdd:cd03238 137 DLGNTVILIEHN 148
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2017-2106 |
1.44e-03 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 42.72 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2017 PEKEVGKVGEWAIRKLGL---LKYG-EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFLWNCALSI-I 2091
Cdd:PRK14258 119 PKLEIDDIVESALKDADLwdeIKHKiHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrL 198
|
90
....*....|....*
gi 507682765 2092 KEGRSVVLTSHSMEE 2106
Cdd:PRK14258 199 RSELTMVIVSHNLHQ 213
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
921-1107 |
1.53e-03 |
|
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: 44.13 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 921 LNFY--EGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKdirsemstirqnLGVCPQHNVLFDMlTVEEHIWFya 998
Cdd:TIGR01271 445 ISFKleKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------------ISFSPQTSWIMPG-TIKDNIIF-- 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 999 clkGLSEKHVK----VEMEQMALDVGLPPSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRG 1070
Cdd:TIGR01271 510 ---GLSYDEYRytsvIKACQLEEDIALFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 507682765 1071 IWE-LLLKYRQGRTIILST---HHMDEAdilgDRIAIISHG 1107
Cdd:TIGR01271 587 IFEsCLCKLMSNKTRILVTsklEHLKKA----DKILLLHEG 623
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
899-1116 |
2.18e-03 |
|
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: 43.25 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 899 VSIQNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGL--FPPTSGTA-YILG---KDIRSEM-STI 971
Cdd:TIGR03269 1 IEVKNLTKKFDG--KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiYHVAlceKCGYVERpSKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 972 RQNLGVCPQHNVLFD--------------------ML----------TVEEHIwfyacLKGLSEKHVKVEME-QMALDVg 1020
Cdd:TIGR03269 79 GEPCPVCGGTLEPEEvdfwnlsdklrrrirkriaiMLqrtfalygddTVLDNV-----LEALEEIGYEGKEAvGRAVDL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1021 LPPSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLK--YRQGRTIILSTHHMDEA 1094
Cdd:TIGR03269 153 IEMVQLSHRITHiardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEavKASGISMVLTSHWPEVI 232
|
250 260
....*....|....*....|..
gi 507682765 1095 DILGDRIAIISHGKLCCVGSSL 1116
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPD 254
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
1888-2076 |
2.49e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.80 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1888 LNDEDEDVRRERQRILDGGGQ---NDILEIKELTKIYRrkrkpavDRICV-----GIPRGECFGLLGVNGAGKSSTFKML 1959
Cdd:PRK11819 298 LLSEEYQKRNETNEIFIPPGPrlgDKVIEAENLSKSFG-------DRLLIddlsfSLPPGGIVGIIGPNGAGKSTLFKMI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1960 TG----DT-TVTRGNAflnknsilsniheVHqnMGYCPQFdaitelltgREHVEffallrgvPEKEVGKV--GEWAIRKL 2032
Cdd:PRK11819 371 TGqeqpDSgTIKIGET-------------VK--LAYVDQS---------RDALD--------PNKTVWEEisGGLDIIKV 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2033 GllKY--------------G---EKYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMD 2076
Cdd:PRK11819 419 G--NReipsrayvgrfnfkGgdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
1015-1107 |
2.97e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1015 MALDVGLPPSKLKSKTSQLSGGMQRKlsVALAFVGGSKVV----ILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTH 1089
Cdd:PRK00635 459 ILIDLGLPYLTPERALATLSGGEQER--TALAKHLGAELIgityILDEPSIGLHPQDTHKLINVIKKLRdQGNTVLLVEH 536
|
90
....*....|....*....
gi 507682765 1090 hmDEADI-LGDRIAIISHG 1107
Cdd:PRK00635 537 --DEQMIsLADRIIDIGPG 553
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1939-2142 |
3.67e-03 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 42.40 E-value: 3.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1939 GECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKNSILS-NIHEVHQNMGYCPQfdaiTELLTGREHVEFFAL-LRGV 2016
Cdd:TIGR00958 507 GEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQ----EPVLFSGSVRENIAYgLTDT 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2017 PEKEVGKVGEWAIRKLGLLKYGEKY------AGNY-SGGNKRKLSTAMALIGGPPVVFLDEPTTGMDPKARRFL--WNCA 2087
Cdd:TIGR00958 583 PDEEIMAAAKAANAHDFIMEFPNGYdtevgeKGSQlSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLqeSRSR 662
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 507682765 2088 lsiikEGRSVVLTSHSMEECEAlCTRMAIMVNGKFRCLGSVQHLKNRFGDGYTIV 2142
Cdd:TIGR00958 663 -----ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
1014-1099 |
4.06e-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: 40.38 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1014 QMALDVGLPPSKLKSKTSQLSGG-MQR-KLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYR-QGRTIILSTHH 1090
Cdd:cd03238 69 QFLIDVGLGYLTLGQKLSTLSGGeLQRvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHN 148
|
90
....*....|..
gi 507682765 1091 ---MDEADILGD 1099
Cdd:cd03238 149 ldvLSSADWIID 160
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
1921-2102 |
4.39e-03 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 41.10 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1921 YRRKRKPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG--------DTTVTRGNAFLNKNSILSNIhevhqnmGYCP 1992
Cdd:COG2401 38 LRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGalkgtpvaGCVDVPDNQFGREASLIDAI-------GRKG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1993 QFDAITELLTGREHVEFFALLRGVPEkevgkvgewairklglLKYGEKYagnysggnkrKLSTAMALIGGPPVVFLDEPT 2072
Cdd:COG2401 111 DFKDAVELLNAVGLSDAVLWLRRFKE----------------LSTGQKF----------RFRLALLLAERPKLLVIDEFC 164
|
170 180 190
....*....|....*....|....*....|.
gi 507682765 2073 TGMDPK-ARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:COG2401 165 SHLDRQtAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2040-2140 |
4.82e-03 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 42.00 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2040 KYAGNYSGGNKRKLSTAMALIGGPPVVFLDEPTTGMDpkarRFLWNCALSIIKE-----GRSVVLTSHSMEECEALCTRM 2114
Cdd:PRK15134 421 RYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQV 496
|
90 100
....*....|....*....|....*.
gi 507682765 2115 AIMVNGKFRCLGSVQHLKNRFGDGYT 2140
Cdd:PRK15134 497 IVLRQGEVVEQGDCERVFAAPQQEYT 522
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2046-2102 |
4.85e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 40.04 E-value: 4.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507682765 2046 SGGNKRKLSTAMAL----IGGPPVVFLDEPTTGMDPKARRFLWNCALSIIKEGRSVVLTSH 2102
Cdd:cd03227 79 SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
919-1107 |
4.93e-03 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 41.38 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 919 LALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTAYILGKdirsemstirqnLGVCPQHNVLFDMlTVEEHIWFYA 998
Cdd:cd03291 56 INLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR------------ISFSSQFSWIMPG-TIKENIIFGV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 999 CLKGLSEKHVkVEMEQMALDVGLPPSKLKSKTSQ----LSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWE- 1073
Cdd:cd03291 123 SYDEYRYKSV-VKACQLEEDITKFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFEs 201
|
170 180 190
....*....|....*....|....*....|....
gi 507682765 1074 LLLKYRQGRTIILSTHHMDEADIlGDRIAIISHG 1107
Cdd:cd03291 202 CVCKLMANKTRILVTSKMEHLKK-ADKILILHEG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
902-1060 |
7.93e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 41.26 E-value: 7.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 902 QNLVKVYRDgmKVAVDGLALNFYEGQITSFLGHNGAGKTTTMSILTGLFPPTSGTaYILGKDIRseMSTIRQNlgvcpqH 981
Cdd:PRK11819 328 ENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKIGETVK--LAYVDQS------R 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 982 NVLFDMLTVEEHIwfyacLKGLSEKHV-KVEMeqmaldvglpPSKL------------KSKTSQLSGGMQRKLSVALAFV 1048
Cdd:PRK11819 397 DALDPNKTVWEEI-----SGGLDIIKVgNREI----------PSRAyvgrfnfkggdqQKKVGVLSGGERNRLHLAKTLK 461
|
170
....*....|..
gi 507682765 1049 GGSKVVILDEPT 1060
Cdd:PRK11819 462 QGGNVLLLDEPT 473
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1019-1108 |
8.24e-03 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 40.94 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1019 VGLPPSK--LKSKTSQLSGGMQRKLSVALAFVGGSKVVILDEPTAGVDPYSRRGIWELLLKYRQ--GRTIILSTHHMDEA 1094
Cdd:PRK15093 143 VGIKDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQML 222
|
90
....*....|....
gi 507682765 1095 DILGDRIAIISHGK 1108
Cdd:PRK15093 223 SQWADKINVLYCGQ 236
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1928-2134 |
8.59e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 40.66 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1928 AVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTG----DTTVTRGNAFLNKNSIL------------SNIHEVHQNMGYC 1991
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGitkdNWHVTADRFRWNGIDLLklsprerrkiigREIAMIFQEPSSC 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1992 pqFDAITELltGREhveffaLLRGVPEKEVGkvGEW----------AIR---KLGLlKYGEKYAGNY----SGGNKRKLS 2054
Cdd:COG4170 102 --LDPSAKI--GDQ------LIEAIPSWTFK--GKWwqrfkwrkkrAIEllhRVGI-KDHKDIMNSYphelTEGECQKVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 2055 TAMALIGGPPVVFLDEPTTGMDPKAR----RFLwnCALSIIKeGRSVVLTSHSMEECEALCTRMAIMVNGKFRCLGSVQH 2130
Cdd:COG4170 169 IAMAIANQPRLLIADEPTNAMESTTQaqifRLL--ARLNQLQ-GTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 507682765 2131 LKNR 2134
Cdd:COG4170 246 ILKS 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1032-1106 |
8.70e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.29 E-value: 8.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507682765 1032 QLSGG--MQRKLSVALAFV---GGSKV-VILDEPTAGVDPYSRRGIWELLLKYRQGRTIILSTHHMDEADILGDRIAIIS 1105
Cdd:COG4717 558 ELSRGtrEQLYLALRLALAellAGEPLpLILDDAFVNFDDERLRAALELLAELAKGRQVIYFTCHEELVELFQEEGAHVI 637
|
.
gi 507682765 1106 H 1106
Cdd:COG4717 638 E 638
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1926-1975 |
9.24e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 9.24e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 507682765 1926 KPAVDRICVGIPRGECFGLLGVNGAGKSSTFKMLTGDTTVTRGNAFLNKN 1975
Cdd:PRK15064 14 KPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDPN 63
|
|
| |
