|
Name |
Accession |
Description |
Interval |
E-value |
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-2368 |
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: 1570.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1 MGFLHQLQLLLWKNVTLKRRSPWVLAFEIFIPLVLFFILLGLRQKKPTISVKEVSFYTAApLTSAGILPVMQSL-C---- 75
Cdd:TIGR01257 1 MGFLRQIQLLLWKNWTLRKRQKIRFVVELVWPLSLFLVLIWLRNANPLYSQHECHFPNKA-MPSAGMLPWLQGIfCnvnn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 76 PDGQRDEFG-----FLQYANStvtqLLERLDRVVEEGNLFDPARPSLG---SELEALRQHLEALSagpgtsgSHLDRSTV 147
Cdd:TIGR01257 80 PCFQSPTPGespgiVSNYNNS----ILARVYRDFQELLMDAPESQHLGqvwAELRTLSQFMDTLR-------THPERIAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 148 SSFSLDSVARNPQELWRFLTQNLSLPNSTAQALLAARVDPPEVYHLLfgPSSALDSqsglhkgqepwsrlggnplfrmee 227
Cdd:TIGR01257 149 RGIRIRDILKDEEALTLFLMKNIGLSDSVVYLLVNSQVRPEQFAYGV--PDLELKD------------------------ 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 228 lllapalleqLTCTpgSGELGRILTVPesQKGALQGYRDAVCSGQAAArarrFSGLSAELRNQLDVAKVSQQLgldaPNG 307
Cdd:TIGR01257 203 ----------IACS--EALLERFIIFS--QRRGAQTVRDALCSLSQGT----LQWIEDTLYANVDFFKLFHVL----PTL 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 308 SDSSPQAPPPRRLQALLGDLLD-AQKVLQDVDVLSALALLLPqgactgrtpgppasgaggaangtgagavmgpnaTAEEG 386
Cdd:TIGR01257 261 LDSRSQGINLRSWGGILSDMSPrIQEFIHRPSVQDLLWVTRP---------------------------------LLQNG 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 387 APSAaalatpdtlqgqcsaFVQLWAGLQPILCGnnrtiEPEAlrrGNMSSLGFTSKEQRN----LGL------------- 449
Cdd:TIGR01257 308 GPET---------------FTQLMGILSDLLCG-----YPEG---GGSRVFSFNWYEDNNykafLGIdstrkdpiysydk 364
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 450 --------LVHLMTSNP---------------KILYAPAGSEVDRVILKANETFAFVGNVTHYAQVWLNISAEIRSFLEQ 506
Cdd:TIGR01257 365 rttsfcnaLIQSLESNPltkiawraakpllmgKILFTPDSPAARRILKNANSTFEELERVRKLVKAWEEVGPQIWYFFDK 444
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 507 GRLQQHLR----------WLQQYVAELRLHPEALNLSLDELPPALRQD---NFSLPSGMALLQQLDTIDNaacgwiQFMS 573
Cdd:TIGR01257 445 STQMTMIRdtlqnptvkdFINRQLGEEGITAEAVLNFLYNGPREKQADdmtNFDWRDIFNITDRFLRLAN------QYLE 518
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 574 KVSVDIFKGFPDEESIVNYTLNQAYQDNVtvFASVIFQTRK--DGSLPPHVHYKIRQNSSFTEKTNEIRRAYWRPGPNTG 651
Cdd:TIGR01257 519 CLVLDKFESYDDEVQLTQRALSLLEENRF--WAGVVFPDMYpwTSSLPPHVKYKIRMDIDVVEKTNKIKDRYWDSGPRAD 596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 652 GRFYFLY---GFVWIQDMMERAIIDTFVGHDVvEPGSYVQMFPYPCYTRDDFLFVIEHMMPLCMVISWVYSVAMTIQHIV 728
Cdd:TIGR01257 597 PVEDFRYiwgGFAYLQDMVEQGITRSQMQAEP-PVGIYLQQMPYPCFVDDSFMIILNRCFPIFMVLAWIYSVSMTVKSIV 675
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 729 AEKEHRLKEVMKTMGLNNAVHWVAWFITGFVQLSISVTALTAILKYGQVLMHSHVVIIWLFLAVYAVATIMFCFLVSVLY 808
Cdd:TIGR01257 676 LEKELRLKETLKNQGVSNAVIWCTWFLDSFSIMSMSIFLLTIFIMHGRILHYSDPFILFLFLLAFSTATIMQCFLLSTFF 755
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 809 SKAKLASACGGIIYFLSYVPYMYVAIREevahDKITAFEKCIASLMSTTAFGLGSKYFALYEVAGVGIQWHTFSQSPVEG 888
Cdd:TIGR01257 756 SKASLAAACSGVIYFTLYLPHILCFAWQ----DRMTADLKTAVSLLSPVAFGFGTEYLVRFEEQGLGLQWSNIGNSPLEG 831
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 889 DDFNLLLAVTMLMVDAVVYGILTWYIEAVHPGMYGLPRPWYFPLQKSYWLG----SGRTEawewswpwartprlSVMEED 964
Cdd:TIGR01257 832 DEFSFLLSMKMMLLDAALYGLLAWYLDQVFPGDYGTPLPWYFLLQESYWLGgegcSTREE--------------RALEKT 897
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 965 QACAMESRRFEETRGMEE---EPTHLPLV--VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILT 1039
Cdd:TIGR01257 898 EPLTEEMEDPEHPEGINDsffERELPGLVpgVCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILT 977
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1040 GLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHS 1119
Cdd:TIGR01257 978 GLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNE 1057
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1120 LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:TIGR01257 1058 EAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGR 1137
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1200 LKCCGSPLFLKGTYGDGYRLTLVKR----PAEPGGPQ------EPGLASSPPGRAPLSSCSEL------QVSQFIRKHVA 1263
Cdd:TIGR01257 1138 LYCSGTPLFLKNCFGTGFYLTLVRKmkniQSQRGGCEgtcsctSKGFSTRCPARVDEITPEQVldgdvnELMDLVYHHVP 1217
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1264 SCLLVSDTSTELSYILPSEAAKKGAFERLFQHLERSLDALHLSSFGLMDTTLEEVFLKVSEEDQSLENSEADVKESRKDV 1343
Cdd:TIGR01257 1218 EAKLVECIGQELIFLLPNKNFKQRAYASLFRELEETLADLGLSSFGISDTPLEEIFLKVTEDADSGSLFAGGAQQKRENA 1297
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1344 lpGAEGPASGEghagnlarcseltqsqaslqsassvgsargDEGAGYTdvygdyrplfdnPQDPDNVSLQEVEAE----- 1418
Cdd:TIGR01257 1298 --NLRHPCSGP------------------------------TEKAGQT------------PQASHTCSPGQPAAHpegqp 1333
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1419 ALSRVGQGSRKLDGGWLKVRQFHGLLVKRFHCARRNSKALFSQILLPAFFVCVAMTVALSVPEIGDLPPLVLSPSQY-HN 1497
Cdd:TIGR01257 1334 PPEPEDPGVPLNTGARLILQHVQALLVKRFQHTIRSHKDFLAQIVLPATFVFLALMLSIIIPPFGEYPALTLHPWMYgQQ 1413
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1498 YTqprgnfipyaneerreyrlRLSPDASPQQLVSTFrlpsgvgATCVLKSPAngslgptlnlssgesrllaarfFDSMCL 1577
Cdd:TIGR01257 1414 YT-------------------FFSMDEPNSEHLEVL-------ADVLLNKPG----------------------FGNRCL 1445
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1578 -ESFTQGLPLSNfvppppspapsdspaspdedLQAWNVslpPTAGPEM--------WTSAPSLPRlvrepVRCTCSAQGT 1648
Cdd:TIGR01257 1446 kEEWLPEYPCGN--------------------STPWKT---PSVSPNIthlfqkqkWTAAHPSPS-----CRCSTREKLT 1497
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1649 GF-SCPSSVGGHPPQMRVV-TGDILTDITGHNVSEYLLFT---------SDRFRLH--RYGAITFGNVLKSIPAS----- 1710
Cdd:TIGR01257 1498 MLpECPEGAGGLPPPQRTQrSTEILQDLTDRNISDFLVKTypalirsslKSKFWVNeqRYGGISIGGKLPAIPITgealv 1577
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1711 ---------FGTRAPPMVRKIAVRRAA-----------QVFYNNKGYHSMPTYLNSLNNAILRANLPKSKgNPAAYGITV 1770
Cdd:TIGR01257 1578 gflsdlgqmMNVSGGPVTREASKEMPDflkhletedniKVWFNNKGWHALVSFLNVAHNAILRASLPKDR-DPEEYGITV 1656
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1771 TNHPMNKTSASLS-LDYLLQGTDVVIAIFIIVAMSFVPASFVVFLVAEKSTKAKHLQFVSGCNPIIYWLANYVWDMLNYL 1849
Cdd:TIGR01257 1657 ISQPLNLTKEQLSeITVLTTSVDAVVAICVIFAMSFVPASFVLYLIQERVNKAKHLQFISGVSPTTYWLTNFLWDIMNYA 1736
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1850 VPATCCVIILFVFDLPAYTSPTNFPAVLSLFLLYGWSITPIMYPASFWFEVPSSAYVFLIVINLFIGITATVATFLLQLF 1929
Cdd:TIGR01257 1737 VSAGLVVGIFIGFQKKAYTSPENLPALVALLMLYGWAVIPMMYPASFLFDVPSTAYVALSCANLFIGINSSAITFVLELF 1816
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1930 EHDKDLKVVNSYLKSCFLIFPNYNLGHGLMEMAYNEYINEYYAKIGQfDKMKSPFEWDIVTRGLVAMAVEGVVGFLLTIM 2009
Cdd:TIGR01257 1817 ENNRTLLRFNAMLRKLLIVFPHFCLGRGLIDLALSQAVTDVYAQFGE-EHSANPFQWDLIGKNLVAMAVEGVVYFLLTLL 1895
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2010 CQYNF-----LRRPQRMPVstkpVEDDVDVASERQRVLRGDADNDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECF 2084
Cdd:TIGR01257 1896 IQHHFflsrwIAEPAKEPI----FDEDDDVAEERQRIISGGNKTDILRLNELTKVYSGTSSP---AVDRLCVGVRPGECF 1968
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2085 GLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEA 2164
Cdd:TIGR01257 1969 GLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIE 2048
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2165 RVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:TIGR01257 2049 KVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSH 2128
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2245 SMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQ-----SVKDVVRFFNRNFPEAMLKERHHTKVQY 2319
Cdd:TIGR01257 2129 SMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFGDGYIVTMKIKSPKddllpDLNPVEQFFQGNFPGSVQRERHYNMLQF 2208
|
2490 2500 2510 2520
....*....|....*....|....*....|....*....|....*....
gi 45446740 2320 QLKSEhiSLAQVFSKMEQVSGVLGIEDYSVSQTTLDNVFVNFAKKQSDN 2368
Cdd:TIGR01257 2209 QVSSS--SLARIFQLLISHKDSLLIEEYSVTQTTLDQVFVNFAKQQTET 2255
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2051-2274 |
5.45e-117 |
|
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: 369.53 E-value: 5.45e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:cd03263 1 LQIRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2274
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILE-VRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
991-1210 |
1.50e-113 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 359.51 E-value: 1.50e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1070
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1151 TAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1210
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
993-1206 |
5.72e-85 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.49 E-value: 5.72e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:COG1131 3 VRGLTKRYGD--KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1153 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1131 161 GLDPEARRELWELLRELAaEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2051-2277 |
9.62e-84 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 274.63 E-value: 9.62e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:COG1131 1 IEVRGLTKRY-----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:COG1131 76 GYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLIL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRF 2277
Cdd:COG1131 156 DEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
2058-2361 |
5.77e-68 |
|
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: 232.28 E-value: 5.77e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2058 KVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCD 2137
Cdd:TIGR01188 1 KVY-----GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2138 ALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2217
Cdd:TIGR01188 76 SVDEDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2218 DPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYmITVRTKSSQSVKDVV 2297
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDT-LESRPRDIQSLKVEV 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2298 RFFNRNFPEAMLkERHHTKVQYQLKSEHISLAQvfskmEQVSGVLG--------IEDYSVSQTTLDNVFVNF 2361
Cdd:TIGR01188 235 SMLIAELGETGL-GLLAVTVDSDRIKILVPDGD-----ETVPEIVEaairngirIRSISTERPSLDDVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2051-2274 |
3.14e-67 |
|
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: 226.87 E-value: 3.14e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:cd03265 1 IEVENLVKKY-----GDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03265 76 GIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLK 2274
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
993-1201 |
2.55e-66 |
|
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: 225.12 E-value: 2.55e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:COG4555 4 VENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:COG4555 162 GLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEALCDRVVILHKGKVV 211
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
998-1322 |
5.44e-66 |
|
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: 226.50 E-value: 5.44e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 998 KVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLF 1077
Cdd:TIGR01188 1 KVY--GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1158 ARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGDGyrlTLVKRPAEPggpqepgl 1236
Cdd:TIGR01188 159 TRRAIWDYIRALKeEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKD---TLESRPRDI-------- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1237 ASSPPGRAPLSscSELQVSQFIRKhvasCLLVSDTSTELSYILPSEAAKKgAFERLfqhlerSLDALHLSSFGLMDTTLE 1316
Cdd:TIGR01188 228 QSLKVEVSMLI--AELGETGLGLL----AVTVDSDRIKILVPDGDETVPE-IVEAA------IRNGIRIRSISTERPSLD 294
|
....*.
gi 45446740 1317 EVFLKV 1322
Cdd:TIGR01188 295 DVFLKL 300
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
993-1210 |
8.81e-66 |
|
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: 222.63 E-value: 8.81e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDkkLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:cd03265 3 VENLVKKYGDF--EAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLK 1210
Cdd:cd03265 161 GLDPQTRAHVWEYIekLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
993-1200 |
1.36e-65 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 219.96 E-value: 1.36e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:cd03230 3 VRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03230 81 EPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 1153 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03230 125 GLDPESRREFWELLRELkKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2051-2264 |
3.22e-63 |
|
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: 213.41 E-value: 3.22e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:cd03230 1 IEVRNLSKRYGKKT-----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03230 76 GYLPEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03230 120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2050-2279 |
8.82e-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: 209.33 E-value: 8.82e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2129
Cdd:COG4555 1 MIEVENLSKKYGKVP-----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2279
Cdd:COG4555 156 LDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGE 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
993-1204 |
1.88e-54 |
|
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: 189.71 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLyENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:cd03264 3 LENLTKRYG--KKRALDGVSLTL-GPGMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1153 GVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1204
Cdd:cd03264 160 GLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2050-2367 |
2.16e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.16 E-value: 2.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqVQQS 2129
Cdd:COG4152 1 MLELKGLTKRFGDKT-----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2208
Cdd:COG4152 73 IGYLPEERGLYPKMKVGEQLVYLARLKGLSKAEaKRRADEW-LERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2209 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTK 2288
Cdd:COG4152 152 ILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEAD 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2289 SSQSvkdvvrfFNRNFPEAMLKERHHTKVQYQLKSEHiSLAQVFSkmeQVSGVLGIEDYSVSQTTLDNVFVNFAKKQSD 2367
Cdd:COG4152 231 GDAG-------WLRALPGVTVVEEDGDGAELKLEDGA-DAQELLR---ALLARGPVREFEEVRPSLNEIFIEVVGEKAE 298
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
993-1326 |
2.67e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.16 E-value: 2.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1072
Cdd:COG4152 4 LKGLTKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD---PEDRRRIGYLPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:COG4152 79 ERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGdGYRLTLVKRPAEPGGP 1231
Cdd:COG4152 159 GLDPVNVELLKDVIRELAaKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLEADGDAGWLR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1232 QEPGLASsppgraplsscselqvsqfirkhvascllVSDTSTELSYILPSEAAKkgafERLFQHLersLDALHLSSFGLM 1311
Cdd:COG4152 238 ALPGVTV-----------------------------VEEDGDGAELKLEDGADA----QELLRAL---LARGPVREFEEV 281
|
330
....*....|....*
gi 45446740 1312 DTTLEEVFLKVSEED 1326
Cdd:COG4152 282 RPSLNEIFIEVVGEK 296
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2050-2268 |
5.41e-51 |
|
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: 180.26 E-value: 5.41e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2129
Cdd:cd03266 1 MITADALTKRFRDVK-KTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:cd03266 160 LDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2051-2265 |
5.65e-49 |
|
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: 173.94 E-value: 5.65e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQsL 2130
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-I 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDearvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03268 75 GALIEAPGFYPNLTARENLRLLARLLGIRKKR----IDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
993-1199 |
1.81e-48 |
|
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: 172.65 E-value: 1.81e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCP 1071
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTkLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03225 82 QNpDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEP 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1151 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd03225 162 TAGLDPAGRRELLELLKKLKaEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
993-1206 |
6.89e-48 |
|
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: 171.75 E-value: 6.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCP 1071
Cdd:COG1122 3 LENLSFSYPGGTP-ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QH--NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:COG1122 82 QNpdDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1150 PTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1122 161 PTAGLDPRGRRELLELLKRLnKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTP 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2051-2265 |
1.03e-47 |
|
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: 170.45 E-value: 1.03e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilAVDRLCLGVRPGeCFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:cd03264 1 LQLENLTKRYGKKR-----ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03264 75 GYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2211 DEPTTGMDPKAR-RFLwNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:cd03264 155 DEPTAGLDPEERiRFR-NLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2051-2268 |
9.99e-47 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 167.46 E-value: 9.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqVQQSL 2130
Cdd:cd03269 1 LEVENVTKRF-----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03269 73 GYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2051-2263 |
4.23e-46 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 169.22 E-value: 4.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSL 2130
Cdd:PRK13537 8 IDFRNVEKRY-----GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
996-1200 |
5.07e-46 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 165.47 E-value: 5.07e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1075
Cdd:cd03268 6 LTKTYG--KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY-QKNIEALRRIGALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:cd03268 83 FYPNLTARENLRLLARLLGIRKKRI----DEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1156 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03268 159 PDGIKELRELILSLrDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
993-1200 |
7.54e-46 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 165.23 E-value: 7.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC 1070
Cdd:cd03266 4 ADALTKRFRDVKKtvQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03266 84 SDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1151 TAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03266 164 TTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2050-2244 |
5.53e-45 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 162.26 E-value: 5.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2129
Cdd:COG4133 2 MLEAENLSCRRGERLL-----FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEArvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:COG4133 77 LAYLGHADGLKPELTVRENLRFWAALYGLRADREA--IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
|
170 180 190
....*....|....*....|....*....|....*
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:COG4133 155 LDEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
993-1199 |
1.73e-44 |
|
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: 161.29 E-value: 1.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemDEIRKNLGMCPQ 1072
Cdd:cd03269 3 VENVTKRFGR--VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD---IAARNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1153 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd03269 158 GLDPVNVELLKDVIRELArAGKTVILSTHQMELVEELCDRVLLLNKGR 205
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2050-2263 |
5.03e-43 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 161.54 E-value: 5.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIE--NLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQ 2127
Cdd:PRK13536 39 TVAIDlaGVSKSYGDKAV-----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLAR 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2207
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK13536 194 LILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
1008-1152 |
2.68e-42 |
|
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: 152.42 E-value: 2.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFDRLTVEEHL 1086
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSlRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1087 WFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
990-1206 |
6.21e-42 |
|
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: 154.75 E-value: 6.21e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRK 1065
Cdd:COG1127 5 MIEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1144
Cdd:COG1127 83 RIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKR--VALA-----RA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1145 IIL-------DEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1127 156 LALdpeillyDEPTAGLDPITSAVIDELIreLRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTP 226
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
993-1206 |
6.59e-42 |
|
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: 154.58 E-value: 6.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLG 1068
Cdd:cd03261 3 LRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglsEAELYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1069 MCPQHNVLFDRLTVEEHLWFYSRLKS-MAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAIIL 1147
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAFPLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKR--VALA-----RALAL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1148 -------DEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03261 154 dpelllyDEPTAGLDPIASGVIDDLIRSLKkeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTP 221
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
993-1200 |
2.77e-40 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 149.21 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1072
Cdd:cd03259 3 LKGLSKTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03259 160 ALDAKLREELREELKELqrELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
993-1196 |
1.06e-39 |
|
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: 147.62 E-value: 1.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirTEMDEIRKNLGMC 1070
Cdd:cd03293 3 VRNVSKTYggGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03293 79 FQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEP 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1151 TAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIIS 1196
Cdd:cd03293 159 FSALDALTREQLQEELLDiwRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
993-1206 |
1.38e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 150.34 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:PRK13537 10 FRNVEKRYGD--KLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1153 GVDPYARRAIWD-LILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13537 168 GLDPQARHLMWErLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAP 222
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2051-2269 |
3.80e-39 |
|
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: 146.53 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELL--QVQQ 2128
Cdd:cd03218 1 LRAENLSKRYGKRKV-----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhkRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2208
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2209 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGT 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
996-1206 |
9.63e-39 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 149.21 E-value: 9.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNV 1075
Cdd:PRK13536 47 VSKSYGD--KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQFDN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK13536 125 LDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1156 PYARRAIWD----LILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13536 205 PHARHLIWErlrsLLAR---GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRP 256
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
993-1206 |
2.52e-38 |
|
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: 144.34 E-value: 2.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDE-IRKNLGMC 1070
Cdd:TIGR04406 4 AENLIKSYK--KRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHlPMHErARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKErGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTP 219
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
993-1192 |
3.36e-38 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 143.00 E-value: 3.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:COG4133 5 AENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRRemDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:COG4133 83 ADGLKPELTVRENLRFWAALYGLRADREAI--DEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFT 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45446740 1153 GVDPYARRAIWDLILKYKP-GRTILLSTHhmDEADLLGDRI 1192
Cdd:COG4133 161 ALDAAGVALLAELIAAHLArGGAVLLTTH--QPLELAAARV 199
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2052-2275 |
8.00e-38 |
|
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: 142.96 E-value: 8.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQQS 2129
Cdd:cd03219 2 EVRGLTKRF-----GGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItgLPPHEIARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHL----QLYTRLRGISW---KDEARVVKWA---LEKLELTKYADKPAGTYSGGNKRKLSTAI 2199
Cdd:cd03219 77 IGRTFQIPRLFPELTVLENVmvaaQARTGSGLLLArarREEREARERAeelLERVGLADLADRPAGELSYGQQRRLEIAR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2200 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:cd03219 157 ALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
1007-1206 |
9.06e-38 |
|
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: 142.96 E-value: 9.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1084
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDItGLPPHEIaRLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 ------------HLWFYSRLKSMAqeEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03219 95 nvmvaaqartgsGLLLARARREER--EARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1153 GVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03219 173 GLNPEETEELAELIRELReRGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTP 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
993-1206 |
2.48e-37 |
|
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: 141.53 E-value: 2.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEiRKNLGMC- 1070
Cdd:cd03218 3 AENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMHK-RARLGIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 -PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:cd03218 80 lPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIkiLKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTP 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
992-1199 |
2.61e-37 |
|
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: 138.53 E-value: 2.61e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 992 CVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMC 1070
Cdd:cd00267 1 EIENLSFRYGGRT--ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLeELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQhnvlfdrltveehlwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd00267 79 PQ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1151 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd00267 108 TSGLDPASRERLLELLRELaEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
1728-2008 |
3.44e-37 |
|
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: 144.84 E-value: 3.44e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1728 AQVFYNNKGYHSMPTYLNSLNNaILRANLPKSKGNPAAYGITVTNHPMNKTSASLSLDYLLQgtdVVIAIFIIVAMSFVP 1807
Cdd:pfam12698 101 VTVYINSSNLLVSKLILNALQS-LLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAY---YLVGLILMIIILIGA 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1808 ASFVVFLVAEKSTKAKHLQFVSGCNPIIYWLANYVWDMLNYLVPATCCVIILFVFDLPaytsPTNFPAVLSLFLLYGWSI 1887
Cdd:pfam12698 177 AIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLFGIGIP----FGNLGLLLLLFLLYGLAY 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1888 TPIMYPASFWFEVPSSAYVFLIVINLFIGItATVATFLLQLFehdkdlkvvNSYLKSCFLIFPNYNLGHGLMEMAYNEYI 1967
Cdd:pfam12698 253 IALGYLLGSLFKNSEDAQSIIGIVILLLSG-FFGGLFPLEDP---------PSFLQWIFSIIPFFSPIDGLLRLIYGDSL 322
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 45446740 1968 NEyyakigqfdkmkspfewdiVTRGLVAMAVEGVVGFLLTI 2008
Cdd:pfam12698 323 WE-------------------IAPSLIILLLFAVVLLLLAL 344
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
985-1198 |
5.15e-37 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 141.38 E-value: 5.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 985 THLPLVVCVDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtemdE 1062
Cdd:COG1116 2 SAAAPALELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1063 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVVLSAR 215
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
993-1200 |
7.64e-37 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 139.55 E-value: 7.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYK--DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-K 1065
Cdd:cd03255 3 LKNLSKTYGggGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklsEKELAAFRrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKII 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:cd03255 163 LADEPTGNLDSETGKEVMELLRELnkEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2050-2357 |
1.83e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 141.76 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2113
Cdd:COG4586 1 IIEVENLSKTYRvyekepglkgalkglfRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2114 VNGHSVLK---ELL--------QVQQslgycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADK 2182
Cdd:COG4586 81 VLGYVPFKrrkEFArrigvvfgQRSQ----------LWWDLPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2183 PAgtysggnkRKLS--------TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALC 2253
Cdd:COG4586 151 PV--------RQLSlgqrmrceLAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALC 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2254 TRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRTKSSQSVKDVVRFfnrnfpeAMLKERHHTKVQYQLKSEhISLAQVFS 2333
Cdd:COG4586 223 DRVIVIDHGRIIYDGSLEELKERFGPYKTIVLELAEPVPPLELPRG-------GEVIEREGNRVRLEVDPR-ESLAEVLA 294
|
330 340
....*....|....*....|....
gi 45446740 2334 KmeqVSGVLGIEDYSVSQTTLDNV 2357
Cdd:COG4586 295 R---LLARYPVRDLTIEEPPIEEV 315
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
994-1206 |
3.43e-36 |
|
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: 138.59 E-value: 3.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 994 DKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMCP 1071
Cdd:cd03295 4 ENVTKRYGGGKK-AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIR-EQDpvELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIE--DLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:cd03295 82 QQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03295 162 PFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTP 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2051-2264 |
3.67e-36 |
|
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: 137.27 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQQSL 2130
Cdd:cd03259 1 LELKGLSKTY-----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-RRNI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03259 75 GMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03259 155 DEPLSALDAKLREELREELKELQReLGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2051-2271 |
5.40e-36 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 137.46 E-value: 5.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQS 2129
Cdd:COG1122 1 IELENLSFSYP----GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKnLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQcDA---LFDElTAREHLQLYTRLRGISwKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:COG1122 77 VGLVFQ-NPddqLFAP-TVEEDVAFGPENLGLP-REEIReRVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2271
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPR 219
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1007-1206 |
6.31e-36 |
|
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: 138.25 E-value: 6.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKnLGMCP--QHNVLFDRLTVE 1083
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDItGLPPHRIAR-LGIARtfQNPRLFPELTVL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 EHL-----------WFYS--RLKSMAQEE--IRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:COG0411 98 ENVlvaaharlgrgLLAAllRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1149 EPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG0411 178 EPAAGLNPEETEELAELIRRLRdeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
1007-1199 |
9.08e-36 |
|
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: 136.41 E-value: 9.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1084
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDItGLPPHERaRAGIGYVPEGRRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWFYSRLKsmAQEEIRREMDKMIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1163
Cdd:cd03224 95 NLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIF 172
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446740 1164 DLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd03224 173 EAIRELRDeGVTILLVEQNARFALEIADRAYVLERGR 209
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
993-1206 |
1.26e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 136.70 E-value: 1.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE--MDE-IRKNLGM 1069
Cdd:COG1137 6 AENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI-THlpMHKrARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMDEAdlLG--DRIAIISHGKLKCCGSP 1206
Cdd:COG1137 163 PFAGVDPIAVADIQKIIrhLKER-GIGVLITDHNVRET--LGicDRAYIISEGKVLAEGTP 220
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
991-1199 |
1.98e-35 |
|
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: 133.66 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1069
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQHNVLFDRlTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGK 1199
Cdd:cd03228 123 ATSALDPETEALILEALRALAKGKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
2052-2263 |
2.03e-35 |
|
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: 135.29 E-value: 2.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQSL 2130
Cdd:cd03225 1 ELKNLSFSYPDGAR---PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLsLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQ-------CDALFDELT-AREHLqlytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:cd03225 78 GLVFQnpddqffGPTVEEEVAfGLENL-------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
2050-2264 |
3.32e-35 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 135.54 E-value: 3.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQV--- 2126
Cdd:COG1137 3 TLEAENLVKSYGKRTV-----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMhkr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 -QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:COG1137 76 aRLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKV 214
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
993-1206 |
3.73e-35 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 135.94 E-value: 3.73e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMD--EIRKNLGMC 1070
Cdd:COG1120 4 AENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSrrELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEE--------HLWFYSRLKsmaqEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:COG1120 81 PQEPPAPFGLTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLrrLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPP 222
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2046-2272 |
1.65e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2046 ADNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ 2125
Cdd:COG1121 2 MMMPAIELENLTVSY-----GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VqqslGYCPQcDALFDE---LTAREHLQLYtRLRGISW------KDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLS 2196
Cdd:COG1121 77 I----GYVPQ-RAEVDWdfpITVRDVVLMG-RYGRRGLfrrpsrADREAVDE-ALERVGLEDLADRPIGELSGGQQQRVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2197 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLaIMVNGRLRCLGSIQH 2272
Cdd:COG1121 150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRV-LLLNRGLVAHGPPEE 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
990-1206 |
1.92e-34 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 140.81 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVY---KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE 1062
Cdd:COG1123 260 LLEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1063 IRKNLGMCPQH--NVLFDRLTVEEHLWF-YSRLKSMAQEEIRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAF 1138
Cdd:COG1123 340 LRRRVQMVFQDpySSLNPRMTVGDIIAEpLRLHGLLSRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1139 VGGSRAIILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQreLGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPT 489
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
980-1206 |
1.93e-34 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 133.68 E-value: 1.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 980 MEEEPthlplVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE 1059
Cdd:COG1121 1 MMMMP-----AIELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1060 mdeiRKNLGMCPQHnVLFDR---LTVEE--------HLWFYSRLKSmaqeEIRREMDKMIEDLELSNKRHSLVQTLSGGM 1128
Cdd:COG1121 74 ----RRRIGYVPQR-AEVDWdfpITVRDvvlmgrygRRGLFRRPSR----ADREAVDEALERVGLEDLADRPIGELSGGQ 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1129 KRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLkCCGSP 1206
Cdd:COG1121 145 QQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELrREGKTILVVTHDLGAVREYFDRVLLLNRGLV-AHGPP 222
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
993-1200 |
2.34e-34 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 132.63 E-value: 2.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1066
Cdd:cd03257 4 VKNLSVSFPTGGGSvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1067 LGMCPQH--NVLFDRLTVEEHLW--FYSRLKSMAQEEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAFVGG 1141
Cdd:cd03257 84 IQMVFQDpmSSLNPRMTIGEQIAepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARALALN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1142 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03257 164 PKLLIADEPTSALDVSVQAQILDLLkkLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
1023-1206 |
2.68e-34 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 144.11 E-value: 2.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1023 FLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRR 1102
Cdd:NF033858 297 FLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAA 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1103 EMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTH 1180
Cdd:NF033858 377 RVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLieLSREDGVTIFISTH 456
|
170 180
....*....|....*....|....*.
gi 45446740 1181 HMDEAdLLGDRIAIISHGKLKCCGSP 1206
Cdd:NF033858 457 FMNEA-ERCDRISLMHAGRVLASDTP 481
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
996-1201 |
4.43e-34 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 131.75 E-value: 4.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHD-IRTEMdeirKNLGMCPQHN 1074
Cdd:TIGR03740 6 LSKRFG--KQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPwTRKDL----HKIGSLIESP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VLFDRLTVEEHLWFYSRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:TIGR03740 80 PLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEPTNGL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1155 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:TIGR03740 156 DPIGIQELRELIRSFpEQGITVILSSHILSEVQQLADHIGIISEGVLG 203
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
2052-2263 |
7.26e-34 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 128.52 E-value: 7.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2130
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLT-----LKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCdalfdeltarehlqlytrlrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd00267 76 GYVPQL---------------------------------------------------SGGQRQRVALARALLLNPDLLLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:cd00267 105 DEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
993-1207 |
1.12e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 132.04 E-value: 1.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCP 1071
Cdd:PRK13632 10 VENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QH-NVLFDRLTVEEHLWFysrlkSMAQEEI-RREMDKMIEDL------ELSNKRHSlvQTLSGGMKRKlsVAIAFVGG-- 1141
Cdd:PRK13632 90 QNpDNQFIGATVEDDIAF-----GLENKKVpPKKMKDIIDDLakkvgmEDYLDKEP--QNLSGGQKQR--VAIASVLAln 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1142 SRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPL 1207
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMvdLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPK 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
990-1241 |
1.17e-33 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 138.50 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIR-K 1065
Cdd:COG1123 4 LLEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1144
Cdd:COG1123 84 RIGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1145 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLkgtYGDGYRLTLV 1222
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLreLQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI---LAAPQALAAV 240
|
250
....*....|....*....
gi 45446740 1223 KRPAEPGGPQEPGLASSPP 1241
Cdd:COG1123 241 PRLGAARGRAAPAAAAAEP 259
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
993-1200 |
1.70e-33 |
|
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: 130.39 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKN 1066
Cdd:cd03258 4 LKNVSKVFGDTGGKvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1067 LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAII 1146
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1147 LDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDInrELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2052-2275 |
2.65e-33 |
|
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: 130.09 E-value: 2.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLG 2131
Cdd:TIGR04406 3 VAENLIKSYKKRKV-----VNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2132 --YCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWAL-EKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2208
Cdd:TIGR04406 78 igYLPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALlEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2209 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVA 224
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
988-1200 |
3.82e-33 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 129.01 E-value: 3.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 988 PLVVCVDkLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMD 1061
Cdd:COG1136 3 PLLELRN-LTKSYGTGEGEvtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlserELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 EIR-KNLGMCPQ-HNvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1139
Cdd:COG1136 82 RLRrRHIGFVFQfFN-LLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1140 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELnrELGTTIVMVTHDPELAA-RADRVIRLRDGRI 222
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
993-1199 |
5.74e-33 |
|
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: 126.92 E-value: 5.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI---RKNLGM 1069
Cdd:cd03229 3 LKNVSKRYGQ--KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELpplRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQHNVLFDRLTVEEHLWFysrlksmaqeeirremdkmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:cd03229 81 VFQDFALFPHLTVLENIAL----------------------------------GLSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd03229 127 PTSALDPITRREVRALLksLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
990-1200 |
5.82e-33 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 128.63 E-value: 5.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKKlALNKLSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIR 1064
Cdd:COG2884 1 MIRFENVSKRYPGGRE-ALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1065 KNLGMCPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGG-MKRklsVAIAfvggs 1142
Cdd:COG2884 79 RRIGVVFQdFRLLPDR-TVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGeQQR---VAIA----- 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1143 RAI-------ILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG2884 150 RALvnrpellLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2050-2264 |
1.47e-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: 125.54 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQVQQ- 2128
Cdd:COG0411 4 LLEVRGLTKRF-----GGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 -SLG----YcpQCDALFDELTAREHLQL-------YTRLRGI-----SWKDEARVVKWA---LEKLELTKYADKPAGTYS 2188
Cdd:COG0411 77 aRLGiartF--QNPRLFPELTVLENVLVaaharlgRGLLAALlrlprARREEREARERAeelLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2189 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRV 231
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
981-1219 |
1.58e-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: 132.58 E-value: 1.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 981 EEEPTHLPLVVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-E 1059
Cdd:COG4987 324 EPAPAPGGPSLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1060 MDEIRKNLGMCPQHNVLFDRlTVEEHLwfysRL-KSMAQEEirrEMDKMIEDLELsnkrHSLVQ---------------T 1123
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLRENL----RLaRPDATDE---ELWAALERVGL----GDWLAalpdgldtwlgeggrR 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1124 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCC 1203
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLE-RMDRILVLEDGRIVEQ 550
|
250
....*....|....*.
gi 45446740 1204 GSPLFLKGTYGDGYRL 1219
Cdd:COG4987 551 GTHEELLAQNGRYRQL 566
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2052-2264 |
1.65e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 123.77 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2130
Cdd:COG4619 2 ELEGLSFRVGGKPI-----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAmPPPEWRRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDElTAREHLQLYTRLRGISWkDEARVVKWaLEKLELTK-YADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNLPFPFQLRERKF-DRERALEL-LERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAeEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
993-1198 |
2.69e-31 |
|
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: 123.41 E-value: 2.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdeiRKNLGMCPQ 1072
Cdd:cd03235 2 VEDLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 H-NVLFD-RLTVEE--------HLWFYSRLKsmaqEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:cd03235 76 RrSIDRDfPISVRDvvlmglygHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIA-----IISHG 1198
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRReGMTILVVTHDLGLVLEYFDRVLllnrtVVASG 213
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
1007-1200 |
2.75e-31 |
|
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: 123.98 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLG-MCPQHNVLFDRLTVEEH 1085
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGvVFGQKTQLWWDLPVIDS 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1086 LWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1165
Cdd:cd03267 116 FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNF 195
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446740 1166 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03267 196 LKEYnrERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2014-2273 |
2.93e-31 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 131.18 E-value: 2.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2014 FLRRPQRM---PVSTKPVEDDVDVASERQRVLRgdadndmvkIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVN 2090
Cdd:COG1123 230 ILAAPQALaavPRLGAARGRAAPAAAAAEPLLE---------VRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGES 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2091 GAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQVQQSLGYCPQcD---ALFDELTAREHLQLYTRLRGISWKDE 2163
Cdd:COG1123 301 GSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrRSLRELRRRVQMVFQ-DpysSLNPRMTVGDIIAEPLRLHGLLSRAE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2164 AR-VVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVV 2240
Cdd:COG1123 380 RReRVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLqRELGLTYL 459
|
250 260 270
....*....|....*....|....*....|...
gi 45446740 2241 LTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:COG1123 460 FISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
2052-2268 |
6.04e-31 |
|
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: 122.26 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVqqslG 2131
Cdd:cd03235 1 EVEDLTVSYGGHPV-----LEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKRI----G 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2132 YCPQ-CDALFD-ELTARE--HLQLYTRLRGISW--KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:cd03235 72 YVPQrRSIDRDfPISVRDvvLMGLYGHKGLFRRlsKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRlAIMVNGRLRCLG 2268
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
993-1199 |
6.76e-31 |
|
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: 123.06 E-value: 6.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLG 1068
Cdd:cd03256 3 VENLSKTYPNGKK-ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1069 MCPQHNVLFDRLTVEEH-----LWFYSRLKSMAQ----EEIRREMdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFV 1139
Cdd:cd03256 82 MIFQQFNLIERLSVLENvlsgrLGRRSTWRSLFGlfpkEEKQRAL-AALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1140 GGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
1000-1200 |
7.70e-31 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 121.85 E-value: 7.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGMCPQHNVLF 1077
Cdd:COG4619 8 FRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRlTVEEHL--WFYSRLKSMAQEEIRREMDKMIEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:COG4619 87 GG-TVRDNLpfPFQLRERKFDRERALELLERLGLPPDILDKP---VERLSGGERQRLALIRALLLQPDVLLLDEPTSALD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1156 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG4619 163 PENTRRVEELLREYlaEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2050-2269 |
8.95e-31 |
|
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: 123.23 E-value: 8.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ 2125
Cdd:COG1120 1 MLEAENLSVGYGGRPV-----LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLaslsRRELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VqqsLGYCPQ-CDALFDeLTARE--------HLQLYTRLRgiswKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLS 2196
Cdd:COG1120 76 R---IAYVPQePPAPFG-LTVRElvalgrypHLGLFGRPS----AEDREAVEEALERTGLEHLADRPVDELSGGERQRVL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2197 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:COG1120 148 IARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGP 221
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
993-1206 |
1.02e-30 |
|
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: 122.35 E-value: 1.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1072
Cdd:cd03300 3 LENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1153 GVDPYARRaiwDLILKYKP-----GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03300 160 ALDLKLRK---DMQLELKRlqkelGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTP 215
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
993-1274 |
1.03e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 125.20 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKK-------------------LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG 1053
Cdd:COG4586 4 VENLSKTYRVYEKepglkgalkglfrreyrevEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1054 HDIRTEMDEIRKNLGmcpqhnVLF--------DrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLS 1125
Cdd:COG4586 84 YVPFKRRKEFARRIG------VVFgqrsqlwwD-LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1126 GGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCC 1203
Cdd:COG4586 157 LGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnrERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1204 GSPLFLKGTYGDGYRLTLV-KRPAEPGGPQEPG-LASSPPGRAPLSSCSELQVSQFIRKhVASCLLVSDTSTE 1274
Cdd:COG4586 237 GSLEELKERFGPYKTIVLElAEPVPPLELPRGGeVIEREGNRVRLEVDPRESLAEVLAR-LLARYPVRDLTIE 308
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2051-2264 |
1.03e-30 |
|
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: 121.83 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQV 2126
Cdd:cd03255 1 IELKNLSKTYGGGGE-KVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlsekELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 -QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:cd03255 80 rRRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEcEALCTRLAIMVNGRL 2264
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKeAGTTIVVVTHDPEL-AEYADRIIELRDGKI 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2046-2275 |
1.62e-30 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 122.01 E-value: 1.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2046 ADNDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----K 2121
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVV-----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2122 ELLQVQQSLGYCPQCDALFDELTAREHLQL----YTRLRgiswKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLS 2196
Cdd:COG1127 76 ELYELRRRIGMLFQGGALFDSLTVFENVAFplreHTDLS----EAEIReLVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2197 TAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
1003-1204 |
1.72e-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: 119.85 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTeMD--EIRKNLGMCPQhnvlfdrl 1080
Cdd:cd03214 10 GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS-LSpkELARKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 tveehlwfysrlksmaqeeirremdkMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1161 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1204
Cdd:cd03214 135 ELLELLrrLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2050-2273 |
2.06e-30 |
|
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: 121.53 E-value: 2.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQ 2125
Cdd:cd03258 1 MIELKNVSKVFGDTG-GKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTllsgKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2200
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEiEERV----LELLELVGLEDK-ADAYpaqlSGGQKQRVGIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:cd03258 155 LANNPKVLLCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
2071-2215 |
3.46e-30 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 117.75 E-value: 3.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDELTAREHL 2149
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDdERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2150 QLYTRLRGISWKDEARVVKWALEKLELTKYADKPAG----TYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2215
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
993-1206 |
3.57e-30 |
|
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: 120.90 E-value: 3.57e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1072
Cdd:cd03299 3 VENLSKDWKEFK---LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1153 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03299 159 ALDVRTKEKLREELkkIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKP 214
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2052-2275 |
1.35e-29 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 118.69 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQS 2129
Cdd:cd03224 2 EVENLNAGY-----GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHerARAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGIswkdeaRVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRR------AKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:cd03224 151 PKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2051-2275 |
1.38e-29 |
|
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: 119.14 E-value: 1.38e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQV 2126
Cdd:cd03261 1 IELRGLTKSFGGRTV-----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQCDALFDELTAREHLQL----YTRLrgiswkDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAI 2199
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFplreHTRL------SEEEIREIVLEKLEavgLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2200 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
1001-1206 |
2.25e-29 |
|
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: 119.67 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIR-KNLGMCPQHNV 1075
Cdd:cd03294 33 KTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELRELRrKKISMVFQSFA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:cd03294 113 LLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1156 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03294 193 PLIRREMQDELLRLqaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTP 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
969-1206 |
3.08e-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: 125.64 E-value: 3.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 969 MESRRFEETRGMEEEPTHLPLVVCVDKLTKVYkDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1048
Cdd:COG4988 315 LDAPEPAAPAGTAPLPAAGPPSIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGS 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1049 ATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSRLKSmaQEEIRR-----EMDKMIEDLElsNKRHSLV- 1121
Cdd:COG4988 394 ILINGVDLSDlDPASWRRQIAWVPQNPYLFA-GTIRENLRLGRPDAS--DEELEAaleaaGLDEFVAALP--DGLDTPLg 468
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1122 ---QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHG 1198
Cdd:COG4988 469 eggRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLA-QADRILVLDDG 547
|
....*...
gi 45446740 1199 KLKCCGSP 1206
Cdd:COG4988 548 RIVEQGTH 555
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
993-1206 |
3.33e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 119.77 E-value: 3.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDD---KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKN 1066
Cdd:PRK13637 5 IENLTHIYMEGtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1067 LGMC---PQHNvLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN---KRHSLVQtLSGGMKRKLSVAIAFVG 1140
Cdd:PRK13637 85 VGLVfqyPEYQ-LFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYedyKDKSPFE-LSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIkeLHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2051-2259 |
3.35e-29 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 117.57 E-value: 3.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKELLQVQQSL 2130
Cdd:cd03293 1 LEVRNVSKTYGGGG-GAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIM 2259
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIWrETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2050-2281 |
5.41e-29 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 117.98 E-value: 5.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkellQVQQS 2129
Cdd:COG1124 1 MLEVRNLSVSYGQGG-RRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV-----TRRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDE--------LTAREHLQLYTRLRGISwKDEARVVKwALEKLELTK-YADKPAGTYSGGNKRKLSTAIA 2200
Cdd:COG1124 75 KAFRRRVQMVFQDpyaslhprHTVDRILAEPLRIHGLP-DREERIAE-LLEQVGLPPsFLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGD 2279
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLREeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
..
gi 45446740 2280 GY 2281
Cdd:COG1124 233 PY 234
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2051-2264 |
6.72e-29 |
|
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: 117.05 E-value: 6.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYK----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFV 2114
Cdd:cd03267 1 IEVSNLSKSYRvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2115 NGHSVLKELLQVQQSLGYC-PQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKR 2193
Cdd:cd03267 81 AGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNReRGTTVLLTSHYMKDIEALARRVLVIDKGRL 232
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
993-1201 |
7.17e-29 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 116.20 E-value: 7.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEmdEIRKNLGMCPQ 1072
Cdd:cd03226 2 IENISFSYKKGTEI-LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAK--ERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 ---HNVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKM-IEDLELsnkRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:cd03226 79 dvdYQLFTD--SVREELLLGLKELDAGNEQAETVLKDLdLYALKE---RHP--LSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1149 EPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
996-1200 |
8.99e-29 |
|
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: 116.51 E-value: 8.99e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP-----PTSGSATIYGHDIRTEMD---EIRKNL 1067
Cdd:cd03260 6 LNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVdvlELRRRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1068 GMCPQHNVLFdRLTVEEHLWFYSRLKSMAQeeiRREMDKMIEDL--------ELSNKRHSLvqTLSGGMKRKLSVAIAFV 1139
Cdd:cd03260 84 GMVFQKPNPF-PGSIYDNVAYGLRLHGIKL---KEELDERVEEAlrkaalwdEVKDRLHAL--GLSGGQQQRLCLARALA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1140 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03260 158 NEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
994-1219 |
1.20e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 116.53 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 994 DKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCP 1071
Cdd:PRK10895 7 KNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRGIGYLP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:PRK10895 85 QEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1151 TAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL------KGTY-GDGYRL 1219
Cdd:PRK10895 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEIlqdehvKRVYlGEDFRL 241
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
2050-2264 |
1.30e-28 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 116.07 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2129
Cdd:cd03257 1 LLEVKNLSVSFPTGG-GSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LG----YCPQcD---ALFDELTAREHLQLYTRLRGISWKDEA--RVVKWALEKLELTK-YADKPAGTYSGGNKRKLSTAI 2199
Cdd:cd03257 80 RRkeiqMVFQ-DpmsSLNPRMTIGEQIAEPLRIHGKLSKKEArkEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIAR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2200 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03257 159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1007-1199 |
1.79e-28 |
|
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: 115.85 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEI-RKNLGMCPQHNVLFDRLTVEE 1084
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItGLPPHRIaRLGIGYVPEGRRIFPSLTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HL--WFYSRlksMAQEEIRREMDKMIEdL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:COG0410 98 NLllGAYAR---RDRAEVRADLERVYE-LfpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45446740 1161 AIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:COG0410 174 EIFEIIrrLN-REGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1000-1206 |
1.22e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 114.80 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDK----KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD--EIRKNLGMCPQH 1073
Cdd:PRK13633 14 YESNEesteKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVFQN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 --NVLFDRLtVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSR--AIILDE 1149
Cdd:PRK13633 94 pdNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQR--VAIAGILAMRpeCIIFDE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIkeLNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTP 228
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
991-1200 |
1.60e-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: 121.48 E-value: 1.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGM 1069
Cdd:COG2274 474 IELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQHNVLFDRlTVEEHLWFYSRLKSMaqEEIRR-----EMDKMIEdlELSNKRHSLV----QTLSGGMKRKLSVAIAFVG 1140
Cdd:COG2274 554 VLQDVFLFSG-TIRENITLGDPDATD--EEIIEaarlaGLHDFIE--ALPMGYDTVVgeggSNLSGGQRQRLAIARALLR 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1200
Cdd:COG2274 629 NPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLA-DRIIVLDKGRI 687
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
2050-2263 |
1.94e-27 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 112.77 E-value: 1.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELlq 2125
Cdd:COG0410 3 MLEVENLHAGY-----GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGlpphRI-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGiswkdEARVVKWALEKL-----ELTKYADKPAGTYSGGNKRKLSTAIA 2200
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLLLGAYARR-----DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGR 213
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2048-2273 |
2.61e-27 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 118.85 E-value: 2.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKELL 2124
Cdd:COG1123 2 TPLLEVRDLSVRYPG---GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLELSE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQ-QSLGYCPQ-CDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:COG1123 79 ALRgRRIGMVFQdPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:COG1123 159 LDPDLLIADEPTTALDVTTQAEILDLLRELQReRGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2043-2263 |
2.71e-27 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 121.38 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2043 RGDADNDMVKIE--NLTkvyksRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL 2120
Cdd:NF033858 257 RPADDDDEPAIEarGLT-----MRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVD 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2121 KELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2200
Cdd:NF033858 332 AGDIATRRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVA 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEaLCTRLAIMVNGR 2263
Cdd:NF033858 412 VIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEAE-RCDRISLMHAGR 474
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
999-1184 |
3.03e-27 |
|
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: 112.87 E-value: 3.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 999 VYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-SATIYGHDI-RTEMDEIRKNLGMCpqHNVL 1076
Cdd:COG1119 11 VRRGGKTI-LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLV--SPAL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1077 FDRLTVEEHLW------FYSrlkSM-----AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:COG1119 88 QLRFPRDETVLdvvlsgFFD---SIglyrePTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDE 1184
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLdkLAAEGAPTLVLVTHHVEE 205
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
991-1200 |
6.27e-27 |
|
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: 110.81 E-value: 6.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1070
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDV-TDLPPKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1151 TAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03301 158 LSNLDAKLRVQMRAELkrLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2054-2269 |
8.56e-27 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 111.52 E-value: 8.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2054 ENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH--SVLKELLQVQQSLG 2131
Cdd:PRK10895 7 KNLAKAYKGRRV-----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2132 YCPQCDALFDELTAREHLQLYTRLR-GISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:PRK10895 82 YLPQEASIFRRLSVYDNLMAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK10895 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGT 220
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
1000-1185 |
9.37e-27 |
|
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: 109.43 E-value: 9.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--N 1074
Cdd:TIGR01166 1 YPGGPE-VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDpdD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:TIGR01166 80 QLFAA-DVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 45446740 1155 DPYARRAIWDLILKYKP-GRTILLSTHHMDEA 1185
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAeGMTVVISTHDVDLA 190
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
2063-2297 |
1.59e-26 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 113.68 E-value: 1.59e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2063 RKIGRILAVDRLCLGVRPGECFGLLGVNGAG--KTSTFKMLTGDESTTGGEAFVNGHSVLKELlqvQQSLG-YCPQCDAL 2139
Cdd:NF000106 21 KHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRRAL---RRTIG*HRPVR*GR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2140 FDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2219
Cdd:NF000106 98 RESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2220 KARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGdGYMITVRTKSSQSVKDVV 2297
Cdd:NF000106 178 RTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG-GRTLQIRPAHAAELDRMV 254
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2051-2269 |
2.03e-26 |
|
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: 110.08 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQS 2129
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQdPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGisWKdEARVVKWALEKLEL-----TKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPKLLK--WP-KEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGT 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2048-2264 |
2.34e-26 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 109.36 E-value: 2.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KEL 2123
Cdd:COG1136 2 SPLLELRNLTKSYGTGE-GEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslseREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQV-QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:COG1136 81 ARLrRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSmEECEALCTRLAIMVNGRL 2264
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNReLGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
2048-2270 |
2.37e-26 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 110.17 E-value: 2.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYK-----------------SRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG 2110
Cdd:COG1134 2 SSMIEVENVSKSYRlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2111 EAFVNGH-SVLKELlqvqqSLGycpqcdalFD-ELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYS 2188
Cdd:COG1134 82 RVEVNGRvSALLEL-----GAG--------FHpELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2189 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDP----KARRFlwnlILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG1134 149 SGMRARLAFAVATAVDPDILLVDEVLAVGDAafqkKCLAR----IRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRL 224
|
....*.
gi 45446740 2265 RCLGSI 2270
Cdd:COG1134 225 VMDGDP 230
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
995-1200 |
5.92e-26 |
|
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: 107.88 E-value: 5.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 995 KLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC 1070
Cdd:cd03292 5 NVTKTYPNGTA-ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1151 TAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03292 164 TGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
991-1207 |
6.16e-26 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 111.70 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMC 1070
Cdd:COG3839 4 LELENVSKSYGGVE--ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRAII---- 1146
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQR--VALG-----RALVrepk 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1147 ---LDEPTAGVDP----YARRAIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1207
Cdd:COG3839 154 vflLDEPLSNLDAklrvEMRAEIKRLHRRL--GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPE 219
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
988-1200 |
6.66e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 114.35 E-value: 6.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 988 PLVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRK 1065
Cdd:COG3845 3 PPALELRGITKRF--GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQHNVLFDRLTVEEHLW--------FYSRLKSmAQEEIRREMDKMIEDLELsnkrHSLVQTLSGGMKRKlsVAI- 1136
Cdd:COG3845 81 GIGMVHQHFMLVPNLTVAENIVlgleptkgGRLDRKA-ARARIRELSERYGLDVDP----DAKVEDLSVGEQQR--VEIl 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1137 -AFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG3845 154 kALYRGARILILDEPTAVLTPQEADELFEILrrLA-AEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
2052-2268 |
7.23e-26 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 106.75 E-value: 7.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSL 2130
Cdd:cd03214 1 EVENLSVGYGGRTV-----LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQcdalfdeltarehlqlytrlrgiswkdearvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03214 76 AYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLAReRGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2051-2277 |
7.79e-26 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 108.09 E-value: 7.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKeLLQVQQSL 2130
Cdd:cd03300 1 IELENVSKFY-----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-LPPHKRPV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03300 75 NTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2211 DEPTTGMDPKARRflwNLILDLI----KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2277
Cdd:cd03300 155 DEPLGALDLKLRK---DMQLELKrlqkELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIyeepANRF 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
1001-1204 |
1.07e-25 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 107.74 E-value: 1.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRTemDEIRKNLGMCPQHNVLF 1077
Cdd:cd03234 16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKP--DQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRLTVEEHLWFYS--RLKSMAQEEIRREM--DKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:cd03234 94 PGLTVRETLTYTAilRLPRKSSDAIRKKRveDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1154 VDP------------YARRaiwdlilkykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCG 1204
Cdd:cd03234 174 LDSftalnlvstlsqLARR-----------NRIVILTIHQ-PRSDLfrLFDRILLLSSGEIVYSG 226
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1000-1200 |
2.23e-25 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 106.52 E-value: 2.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF- 1077
Cdd:cd03245 12 YPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFy 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 ----DRLTV------EEHLWFYSRLkSMAQEEIRREMDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIIL 1147
Cdd:cd03245 92 gtlrDNITLgapladDERILRAAEL-AGVTDFVNKHPNGL--DLQIGERG----RGLSGGQRQAVALARALLNDPPILLL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1148 DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLgDRIAIISHGKL 1200
Cdd:cd03245 165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLV-DRIIVMDSGRI 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
990-1206 |
2.64e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 108.18 E-value: 2.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLG 1068
Cdd:PRK13635 5 IIRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1069 MCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--I 1145
Cdd:PRK13635 85 MVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQR--VAIAGVLALQPdiI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVrqLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTP 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
2053-2262 |
2.84e-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: 105.80 E-value: 2.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2053 IENLTkvYKSRKIGRILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELlqvQQSLG 2131
Cdd:cd03226 2 IENIS--FSYKKGTEILDDLSLDL--YAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIkAKER---RKSIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2132 YCPQ--CDALFDELTAREhlqLYTRLRGISwkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:cd03226 75 YVMQdvDYQLFTDSVREE---LLLGLKELD--AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2262
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANG 202
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
989-1209 |
4.47e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 107.13 E-value: 4.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 989 LVVCVDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNL 1067
Cdd:PRK13647 3 NIIEVEDLHFRYKDGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEkWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1068 GMCPQ--HNVLFDrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:PRK13647 82 GLVFQdpDDQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1209
Cdd:PRK13647 161 VLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
2050-2264 |
5.10e-25 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 109.03 E-value: 5.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKelLQVQQ- 2128
Cdd:COG3842 5 ALELENVSKRY-----GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG--LPPEKr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQCDALFDELTAREHLQLYTRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2207
Cdd:COG3842 78 NVGMVFQDYALFPHLTVAENVAFGLRMRGVP-KAEIRArVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG3842 157 LLLDEPLSALDAKLREEMREELRRLQReLGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1000-1206 |
1.12e-24 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.41 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1078
Cdd:COG1132 349 YPGDRP-VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGVVPQDTFLFS 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RlTVEEHLwFYSRLKSmAQEEIRR-----EMDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:COG1132 428 G-TIRENI-RYGRPDA-TDEEVEEaakaaQAHEFIEALP--DGYDTVVgergVNLSGGQRQRIAIARALLKDPPILILDE 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGSP 1206
Cdd:COG1132 503 ATSALDTETEALIQEALERLMKGRTTIVIAHrlstirNA-------DRILVLDDGRIVEQGTH 558
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1004-1200 |
1.23e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.45 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1004 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-----MDEIRKNLGMCPQ--HNVL 1076
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnknLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1077 FDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:PRK13641 99 FEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDliSKSPFE-LSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1155 DPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK13641 177 DPEGRKEMMQLFKDYqKAGHTVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1005-1212 |
1.36e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 106.26 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1005 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE-----IRKNLGMC---PQHNvL 1076
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkpLRKKVGIVfqfPEHQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1077 FDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSnkrHSLVQ----TLSGG-MKRklsVAIAFVGG--SRAIILDE 1149
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLP---EELLArspfELSGGqMRR---VAIAGVLAmePEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGT 1212
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFykLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPreIFADPD 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
2078-2264 |
1.57e-24 |
|
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: 104.28 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKEllQVQQSLGYCPQCDALFDELTAREHLQLYTR 2154
Cdd:cd03234 30 VESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGLTVRETLTYTAI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2155 LRGISWKDEARVVKWAlEKLELTKYADKPAGTY-----SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPkarrFLWNLI 2229
Cdd:cd03234 108 LRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNlvkgiSGGERRRVSIAVQLLWDPKVLILDEPTSGLDS----FTALNL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 2230 L----DLIKTGRSVVLTSHS-MEECEALCTRLAIMVNGRL 2264
Cdd:cd03234 183 VstlsQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEI 222
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2050-2247 |
2.01e-24 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 103.98 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKsrkiGRILAVDRLCLGVRPGE-CFgLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELL 2124
Cdd:COG2884 1 MIRFENVSKRYP----GGREALSDVSLEIEKGEfVF-LTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQQSLGYCPQcDA-LFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2203
Cdd:COG2884 76 YLRRRIGVVFQ-DFrLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 2204 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2247
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLE 198
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
995-1204 |
2.44e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 103.77 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 995 KLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhDIRTEMDEirkNLGMCPQhn 1074
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-RVSSLLGL---GGGFNPE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 vlfdrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKL--SVAIAFvgGSRAIILDEPTA 1152
Cdd:cd03220 99 -----LTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLafAIATAL--EPDILLIDEVLA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1153 GVDPY----ARRAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1204
Cdd:cd03220 172 VGDAAfqekCQRRLRELL---KQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
993-1200 |
2.63e-24 |
|
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: 103.38 E-value: 2.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGM 1069
Cdd:cd03262 3 IKNLHKSFGD--FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQHNVLFDRLTVEEHLWFYSR-LKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA---- 1144
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQR--VAIA-----RAlamn 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1145 ---IILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03262 154 pkvMLFDEPTSALDPELVGEVLDVMKDLaEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2054-2264 |
2.72e-24 |
|
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: 102.63 E-value: 2.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2054 ENLTK-VYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELLQvqQSL 2130
Cdd:cd03213 7 RNLTVtVKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRSFR--KII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGIswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03213 85 GYVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSM-EECEALCTRLAIMVNGRL 2264
Cdd:cd03213 136 DEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2048-2263 |
3.02e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 104.01 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES-TTGGEAFVNGHSVLKE-LLQ 2125
Cdd:COG1119 1 DPLLELRNVTVRRGGKTI-----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPpTYGNDVRLFGERRGGEdVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYC-PQCDALFDE-LTARE--------HLQLYtrlRGISWKDEARVVKWaLEKLELTKYADKPAGTYSGGNKRKL 2195
Cdd:COG1119 76 LRKRIGLVsPALQLRFPRdETVLDvvlsgffdSIGLY---REPTDEQRERAREL-LELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2196 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG-RSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGR 220
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
993-1206 |
3.24e-24 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 103.96 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1072
Cdd:cd03296 5 VRNVSKRFGDFV--ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSMAQE----EIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1149 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:cd03296 162 EPFGALDAKVRKELrrWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTP 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2051-2268 |
3.51e-24 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 103.00 E-value: 3.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRK-----------------IGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAF 2113
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgeVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2114 VNG--HSVLkellqvqqSLGYcpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN 2191
Cdd:cd03220 81 VRGrvSSLL--------GLGG-----GFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:cd03220 148 KARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
999-1206 |
5.25e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.39 E-value: 5.25e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 999 VYK-DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQH- 1073
Cdd:PRK13639 8 KYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTVGIVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:PRK13639 88 dDQLFAP-TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTS 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1153 GVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13639 167 GLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTP 221
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2050-2264 |
5.66e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 5.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MV--KIENLTKvYKSRKIGR-ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2117
Cdd:COG1129 236 MVgrELEDLFP-KRAAAPGEvVLEVEGLSVGgvvrdvsfsVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGK 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2118 SVlkELLQVQQS----LGYCP---QCDALFDELTARE-----HLQLYTRLRGISWKDEARVVKWALEKLEL-TKYADKPA 2184
Cdd:COG1129 315 PV--RIRSPRDAiragIAYVPedrKGEGLVLDLSIREnitlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2185 GTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG1129 393 GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
995-1200 |
5.76e-24 |
|
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: 102.19 E-value: 5.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 995 KLTKVYKDDKKLALNkLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHN 1074
Cdd:cd03298 2 RLDKIRFSYGEQPMH-FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDV-TAAPPADRPVSMLFQEN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VLFDRLTVEEH--LWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03298 80 NLFAHLTVEQNvgLGLSPGLKLTAED--RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03298 158 ALDPALRAEMLDLVLDLhaETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
993-1200 |
6.36e-24 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 105.55 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IRK 1065
Cdd:COG1135 4 LENLSKTFPTKGGpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDL-TALSErelraARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQH-NvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAfvggsRA 1144
Cdd:COG1135 83 KIGMIFQHfN-LLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQR--VGIA-----RA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1145 I-----IL--DEPTAGVDPYARRAIWDLILK--YKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG1135 155 LannpkVLlcDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2051-2268 |
9.81e-24 |
|
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: 101.56 E-value: 9.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK------ELL 2124
Cdd:cd03301 1 VELENVTKRFGNVT-----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDlppkdrDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQQSLgycpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:cd03301 76 MVFQNY-------ALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
991-1200 |
1.09e-23 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 99.81 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLG 1068
Cdd:cd03216 1 LELRGITKRFGGVK--ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1069 MCPQhnvlfdrltveehlwfysrlksmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:cd03216 79 MVYQ---------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1149 EPTAGVDPYARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03216 108 EPTAALTPAEVERLFKVIrrLR-AQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2051-2264 |
1.88e-23 |
|
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: 101.10 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK---E 2122
Cdd:cd03260 1 IELRDLNVYYGDKH-----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDldvD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 LLQVQQSLGYCPQCDALFDeLTAREHLQLYTRLRGISWKDEAR-VVKWALEKLELTKY-ADKPAGTY-SGGNKRKLSTAI 2199
Cdd:cd03260 76 VLELRRRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDeRVEEALRKAALWDEvKDRLHALGlSGGQQQRLCLAR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2200 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIAEL-KKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
993-1200 |
2.31e-23 |
|
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: 101.42 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGM 1069
Cdd:COG1124 4 VRNLSVSYgqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRkAFRRRVQM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQH--NVLFDRLTVEEHLwfySR-LKSMAQEEIRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:COG1124 84 VFQDpyASLHPRHTVDRIL---AEpLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEPELL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLILKYK--PGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG1124 161 LLDEPTSALDVSVQAEILNLLKDLReeRGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2051-2263 |
2.39e-23 |
|
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: 99.18 E-value: 2.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQ--- 2127
Cdd:cd03229 1 LELKNVSKRY-----GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPplr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLQLytrlrgiswkdearvvkwALekleltkyadkpagtySGGNKRKLSTAIALIGYPAF 2207
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIAL------------------GL----------------SGGQQQRVALARALAMDPDV 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:cd03229 122 LLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1003-1206 |
6.20e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 101.46 E-value: 6.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMCPQH--NVLF 1077
Cdd:PRK13636 17 DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:PRK13636 97 SA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPM 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1158 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13636 176 GVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNP 226
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
999-1200 |
6.77e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 100.24 E-value: 6.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 999 VYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFP--PTSGSATIYGHDI---RTEMDEIRKNLGMC 1070
Cdd:PRK14239 13 VYYNKKK-ALNSVSLDFYPNEITALIGPSGSGKSTllrSINRMNDLNPevTITGSIVYNGHNIyspRTDTVDLRKEIGMV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDrLTVEEHLWFYSRLKSMAQEEIrreMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:PRK14239 92 FQQPNPFP-MSIYENVVYGLRLKGIKDKQV---LDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQRVCIARVLATSP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK14239 168 KIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2050-2264 |
7.16e-23 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 102.46 E-value: 7.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----KELL 2124
Cdd:COG1135 1 MIELENLSKTFPTKG-GPVTALDDVSLTIEKGEIFGIIGYSGAGK-STLiRCINLLERPTSGSVLVDGVDLTalseRELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQQSLGYCPQCDALFDELTAREHLQLYTRLRGISwKDE--ARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTA 2198
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVP-KAEirKRV----AELLELVGLSDK-ADAYpsqlSGGQKQRVGIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2199 IALIGYPAFIFLDEPTTGMDPKARRflwnLILDLIK-----TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG1135 153 RALANNPKVLLCDEATSALDPETTR----SILDLLKdinreLGLTIVLITHEMDVVRRICDRVAVLENGRI 219
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
998-1200 |
8.70e-23 |
|
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: 98.01 E-value: 8.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 998 KVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGL--FPPTSGSATIYGHDIRteMDEIRKNLGMCPQHNV 1075
Cdd:cd03213 16 SPSKSGKQL-LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRrtGLGVSGEVLINGRPLD--KRSFRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSmaqeeirremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:cd03213 93 LHPTLTVRETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1156 PYARRAIWDLILKY-KPGRTILLSTHHM-DEADLLGDRIAIISHGKL 1200
Cdd:cd03213 144 SSSALQVMSLLRRLaDTGRTIICSIHQPsSEIFELFDKLLLLSQGRV 190
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1000-1206 |
9.47e-23 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 99.11 E-value: 9.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1078
Cdd:cd03244 12 YRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 ---RLTV-------EEHLWfySRLKSMAQEEIRREMDKMIEDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:cd03244 92 gtiRSNLdpfgeysDEELW--QALERVGLKEFVESLPGGLDTVVEEGGEN-----LSVGQRQLLCLARALLRKSKILVLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1149 EPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1206
Cdd:cd03244 165 EATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTiIDS--DRILVLDKGRVVEFDSP 221
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1005-1200 |
9.71e-23 |
|
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: 97.50 E-value: 9.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1005 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCP---QHNVLFDR 1079
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVtrRSPRDAIRAGIAYVPedrKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLwfysrlksmaqeeirremdkmiedlelsnkrhSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:cd03215 93 LSVAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45446740 1160 RAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03215 141 AEIYRLIRELAdAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1000-1206 |
9.84e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 100.21 E-value: 9.84e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDIRTEMD---EIRKNLGMCPQH-NV 1075
Cdd:PRK13648 17 YQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQAITDDnfeKLRKHIGIVFQNpDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK13648 95 QFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1156 PYARRAIWDLILKYKPGR--TILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHniTIISITHDLSEA-MEADHVIVMNKGTVYKEGTP 226
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2050-2263 |
9.86e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 100.06 E-value: 9.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLtkvykSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2127
Cdd:PRK11300 5 LLSVSGL-----MMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIegLPGHQIAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTARE------HLQLYTRLRGISWKDEA----------RVVKWaLEKLELTKYADKPAGTYSGGN 2191
Cdd:PRK11300 80 MGVVRTFQHVRLFREMTVIEnllvaqHQQLKTGLFSGLLKTPAfrraesealdRAATW-LERVGLLEHANRQAGNLAYGQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK11300 159 QRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2051-2271 |
1.30e-22 |
|
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: 98.95 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2130
Cdd:cd03299 1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03299 74 SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2271
Cdd:cd03299 154 DEPFSALDVRTKEKLREELKKIRKEFGVTVLhVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
990-1206 |
1.86e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 99.87 E-value: 1.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA---TIYGHDIRTE-MDEIRK 1065
Cdd:PRK13640 5 IVEFKHVSFTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNskiTVDGITLTAKtVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1066 NLGMCPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1144
Cdd:PRK13640 85 KVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1145 IILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13640 165 IILDESTSMLDPAGKEQILKLIrkLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSP 227
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
996-1200 |
2.60e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 101.03 E-value: 2.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKK--LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1069
Cdd:PRK11153 7 ISKVFPQGGRtiHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQIGM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQH-NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRAIIL- 1147
Cdd:PRK11153 87 IFQHfNLLSSR-TVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQR--VAIARALASNPKVLl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1148 -DEPTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11153 164 cDEATSALDPATTRSILELLKDInrELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1007-1195 |
2.76e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 103.17 E-value: 2.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYG--HDIRTEMDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWF---YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGmKRKLsVAI--AFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:COG1129 99 NIFLgrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVA-QQQL-VEIarALSRDARVLILDEPTASLTEREV 176
|
170 180 190
....*....|....*....|....*....|....*...
gi 45446740 1160 RAIWDLI--LKYKpGRTILLSTHHMDEADLLGDRIAII 1195
Cdd:COG1129 177 ERLFRIIrrLKAQ-GVAIIYISHRLDEVFEIADRVTVL 213
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1006-1206 |
3.03e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.52 E-value: 3.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1006 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCP--QHNVLFDRLTVE 1083
Cdd:PRK11300 19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREMTVI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 EHL-----------WFYSRLKSMAQEEIRRE-MDKMIEDLE------LSNKRHSlvqTLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:PRK11300 99 ENLlvaqhqqlktgLFSGLLKTPAFRRAESEaLDRAATWLErvglleHANRQAG---NLAYGQQRRLEIARCMVTQPEIL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIaeLRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTP 238
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2073-2244 |
3.04e-22 |
|
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: 96.66 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2073 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLY 2152
Cdd:TIGR01189 18 GLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALENLHFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TRLRGiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFIfLDEPTTGMDPKARRFLWNLILD 2231
Cdd:TIGR01189 98 AAIHG----GAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALArLWLSRRPLWI-LDEPTTALDKAGVALLAGLLRA 172
|
170
....*....|...
gi 45446740 2232 LIKTGRSVVLTSH 2244
Cdd:TIGR01189 173 HLARGGIVLLTTH 185
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1007-1205 |
3.40e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 98.27 E-value: 3.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIR-KNLGMC-----PqhNVlFDRL 1080
Cdd:COG4674 25 ALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDL-TGLDEHEiARLGIGrkfqkP--TV-FEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHL---------WFYSrLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:COG4674 101 TVFENLelalkgdrgVFAS-LFARLTAEERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1152 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1205
Cdd:COG4674 180 AGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGS 233
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
1007-1206 |
4.23e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 98.66 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1079
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITStsknkDIKQIRKKVGLVFQfpESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 lTVEEHLWFYSRLKSMAQEE---IRREMDKMI---EDLELSNKRHslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:PRK13649 102 -TVLKDVAFGPQNFGVSQEEaeaLAREKLALVgisESLFEKNPFE-----LSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1154 VDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13649 176 LDPKGRKELMTLFKKlHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKP 229
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1006-1206 |
6.93e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.88 E-value: 6.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1006 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMDEIR-KNLGMCPQHNVLFDRL 1080
Cdd:PRK10070 42 LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdAELREVRrKKIAMVFQSFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:PRK10070 122 TVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1161 AIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK10070 202 EMQDELVKLqaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTP 249
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2068-2264 |
7.49e-22 |
|
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: 95.19 E-value: 7.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2068 ILAVDRLCLG---------VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQSLGYCP-- 2134
Cdd:cd03215 4 VLEVRGLSVKgavrdvsfeVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdaIRAGIAYVPed 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2135 -QCDALFDELTAREHLQLYTRLrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEP 2213
Cdd:cd03215 84 rKREGLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2214 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2051-2269 |
8.79e-22 |
|
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: 96.64 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQQSL 2130
Cdd:cd03296 3 IEVRNVSKRF-----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ-ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWK-DEARV---VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2206
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERpPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2207 FIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1007-1200 |
9.16e-22 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 96.49 E-value: 9.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE---IRKNLGMCPQHNVLFDRLTVE 1083
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAIVPEGRRVFSRMTVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 EHL----WFYSRlkSMAQEEIRRemdkmIEDL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:PRK11614 99 ENLamggFFAER--DQFQERIKW-----VYELfpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 1158 ARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11614 172 IIQQIFDTIEQLREqGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2047-2264 |
9.81e-22 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.63 E-value: 9.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2047 DNDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVL----K 2121
Cdd:COG1129 1 AEPLLEMRGISKSF-----GGVKALDGVSLELRPGEVHALLGENGAGK-STLmKILSGVYQPDSGEILLDGEPVRfrspR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2122 ELLQ-----VQQSLgycpqcdALFDELTAREHL---QLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKR 2193
Cdd:COG1129 75 DAQAagiaiIHQEL-------NLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG1129 148 LVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
993-1199 |
1.10e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 97.08 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVY---KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKN--- 1066
Cdd:COG1101 4 LKNLSKTFnpgTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV-TKLPEYKRAkyi 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1067 --------LGMCPqhnvlfdRLTVEEHLWF-YSRLKSM--------AQEEIRREMDKMIeDLELSNKRHSLVQTLSGGMK 1129
Cdd:COG1101 83 grvfqdpmMGTAP-------SMTIEENLALaYRRGKRRglrrgltkKRRELFRELLATL-GLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1130 RKLSVAIAFVGGSRAIILDEPTAGVDPyaRRAiwDLILKY------KPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDP--KTA--ALVLELtekiveENNLTTLMVTHNMEQALDYGNRLIMMHEGR 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
996-1237 |
1.32e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 1.32e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1073
Cdd:PRK13652 9 LCYSYSGSKE-ALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNp 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 -NVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:PRK13652 88 dDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLTLVKRPAEP 1228
Cdd:PRK13652 167 GLDPQGVKELIDFLndLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVeeIFLQPDLLARVHLDLPSLPKLI 246
|
....*....
gi 45446740 1229 GGPQEPGLA 1237
Cdd:PRK13652 247 RSLQAQGIA 255
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2051-2264 |
1.82e-21 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 96.56 E-value: 1.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSR-------------------KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2111
Cdd:cd03294 1 IKIKGLYKIFGKNpqkafkllakgkskeeilkKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2112 AFVNGHSVL----KELLQVQ-QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGT 2186
Cdd:cd03294 81 VLIDGQDIAamsrKELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2187 YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2048-2264 |
2.06e-21 |
|
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: 101.03 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNghsVLKELL--- 2124
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVR---VGDEWVdmt 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 --------QVQQSLGYCPQCDALFDELTAREHLqlyTRLRGISWKDEARVVKwALEKLELTKYADKPA--------GTYS 2188
Cdd:TIGR03269 354 kpgpdgrgRAKRYIGILHQEYDLYPHRTVLDNL---TEAIGLELPDELARMK-AVITLKMVGFDEEKAeeildkypDELS 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2189 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKArEEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2078-2244 |
2.40e-21 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 102.49 E-value: 2.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDEST---TGGEAFVNGHSVLKELlqvQQSLGYCPQCDALFDELTAREHLQLYTR 2154
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSF---QRSIGYVQQQDLHLPTSTVRESLRFSAY 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2155 LR---GISWKDEARVVKWALEKLELTKYADKPAGTYSGG----NKRKLSTAIALIGYPA-FIFLDEPTTGMDPKARRFLW 2226
Cdd:TIGR00956 863 LRqpkSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGlnveQRKRLTIGVELVAKPKlLLFLDEPTSGLDSQTAWSIC 942
|
170
....*....|....*...
gi 45446740 2227 NLILDLIKTGRSVVLTSH 2244
Cdd:TIGR00956 943 KLMRKLADHGQAILCTIH 960
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2051-2270 |
2.59e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 96.66 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE---LLQVQ 2127
Cdd:PRK13637 3 IKIENLTHIYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKkvkLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCD--ALFDElTAREHLQLYTRLRGISWKDEARVVKWALE--KLELTKYADKPAGTYSGGNKRKLSTAIALIG 2203
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNivGLDYEDYKDKSPFELSGGQKRRVAIAGVVAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2204 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:PRK13637 162 EPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTP 229
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1002-1181 |
2.67e-21 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 100.51 E-value: 2.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1002 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1080
Cdd:TIGR02868 345 PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLwfysRL--KSMAQEEIRREMDKM-----IEDLE--LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:TIGR02868 424 TVRENL----RLarPDATDEELWAALERVgladwLRALPdgLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPT 499
|
170 180 190
....*....|....*....|....*....|
gi 45446740 1152 AGVDPYARRAIWDLILKYKPGRTILLSTHH 1181
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1003-1206 |
4.14e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.76 E-value: 4.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdiRT----EMdeirkNLGMCPQhnvlfd 1078
Cdd:COG1134 37 EEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---RVsallEL-----GAGFHPE------ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 rLTVEEHLWFYSRLKSMAQEEIRREMDKmIEDL-ELSNKRHSLVQTLSGGMKRKLSVAIAFvggsrAI-----ILDEPTA 1152
Cdd:COG1134 103 -LTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDFIDQPVKTYSSGMRARLAFAVAT-----AVdpdilLVDEVLA 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1153 GVDPY----ARRAIWDLILKykpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:COG1134 176 VGDAAfqkkCLARIRELRES---GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDP 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
990-1206 |
5.69e-21 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 100.97 E-value: 5.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKddKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNL 1067
Cdd:NF033858 1 VARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadARHRRAVCPRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1068 GMCPQ---HNvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRA 1144
Cdd:NF033858 79 AYMPQglgKN-LYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1145 IILDEPTAGVDPYARRAIWDLI---LKYKPGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGSP 1206
Cdd:NF033858 158 LILDEPTTGVDPLSRRQFWELIdriRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTP 221
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1000-1231 |
6.16e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 95.07 E-value: 6.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI---RTEMDEIRKNLGMC---PQH 1073
Cdd:PRK13638 11 YQDEP--VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:PRK13638 89 QIFYT--DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1154 VDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLT---LVKRPAE 1227
Cdd:PRK13638 167 LDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPgeVFACTEAMEQAGLTqpwLVKLHTQ 246
|
....
gi 45446740 1228 PGGP 1231
Cdd:PRK13638 247 LGLP 250
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
1000-1201 |
6.34e-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: 92.38 E-value: 6.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDr 1079
Cdd:cd03247 10 YPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFD- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 ltveehlwfysrlksmaqeeirremdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:cd03247 89 ----------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1160 RAIWDLILKYKPGRTILLSTHHmdeadLLG----DRIAIISHGKLK 1201
Cdd:cd03247 135 RQLLSLIFEVLKDKTLIWITHH-----LTGiehmDKILFLENGKII 175
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1007-1221 |
7.97e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 95.23 E-value: 7.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-----EMDEIRKNLGMCPQ--HNVLFDR 1079
Cdd:PRK13646 22 AIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQfpESQLFED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 lTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSnkRHSLVQT---LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1156
Cdd:PRK13646 102 -TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1157 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP--LFLKGTYGDGYRLTL 1221
Cdd:PRK13646 179 QSKRQVMRLLksLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPkeLFKDKKKLADWHIGL 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1002-1211 |
8.36e-21 |
|
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: 93.44 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1002 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1080
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLwFYSRLKSMAQEEIRRE----MDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03254 92 TIMENI-RLGRPNATDEEVIEAAkeagAHDFIMKLP--NGYDTVLgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1153 GVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP--LFLKG 1211
Cdd:cd03254 169 NIDTETEKLIQEALEKLMKGRTSIIIAHRLStikNA----DKILVLDDGKIIEEGTHdeLLAKK 228
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
993-1211 |
8.67e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.80 E-value: 8.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDK-KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKNLGM 1069
Cdd:PRK13650 7 VKNLTFKYKEDQeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENvwDIRHKIGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQH-NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFVGGSRA--II 1146
Cdd:PRK13650 86 VFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQR--VAIAGAVAMRPkiII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1147 LDEPTAGVDPYARRaiwDLI-----LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSP--LFLKG 1211
Cdd:PRK13650 164 LDEATSMLDPEGRL---ELIktikgIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPreLFSRG 231
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
1002-1213 |
8.98e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 93.83 E-value: 8.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1002 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1080
Cdd:cd03253 11 DPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVVPQDTVLFND- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLwFYSRLkSMAQEEIRREMDK-MIED--LELSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:cd03253 90 TIGYNI-RYGRP-DATDEEVIEAAKAaQIHDkiMRFPDGYDTIVGerglKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1154 VDPYARRAIWDLILKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFL---KGTY 1213
Cdd:cd03253 168 LDTHTEREIQAALRDVSKGRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELlakGGLY 229
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1003-1206 |
9.87e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 94.67 E-value: 9.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH-NVLFDR 1079
Cdd:PRK13644 13 DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVFQNpETQFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:PRK13644 93 RTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1160 RAIWDLILK-YKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13644 173 IAVLERIKKlHEKGKTIVYITHNLEELH-DADRIIVMDRGKIVLEGEP 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
1000-1205 |
1.03e-20 |
|
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: 93.70 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1078
Cdd:cd03252 10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RlTVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:cd03252 90 R-SIRDNIALADPGMSMERvIEAAKLAGAHDFISELPEGYDTIVgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1154 VDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLKCCGS 1205
Cdd:cd03252 169 LDYESEHAIMRNMHDICAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGS 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2051-2264 |
1.53e-20 |
|
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: 90.57 E-value: 1.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqvqqsl 2130
Cdd:cd03216 1 LELRGITKRF-----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 gycpqcdalfdeLTAREHLQLytrlrGIswkdeaRVVkwalekleltkyadkpagtY--SGGNKRKLSTAIALIGYPAFI 2208
Cdd:cd03216 67 ------------ASPRDARRA-----GI------AMV-------------------YqlSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2209 FLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
993-1196 |
2.05e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 93.39 E-value: 2.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVY--KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEiRknlGMC 1070
Cdd:COG4525 6 VRHVSVRYpgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGAD-R---GVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:COG4525 82 FQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1151 TAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIIS 1196
Cdd:COG4525 162 FGALDALTREQMQELLLDVwqRTGKGVFLITHSVEEALFLATRLVVMS 209
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2050-2264 |
2.09e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 95.25 E-value: 2.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQ 2125
Cdd:PRK11153 1 MIELKNISKVFPQGG-RTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTalseKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKD-EARVvkwaLEKLELTKYADKpAGTY----SGGNKRKLSTAIA 2200
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEiKARV----TELLELVGLSDK-ADRYpaqlSGGQKQRVAIARA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRflwnLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTR----SILELLKDinrelGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2052-2263 |
2.12e-20 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 92.63 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQVQ 2127
Cdd:cd03256 2 EVENLSKTYPNGKK----ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINklkgKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLqLYTRLRGISW---------KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTA 2198
Cdd:cd03256 78 RQIGMIFQQFNLIERLSVLENV-LSGRLGRRSTwrslfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2199 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGR 222
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
1000-1199 |
2.90e-20 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 92.29 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1078
Cdd:cd03251 10 YPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGLVSQDVFLFN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RlTVEEHLwFYSRLKSmAQEEIRR-----EMDKMIEDLElsNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:cd03251 90 D-TVAENI-AYGRPGA-TREEVEEaaraaNAHEFIMELP--EGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKPGRTIL-----LSThhMDEAdllgDRIAIISHGK 1199
Cdd:cd03251 165 ATSALDTESERLVQAALERLMKNRTTFviahrLST--IENA----DRIVVLEDGK 213
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
980-1206 |
3.23e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 95.40 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 980 MEEEPTHLPLVVCVDKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTE 1059
Cdd:PRK09452 4 LNKQPSSLSPLVELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-TH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1060 MDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIR-REMD--KMIEDLELSNKRhslVQTLSGGMKRKLSVAI 1136
Cdd:PRK09452 81 VPAENRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITpRVMEalRMVQLEEFAQRK---PHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1137 AFVGGSRAIILDEPTAGVDpYARRAIWDLILKY---KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD-YKLRKQMQNELKAlqrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTP 229
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
1007-1185 |
3.48e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.76 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirKNLGMCPQHNVLFDRL--TVEE 1084
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 --------HLWFYSRLKSMAQEEIRREMDKM-IEDLElsnKRHslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:NF040873 77 lvamgrwaRRGLWRRLTRDDRAAVDDALERVgLADLA---GRQ--LGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|.
gi 45446740 1156 PYARRAIWDLILKY-KPGRTILLSTHHMDEA 1185
Cdd:NF040873 152 AESRERIIALLAEEhARGATVVVVTHDLELV 182
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1000-1206 |
5.04e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 92.14 E-value: 5.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVL-F 1077
Cdd:PRK13548 10 VRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLPQHSSLsF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DrLTVEE--HLWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKlsVAIAFV--------GGSRAIIL 1147
Cdd:PRK13548 90 P-FTVEEvvAMGRAPHGLSRAED--DALVAAALAQVDLAHLAGRDYPQLSGGEQQR--VQLARVlaqlwepdGPPRWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1148 DEPTAGVDPY--------ARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13548 165 DEPTSALDLAhqhhvlrlARQ------LAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
2050-2313 |
6.45e-20 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 94.52 E-value: 6.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELLQVQQS 2129
Cdd:PRK11607 19 LLEIRNLTKSFDGQ-----HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD-LSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:PRK11607 93 INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS----IQHLKNRFGDGYMIT 2284
Cdd:PRK11607 173 LDEPMGALDKKLRDRMQLEVVDILeRVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEpeeiYEHPTTRYSAEFIGS 252
|
250 260
....*....|....*....|....*....
gi 45446740 2285 VrtkssqsvkdvvrffnrNFPEAMLKERH 2313
Cdd:PRK11607 253 V-----------------NVFEGVLKERQ 264
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2078-2244 |
6.68e-20 |
|
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: 90.00 E-value: 6.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELlqvQQSLGYCPQCDALFDELTAREHLQLYTRL 2155
Cdd:cd03232 30 VKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNF---QRSTGYVEQQDVHSPNLTVREALRFSALL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2156 RGISwkdearvvkwaLEkleltkyadkpagtysggNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2235
Cdd:cd03232 107 RGLS-----------VE------------------QRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
....*....
gi 45446740 2236 GRSVVLTSH 2244
Cdd:cd03232 158 GQAILCTIH 166
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
2080-2265 |
6.71e-20 |
|
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: 90.43 E-value: 6.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2080 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKELLQVQQ-SLGYCPQCDALFDELTAREHLqLYTR 2154
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfDSRKKINLPPQQrKIGLVFQQYALFPHLNVRENL-AFGL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2155 LRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK 2234
Cdd:cd03297 101 KRKRNREDRISVDE-LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
|
170 180 190
....*....|....*....|....*....|..
gi 45446740 2235 T-GRSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:cd03297 180 NlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
2070-2264 |
7.64e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 92.06 E-value: 7.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYCPQC--DALF---- 2140
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNpdDQLFaptv 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2141 DELTAREHLQLytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2220
Cdd:PRK13639 97 EEDVAFGPLNL-----GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 2221 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK13639 172 GASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKI 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2053-2244 |
1.12e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2053 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkellqvqQSLGY 2132
Cdd:COG0488 1 LENLSKSFGGRPL-----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGY 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2133 CPQCDALFDELTAREHL--------QLYTRLRGIS-------------------------WKDEARVVKwALEKLELTK- 2178
Cdd:COG0488 66 LPQEPPLDDDLTVLDTVldgdaelrALEAELEELEaklaepdedlerlaelqeefealggWEAEARAEE-ILSGLGFPEe 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2179 YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2244
Cdd:COG0488 145 DLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEF---LKNYPGTVLVVSH 207
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
2050-2244 |
1.19e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 89.48 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTkvykSRKIGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQS 2129
Cdd:PRK13538 1 MLEARNLA----CERDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISwkDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTA-IALIGYPAFI 2208
Cdd:PRK13538 76 LLYLGHQPGIKTELTALENLRFYQRLHGPG--DDEALWE-ALAQVGLAGFEDVPVRQLSAGQQRRVALArLWLTRAPLWI 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446740 2209 fLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:PRK13538 153 -LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
996-1206 |
1.42e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 93.36 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNV 1075
Cdd:PRK11607 25 LTKSF--DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQSYA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK11607 102 LFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1156 PYARR----AIWDLILKYkpGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK11607 182 KKLRDrmqlEVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEP 234
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2050-2275 |
2.78e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 2.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2127
Cdd:PRK09700 5 YISMAGIGK-----SFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYnkLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHL---QLYTR----LRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIA 2200
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSN 234
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
1008-1198 |
2.95e-19 |
|
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: 89.06 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrtemDEIRKNLGMCPQHNVLFDRLTVEEH-- 1085
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI----TEPGPDRMVVFQNYSLLPWLTVRENia 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1086 LWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1165
Cdd:TIGR01184 77 LAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEE 156
|
170 180 190
....*....|....*....|....*....|....*
gi 45446740 1166 ILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:TIGR01184 157 LMQIweEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
987-1206 |
4.04e-19 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.34 E-value: 4.04e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 987 LPLVVCVDKLTKVYkddkklaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIrtEMDEI 1063
Cdd:TIGR00955 27 LRGCFCRERPRKHL-------LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPI--DAKEM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1064 RKNLGMCPQHNVLFDRLTVEEHLWFYSRLK---SMAQEEIRREMDKMIEDLELSNKRHSLVQT------LSGGMKRKLSV 1134
Cdd:TIGR00955 98 RAISAYVQQDDLFIPTLTVREHLMFQAHLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAF 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1135 AIAFVGGSRAIILDEPTAGVDPYAR----RAIWDLILKykpGRTILLSTHHmDEADL--LGDRIAIISHGKLKCCGSP 1206
Cdd:TIGR00955 178 ASELLTDPPLLFCDEPTSGLDSFMAysvvQVLKGLAQK---GKTIICTIHQ-PSSELfeLFDKIILMAEGRVAYLGSP 251
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1012-1200 |
4.35e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 93.16 E-value: 4.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1012 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCP---QHNVLFDRLTVEE-- 1084
Cdd:COG1129 272 SFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYVPedrKGEGLVLDLSIREni 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 ---HLWFYSRLKSMAQEEIRREMDKMIEDLEL-SNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEPTAGVDPYA 1158
Cdd:COG1129 352 tlaSLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQK--VVLAkwLATDPKVLILDEPTRGIDVGA 429
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 1159 RRAIWDLILKY-KPGRTILLSTHHMDEadLLG--DRIAIISHGKL 1200
Cdd:COG1129 430 KAEIYRLIRELaAEGKAVIVISSELPE--LLGlsDRILVMREGRI 472
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1007-1206 |
6.02e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 6.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSA-----TIYGHDIRTEMDEIRKNLGMCPQ--HNVLFDR 1079
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVFQfpESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 lTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNK--RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:PRK13643 101 -TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEfwEKSPFE-LSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1158 ARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK13643 179 ARIEMMQLFESiHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTP 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
993-1194 |
7.01e-19 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 90.11 E-value: 7.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDIRT----EMDEI 1063
Cdd:COG0444 4 VRNLKVYFPTRRGVvkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1064 R-KNLGMCPQhnvlfD-------RLTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQ---TLSGGMKRK 1131
Cdd:COG0444 84 RgREIQMIFQ-----DpmtslnpVMTVGDQIAePLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1132 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAI 1194
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLkdLQRELGLAILFITHDLGVVAEIADRVAV 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
1003-1181 |
7.23e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 87.03 E-value: 7.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1082
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1083 EEHLWFYSRLKSMAQeeirREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1162
Cdd:TIGR01189 91 LENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALL 166
|
170 180
....*....|....*....|
gi 45446740 1163 WDLILKY-KPGRTILLSTHH 1181
Cdd:TIGR01189 167 AGLLRAHlARGGIVLLTTHQ 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
999-1205 |
7.81e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 7.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 999 VYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP------PTSGSATIYGHDI-RTEMDEIRKNLGMCP 1071
Cdd:PRK14246 18 LYINDKAI-LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIfQIDAIKLRKEVGMVF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLWFysRLKSMAQEEiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK14246 97 QQPNPFPHLSIYDNIAY--PLKSHGIKE-KREIKKIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPK 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS 1205
Cdd:PRK14246 174 VLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2048-2265 |
8.16e-19 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkellqvq 2127
Cdd:COG0488 313 KKVLELEGLSKSYGDKTL-----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGT-VKLGETV-------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 qSLGYCPQ-CDALFDELTAREHLQlytrlRGISWKDEARVVKWaLEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:COG0488 379 -KIGYFDQhQEELDPDKTVLDELR-----DGAPGGTEQEVRGY-LGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPP 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2206 AFIFLDEPTTGMDPKARrflwNLILDLIKT--GrSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:COG0488 452 NVLLLDEPTNHLDIETL----EALEEALDDfpG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2068-2264 |
1.15e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 92.04 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2068 ILAVDRLC--------LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQQSLGYCP--- 2134
Cdd:PRK15439 268 VLTVEDLTgegfrnisLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEInaLSTAQRLARGLVYLPedr 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2135 QCDALFDELTAREHLQLYTRLRGISWKDEARvvkwalEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK15439 348 QSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYrralnikfnhAEQAARTLSGGNQQKVLIAKCLEAS 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK15439 422 PQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2050-2264 |
1.17e-18 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 87.46 E-value: 1.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KELLQV 2126
Cdd:PRK09493 1 MIEFKNVSKHF-----GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQCDALFDELTAREHLQL-YTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK09493 156 KLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRI 214
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
993-1206 |
1.32e-18 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 90.14 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQ 1072
Cdd:PRK10851 5 IANIKKSFGRTQ--VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWF----YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:PRK10851 82 HYALFRHMTVFDNIAFgltvLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1149 EPTAGVDPYARRAI--WDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK10851 162 EPFGALDAQVRKELrrWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTP 221
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2051-2264 |
1.68e-18 |
|
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: 86.31 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL----KELLQV 2126
Cdd:cd03292 1 IEFINVTKTYP----NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSdlrgRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2206
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2207 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1007-1207 |
2.48e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 2.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT------EMDEIRKNLGMC---PQHNVLF 1077
Cdd:PRK13645 26 ALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEYQLFQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:PRK13645 106 E--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEdyvKRSPF--ELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1155 DPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPL 1207
Cdd:PRK13645 182 DPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPF 236
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
2070-2248 |
4.53e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.59 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvlkellqvqqSLGYCPQCDALFDEL--TARE 2147
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA----------RVAYVPQRSEVPDSLplTVRD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 --------HLQLYTRLRGiswKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDP 2219
Cdd:NF040873 77 lvamgrwaRRGLWRRLTR---DDRAAVDD-ALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180
....*....|....*....|....*....
gi 45446740 2220 KARRFLWNLILDLIKTGRSVVLTSHSMEE 2248
Cdd:NF040873 153 ESRERIIALLAEEHARGATVVVVTHDLEL 181
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
999-1215 |
5.16e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 86.69 E-value: 5.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 999 VYKDDKKLALNKL---SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQH- 1073
Cdd:PRK13642 11 VFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIGMVFQNp 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:PRK13642 91 DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1154 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEAdLLGDRIAIISHGKLKCCGSPLFLKGTYGD 1215
Cdd:PRK13642 171 LDPTGRQEIMRVIheIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSED 233
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2050-2259 |
7.55e-18 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 85.68 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqvqqs 2129
Cdd:COG4525 3 MLTVRHVSVRYPGGG-QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 lgycP--------QCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL 2201
Cdd:COG4525 74 ----PgadrgvvfQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2202 IGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIM 2259
Cdd:COG4525 150 AADPRFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVEEALFLATRLVVM 208
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
2079-2283 |
7.91e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 90.11 E-value: 7.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2079 RPGECFGLLGVNGAGKTS-----TFKMLTGdeSTTGGEAFVNGHSVLKEllQVQQSLGYCPQCDALFDELTAREHLQLYT 2153
Cdd:TIGR00955 49 KPGELLAVMGSSGAGKTTlmnalAFRSPKG--VKGSGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLTVREHLMFQA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2154 RLR---GISWKDEARVVKWALEKLELTKYADKPAGT------YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2224
Cdd:TIGR00955 125 HLRmprRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2225 LWNLILDLIKTGRSVVLTSH--SMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYMI 2283
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTIHqpSSELFE-LFDKIILMAEGRVAYLGSPDQAVPFFSDlGHPC 265
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
982-1201 |
8.16e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 8.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 982 EEPTHLP-LVVCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtem 1060
Cdd:COG0488 306 PPPERLGkKVLELEGLSKSY-GDKTL-LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1061 deirknLGMCPQHNVLFD-RLTVEEHLWfysRLKSMAQE-EIRremdKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1137
Cdd:COG0488 380 ------IGYFDQHQEELDpDKTVLDELR---DGAPGGTEqEVR----GYLGRFLFSGDDaFKPVGVLSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1138 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGrTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALDDF-PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2068-2264 |
8.84e-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: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2068 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQQSLGYCPQCDALFDElTA 2145
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTD-IRQLdpADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2146 REHLQLytrlrGISWKDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPT 2214
Cdd:cd03245 95 RDNITL-----GAPLADDERILR-AAELAGVTDFVNKhPNGldlqigergrGLSGGQRQAVALARALLNDPPILLLDEPT 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2215 TGMDPKA-RRFLWNliLDLIKTGRSVVLTSH--SMEEceaLCTRLAIMVNGRL 2264
Cdd:cd03245 169 SAMDMNSeERLKER--LRQLLGDKTLIIITHrpSLLD---LVDRIIVMDSGRI 216
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1007-1204 |
8.86e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.46 E-value: 8.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK09700 20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGIIYQELSVIDELTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLwFYSRL---KSMA-----QEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1156
Cdd:PRK09700 100 NL-YIGRHltkKVCGvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1157 YARRAIWDLI--LKyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCG 1204
Cdd:PRK09700 179 KEVDYLFLIMnqLR-KEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
994-1200 |
9.56e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 9.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 994 DKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGM 1069
Cdd:PRK10908 5 EHVSKAYLGGRQ-ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQ-HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:PRK10908 84 IFQdHHLLMDR-TVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLAD 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1149 EPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK10908 163 EPTGNLDDALSEGILRLFEEFnRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2051-2264 |
1.04e-17 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 84.12 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL---KELLQVQ 2127
Cdd:cd03262 1 IEIKNLHKSFGDFHV-----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTddkKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLQL-YTRLRGISwKDEARvvKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIG 2203
Cdd:cd03262 76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMS-KAEAE--ERALELLEkvgLADKADAYPAQLSGGQQQRVAIARALAM 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2204 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03262 153 NPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1004-1200 |
1.50e-17 |
|
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: 83.50 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1004 KKLALNKLSLNL-YENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsaTIYGHDirTEMDEIRKNLGMCP---------QH 1073
Cdd:cd03297 8 KRLPDFTLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGG--TIVLNG--TVLFDSRKKINLPPqqrkiglvfQQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NVLFDRLTVEEHLWFysRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:cd03297 84 YALFPHLNVRENLAF--GLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 1154 VDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:cd03297 162 LDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
993-1206 |
1.57e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 84.68 E-value: 1.57e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMD-EIRKNLGMCP 1071
Cdd:PRK11231 5 TENLTVGYGT--KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSrQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRREMDKMiEDLELSNKRhslVQTLSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK11231 83 QHHLTPEGITVRElvaygrspWLSLWGRLSAEDNARVNQAMEQT-RINHLADRR---LTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTP 222
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1007-1200 |
1.59e-17 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 84.29 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1079
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEkairlLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1158
Cdd:COG4161 97 LTVMENLIEAPcKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 1159 RRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG4161 177 TAQVVEIIRELSqTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
2071-2268 |
2.00e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 87.20 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQSLGYCPQCDALFDELTAREHL 2149
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVASVPQDTSLSFEFDVRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2150 QL-----YTRLRGISWKDEaRVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR 2223
Cdd:PRK09536 99 EMgrtphRSRFDTWTETDR-AAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDiNHQVR 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 2224 FLwNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:PRK09536 178 TL-ELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2070-2278 |
2.01e-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: 88.67 E-value: 2.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELL--QVQQSLGYCPQCDALFDElTARE 2147
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVD-LRDLDedDLRRRIAVVPQRPHLFDT-TLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HLQLyTRLRGiswkDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTG 2216
Cdd:COG4987 428 NLRL-ARPDA----TDEELWA-ALERVGLGDWLAAlPDGldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEG 501
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2217 MDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2278
Cdd:COG4987 502 LDAATEQALLADLLEALA-GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNG 561
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
990-1198 |
2.18e-17 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 84.68 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFP--PTSGS-ATIYGHDIRTE---MDEI 1063
Cdd:PRK09984 4 IIRVEKLAKTFNQHQ--ALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdKSAGShIELLGRTVQREgrlARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1064 RKN---LGMCPQHNVLFDRLTVEEHL----------------WFYSRLKSMAQEEIRRemdkmiedLELSNKRHSLVQTL 1124
Cdd:PRK09984 82 RKSranTGYIFQQFNLVNRLSVLENVligalgstpfwrtcfsWFTREQKQRALQALTR--------VGMVHFAHQRVSTL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1125 SGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:PRK09984 154 SGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLrdINQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
1008-1199 |
2.64e-17 |
|
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: 83.74 E-value: 2.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHL 1086
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLFDG-TIAENI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1087 WF--YSRLKSMAQEEIRR-EMDKMIEDLElsNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:cd03249 98 RYgkPDATDEEVEEAAKKaNIHDFIMSLP--DGYDTLVgergSQLSGGQKQRIAIARALLRNPKILLLDEATSALDAESE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 1160 RAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGK 1199
Cdd:cd03249 176 KLVQEALDRAMKGRTTIVIAHRLStirNA----DLIAVLQNGQ 214
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
993-1200 |
2.90e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.14 E-value: 2.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkdDKKL-----ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-------- 1059
Cdd:PRK13651 5 VKNIVKIF--NKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1060 -----------------MDEIRKNLGMCPQ--HNVLFDRlTVEEHLWFYSRLKSMAQEEIRREMDKMIE--DLELSNKRH 1118
Cdd:PRK13651 83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1119 SLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTHHMDEADLLGDRIAIISH 1197
Cdd:PRK13651 162 SPFE-LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNlNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
...
gi 45446740 1198 GKL 1200
Cdd:PRK13651 241 GKI 243
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
1003-1181 |
2.94e-17 |
|
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: 82.54 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRLTV 1082
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1083 EEHLWFYSRLKSMAQEEirremdKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1162
Cdd:cd03231 91 LENLRFWHADHSDEQVE------EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170 180
....*....|....*....|
gi 45446740 1163 WDLILKY-KPGRTILLSTHH 1181
Cdd:cd03231 165 AEAMAGHcARGGMVVLTTHQ 184
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
996-1200 |
3.27e-17 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 87.85 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHN 1074
Cdd:TIGR02203 336 VTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADyTLASLRRQVALVSQDV 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VLFDRlTVEEHLwFYSRLKSMAQEEIRREMdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAII 1146
Cdd:TIGR02203 416 VLFND-TIANNI-AYGRTEQADRAEIERAL-AAAYAQDFVDKLPLGLDTpigengvlLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1147 LDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIE-KADRIVVMDDGRI 545
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
993-1200 |
3.30e-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: 81.49 E-value: 3.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1071
Cdd:cd03246 3 VENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDrltveehlwfysrlKSMAqEEIrremdkmiedlelsnkrhslvqtLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:cd03246 83 QDDELFS--------------GSIA-ENI-----------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1152 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMdEADLLGDRIAIISHGKL 1200
Cdd:cd03246 125 SHLDVEGERALNQAIAALKaAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2050-2269 |
3.60e-17 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.52 E-value: 3.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG----HSVLKELlq 2125
Cdd:PRK11231 2 TLRTENLTVGYGTKRI-----LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDkpisMLSSRQL-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 vQQSLGYCPQCDALFDELTARE--------HLQLYTRLrgiSWKDEARVvKWALEKLELTKYADKPAGTYSGGNKRKLST 2197
Cdd:PRK11231 75 -ARRLALLPQHHLTPEGITVRElvaygrspWLSLWGRL---SAEDNARV-NQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2198 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGT 221
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
980-1206 |
3.64e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 84.90 E-value: 3.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 980 MEEEPTHLPLVVCVDKLTKVYkDDKK----LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI---- 1051
Cdd:PRK13631 11 KVPNPLSDDIILRVKNLYCVF-DEKQenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1052 YGHDIRTEMD-------------EIRKNLGMC---PQHNVLFDrlTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSN 1115
Cdd:PRK13631 90 IGDKKNNHELitnpyskkiknfkELRRRVSMVfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1116 ---KRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDR 1191
Cdd:PRK13631 168 sylERSPF--GLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVLEVADE 245
|
250
....*....|....*
gi 45446740 1192 IAIISHGKLKCCGSP 1206
Cdd:PRK13631 246 VIVMDKGKILKTGTP 260
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
2050-2264 |
4.44e-17 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 84.72 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL----KE 2122
Cdd:COG0444 1 LLEVRNLKVYFPTRR-GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGllpPPGITSGEILFDGEDLLklseKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 LLQV-QQSLGYCPQcDAL------------FDElTAREHlqlytrlRGISWKD-EARVVKwALEKLELT---KYADKPAG 2185
Cdd:COG0444 80 LRKIrGREIQMIFQ-DPMtslnpvmtvgdqIAE-PLRIH-------GGLSKAEaRERAIE-LLERVGLPdpeRRLDRYPH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2186 TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1011-1180 |
5.52e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 81.84 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGmcpQHNVLFDRLTVEEHLWFY 1089
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG---HRNAMKPALTVAENLEFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1090 SRLKSMAQEEIrremDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY 1169
Cdd:PRK13539 98 AAFLGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|..
gi 45446740 1170 -KPGRTILLSTH 1180
Cdd:PRK13539 174 lAQGGIVIAATH 185
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2026-2278 |
6.48e-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: 87.58 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2026 KPVEDDVDVASERQRVLRGDadndmVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDE 2105
Cdd:COG2274 454 LPPEREEGRSKLSLPRLKGD-----IELENVSFRYPGDSP---PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLY 525
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2106 STTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREHLQLytrlrGISWKDEARVVkWALEKLELTKYADK-P 2183
Cdd:COG2274 526 EPTSGRILIDGIDLRQiDPASLRRQIGVVLQDVFLFSG-TIRENITL-----GDPDATDEEII-EAARLAGLHDFIEAlP 598
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2184 AG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMeECEALC 2253
Cdd:COG2274 599 MGydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRL-STIRLA 676
|
250 260
....*....|....*....|....*
gi 45446740 2254 TRLAIMVNGRLRCLGSIQHLKNRFG 2278
Cdd:COG2274 677 DRIIVLDKGRIVEDGTHEELLARKG 701
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1005-1198 |
8.64e-17 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 82.44 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1005 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEirknLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK11248 14 KPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAE----RGVVFQNEGLLPWRNVQD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWD 1164
Cdd:PRK11248 90 NVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQT 169
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446740 1165 LILK--YKPGRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:PRK11248 170 LLLKlwQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2051-2278 |
1.03e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 87.10 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KELLQVQQ 2128
Cdd:NF033858 2 ARLEGVSHRY-----GKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAdaRHRRAVCP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQC--DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2206
Cdd:NF033858 77 RIAYMPQGlgKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2207 FIFLDEPTTGMDPKARRFLWNLIlDLIKTGR---SVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2278
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELI-DRIRAERpgmSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTG 229
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
994-1201 |
1.37e-16 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 82.17 E-value: 1.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 994 DKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGhdirtEMDEIRKNLGMCPQh 1073
Cdd:PRK13546 26 DALIPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQ- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 nvlfdrLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP-TA 1152
Cdd:PRK13546 100 ------LTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAlSV 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1153 GVDPYARRAIwDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:PRK13546 174 GDQTFAQKCL-DKIYEFKeQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
1084-1226 |
1.38e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 84.02 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 EHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1163
Cdd:NF000106 105 ENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVW 184
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1164 DLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFLKGTYGDgyrLTLVKRPA 1226
Cdd:NF000106 185 DEVRSMvRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGG---RTLQIRPA 245
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2047-2264 |
1.56e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.44 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2047 DNDMVKIENLTKVYKSRKIG-RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE--L 2123
Cdd:PRK13633 1 MNEMIKCKNVSYKYESNEEStEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEenL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQVQQSLGYCPQ------CDALFDELTA--REHLqlytrlrGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKL 2195
Cdd:PRK13633 81 WDIRNKAGMVFQnpdnqiVATIVEEDVAfgPENL-------GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2196 STAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECeALCTRLAIMVNGRL 2264
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKV 222
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
998-1217 |
1.90e-16 |
|
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: 79.88 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 998 KVYKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFP---PTSGSATIYGHDIrTEM--DEI-RKNLGMCP 1071
Cdd:cd03217 7 HVSVGGKEI-LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPkyeVTEGEILFKGEDI-TDLppEERaRLGIFLAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLwfysrlksmaqeeirREMDKmiedlelsnkrhslvqTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:cd03217 84 QYPPEIPGVKNADFL---------------RYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1152 AGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLL-GDRIAIISHGKLKCCGSPLFLKGTYGDGY 1217
Cdd:cd03217 133 SGLDIDALRLVAEVINKLReEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALEIEKKGY 200
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1007-1206 |
1.95e-16 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 85.24 E-value: 1.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIR--------KNLGMCPQHNVLFD 1078
Cdd:TIGR03269 299 AVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRVGDEWVDMTKPGpdgrgrakRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RLTVEEHLwfysrLKSMAQeEIRREMDKM----------IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:TIGR03269 379 HRTVLDNL-----TEAIGL-ELPDELARMkavitlkmvgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILD 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1149 EPTAGVDPYARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:TIGR03269 453 EPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1007-1200 |
2.61e-16 |
|
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: 85.56 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1085
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYLPQEPYIFSG-SILEN 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1086 LWFYSRLKSMAQE--------EIRREMDKMIEDLELSNKRHSlvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:TIGR01193 568 LLLGAKENVSQDEiwaaceiaEIKDDIENMPLGYQTELSEEG--SSISGGQKQRIALARALLTDSKVLILDESTSNLDTI 645
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 1158 ARRAIWDLILKYKPgRTILLSTHHMDEADLLgDRIAIISHGKL 1200
Cdd:TIGR01193 646 TEKKIVNNLLNLQD-KTIIFVAHRLSVAKQS-DKIIVLDHGKI 686
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
980-1200 |
3.29e-16 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.85 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 980 MEEEPTHLPLVVCVDKLTkVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTT---TMSILTGLFPP--TSGSATIYGH 1054
Cdd:COG1117 1 MTAPASTLEPKIEVRNLN-VYYGDKQ-ALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMNDLIPGarVEGEILLDGE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1055 DIRT-EMD--EIRKNLGMCPQH----------NVLFD-RLtveeHlwfysRLKSmaqeeiRREMDKMIEDL--------E 1112
Cdd:COG1117 79 DIYDpDVDvvELRRRVGMVFQKpnpfpksiydNVAYGlRL----H-----GIKS------KSELDEIVEESlrkaalwdE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1113 LSNKRHSLVQTLSGGMKRKLSVAiafvggsRAI------IL-DEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEA 1185
Cdd:COG1117 144 VKDRLKKSALGLSGGQQQRLCIA-------RALavepevLLmDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQA 216
|
250
....*....|....*
gi 45446740 1186 DLLGDRIAIISHGKL 1200
Cdd:COG1117 217 ARVSDYTAFFYLGEL 231
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
1007-1186 |
3.66e-16 |
|
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: 84.26 E-value: 3.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEH 1085
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAWVPQHPFLFAG-TIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1086 LWFYSRLKS--MAQEEIRR-EMDKMIEDLELSnkRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1158
Cdd:TIGR02857 416 IRLARPDASdaEIREALERaGLDEFVAALPQG--LDTPIgeggAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAET 493
|
170 180 190
....*....|....*....|....*....|.
gi 45446740 1159 RRAIWDLILKYKPGRTILLSTH---HMDEAD 1186
Cdd:TIGR02857 494 EAEVLEALRALAQGRTVLLVTHrlaLAALAD 524
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2050-2269 |
3.83e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 81.32 E-value: 3.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTG----GEAFVNGHSVLKELL 2124
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLlQPTEGkvtvGDIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISwKDEARvvKWALEKLELT----KYADKPAGTYSGGNKRKLSTA 2198
Cdd:PRK13643 81 PVRKKVGVVFQFpeSQLFEE-TVLKDVAFGPQNFGIP-KEKAE--KIAAEKLEMVgladEFWEKSPFELSGGQMRRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2199 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK13643 157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGT 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2073-2244 |
4.35e-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: 79.07 E-value: 4.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2073 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLY 2152
Cdd:cd03231 18 GLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLRFW 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TRLRGiswkDEArvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2232
Cdd:cd03231 98 HADHS----DEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGH 171
|
170
....*....|..
gi 45446740 2233 IKTGRSVVLTSH 2244
Cdd:cd03231 172 CARGGMVVLTTH 183
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
2054-2298 |
4.61e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 83.16 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2054 ENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQVQ-Q 2128
Cdd:PRK10070 27 QGLSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaELREVRrK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFI 2208
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2209 FLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMIT--- 2284
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTffr 266
|
250
....*....|....*
gi 45446740 2285 -VRTKSSQSVKDVVR 2298
Cdd:PRK10070 267 gVDISQVFSAKDIAR 281
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
993-1200 |
5.72e-16 |
|
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: 80.26 E-value: 5.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE------ 1062
Cdd:TIGR02323 6 VSGLSKSYGGGK--GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAElelyQLSEaerrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1063 IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQE---EIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIAF 1138
Cdd:TIGR02323 84 MRTEWGFVHQNPRDGLRMRVSAGANIGERLMAIGARhygNIRATAQDWLEEVEIDPTRiDDLPRAFSGGMQQRLQIARNL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1139 VGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:TIGR02323 164 VTRPRLVFMDEPTGGLDVSVQARLLDLLrgLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRV 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1011-1200 |
5.78e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 80.27 E-value: 5.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDIRTE-MD--EIRKNLGMCPQHNVLFDRLTV 1082
Cdd:PRK14267 23 VDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSPdVDpiEVRREVGMVFQYPNPFPHLTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1083 EEHLWFYSRLKSMAQEeiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:PRK14267 103 YDNVAIGVKLNGLVKS--KKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANI 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1155 DPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK14267 181 DPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
2079-2244 |
7.16e-16 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 84.51 E-value: 7.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2079 RPGECFGLLGVNGAGKTSTFKMLTGDEstTGGeaFVNGHSVLKELLQVQQSL----GYCPQCDALFDELTAREHLQLYTR 2154
Cdd:PLN03140 904 RPGVLTALMGVSGAGKTTLMDVLAGRK--TGG--YIEGDIRISGFPKKQETFarisGYCEQNDIHSPQVTVRESLIYSAF 979
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2155 LR---GISWKDEARVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2226
Cdd:PLN03140 980 LRlpkEVSKEEKMMFVDEVMELVELDNLKDAIVGLpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVM 1059
|
170
....*....|....*...
gi 45446740 2227 NLILDLIKTGRSVVLTSH 2244
Cdd:PLN03140 1060 RTVRNTVDTGRTVVCTIH 1077
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
2085-2276 |
8.47e-16 |
|
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: 81.70 E-value: 8.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2085 GLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhSVLKE------LLQVQQSLGYCPQCDALFDELTAREHLQL-YTRLRG 2157
Cdd:TIGR02142 27 AIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG-RTLFDsrkgifLPPEKRRIGYVFQEARLFPHLSVRGNLRYgMKRARP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2158 iswkdEARVVKWA--LEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARR----FLWNLILD 2231
Cdd:TIGR02142 106 -----SERRISFErvIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYeilpYLERLHAE 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 2232 LiktGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2276
Cdd:TIGR02142 181 F---GIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2048-2273 |
9.01e-16 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 81.30 E-value: 9.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQvQ 2127
Cdd:PRK11432 4 KNFVVLKNITKRF-----GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2207
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIKtgrSVVLTS----HSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:PRK11432 158 LLFDEPLSNLDANLRRSMREKIRELQQ---QFNITSlyvtHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2051-2263 |
1.40e-15 |
|
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: 76.65 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2129
Cdd:cd03228 1 IEFKNVSFSYPGRPK---PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDElTAREHLqlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:cd03228 78 IAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECEaLCTRLAIMVNGR 2263
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2050-2281 |
1.41e-15 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 79.29 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVLKE---- 2122
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA--LHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGlitGDKSAGSHIELLGRTVQREgrla 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 --LLQVQQSLGYCPQCDALFDELTAREHLQL---------YTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGN 2191
Cdd:PRK09984 79 rdIRKSRANTGYIFQQFNLVNRLSVLENVLIgalgstpfwRTCFSWFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSS 237
|
250
....*....|..
gi 45446740 2271 QHLKN-RFGDGY 2281
Cdd:PRK09984 238 QQFDNeRFDHLY 249
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2047-2264 |
1.54e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 79.26 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2047 DNDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKtSTF-KMLTGDESTTGGEAFVNGHSVLKE-LL 2124
Cdd:PRK13632 4 KSVMIKVENVSFSYPNSEN---NALKNVSFEINEGEYVAILGHNGSGK-STIsKILTGLLKPQSGEIKIDGITISKEnLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 QVQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIG 2203
Cdd:PRK13632 80 EIRKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2204 YPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2264
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEA-ILADKVIVFSEGKL 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1008-1206 |
1.88e-15 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 78.21 E-value: 1.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---TEMDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK09493 17 LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpkVDERLIRQEAGMVFQQFYLFPHLTALE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR---- 1159
Cdd:PRK09493 97 NVMFGPlRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRhevl 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1160 RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK09493 177 KVMQDLA---EEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDP 220
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
991-1199 |
2.44e-15 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 75.18 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsatiyghdirtemdeirknlgmc 1070
Cdd:cd03221 1 IELENLSKTY-GGKLL-LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEG----------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 pqhnvlfdrlTVEEHlwfysrlksmaqeeirremdkmiedlelSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:cd03221 56 ----------IVTWG----------------------------STVKIGYFEQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1151 TAGVDPYARRAIWDLILKYKpgRTILLSTHhmDEA--DLLGDRIAIISHGK 1199
Cdd:cd03221 98 TNHLDLESIEALEEALKEYP--GTVILVSH--DRYflDQVATKIIELEDGK 144
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2076-2265 |
2.63e-15 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 77.51 E-value: 2.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ---QSLGYCPQCDALFDELTAREHLQ 2150
Cdd:PRK10584 31 LVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqMDEEARAKlraKHVGFVFQSFMLIPTLNALENVE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2151 LYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2230
Cdd:PRK10584 111 LPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLF 190
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446740 2231 DLIKT-GRSVVLTSHSmEECEALCTRLAIMVNGRLR 2265
Cdd:PRK10584 191 SLNREhGTTLILVTHD-LQLAARCDRRLRLVNGQLQ 225
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2050-2264 |
2.97e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 81.23 E-value: 2.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKEllqvqq 2128
Cdd:COG3845 5 ALELRGITKRF-----GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVrIRS------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 slgycPQcDA-------------LFDELTAREHLQLY---TRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNK 2192
Cdd:COG3845 74 -----PR-DAialgigmvhqhfmLVPNLTVAENIVLGlepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2193 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG3845 148 QRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKV 219
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2050-2263 |
3.67e-15 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 77.09 E-value: 3.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIG--RILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVN-GHSVL------ 2120
Cdd:COG4778 4 LLEVENLSKTFTLHLQGgkRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVdlaqas 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2121 -KELLQV-QQSLGYC-------PQCDALfdELTArEHLqlytRLRGISwKDEARV-VKWALEKLEL-TKYADKPAGTYSG 2189
Cdd:COG4778 84 pREILALrRRTIGYVsqflrviPRVSAL--DVVA-EPL----LERGVD-REEARArARELLARLNLpERLWDLPPATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2190 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1008-1200 |
4.43e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.82 E-value: 4.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMD----------EIRKN----LGMCP 1071
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvtRSPQDglangivyisEDRKRdglvLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVlfdRLTVEEHLwfysrlkSMAQEEIRREMDKM-IED-LELSN-KRHSLVQT---LSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:PRK10762 348 KENM---SLTALRYF-------SRAGGSLKHADEQQaVSDfIRLFNiKTPSMEQAiglLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1146 ILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEadLLG--DRIAIISHGKL 1200
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPE--VLGmsDRILVMHEGRI 473
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1008-1200 |
5.04e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 77.26 E-value: 5.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLF-----PPTSGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDRLT 1081
Cdd:PRK14247 19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIfKMDVIELRRRVQMVFQIPNPIPNLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEEHLWFYSRLKSMA------QEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK14247 99 IFENVALGLKLNRLVkskkelQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLD 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 1156 PYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK14247 179 PENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
2050-2264 |
5.91e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 5.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYksrkIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQ 2125
Cdd:PRK10908 1 MIRFEHVSKAY----LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlknrEVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
1006-1193 |
6.12e-15 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 77.13 E-value: 6.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1006 LALNKLSLNLYENQVVSFLGHNGAGKTTTMSI---LTGLFPP--TSGSATIYGHDIR-TEMD--EIRKNLGMCPQHNVLF 1077
Cdd:PRK14243 24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCfnrLNDLIPGfrVEGKVTFHGKNLYaPDVDpvEVRRRIGMVFQKPNPF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRlTVEEHLWFYSRLKSMaqeeiRREMDKMIEDL--------ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:PRK14243 104 PK-SIYDNIAYGARINGY-----KGDMDELVERSlrqaalwdEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 1150 PTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIA 1193
Cdd:PRK14243 178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTA 221
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2049-2312 |
6.48e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 77.46 E-value: 6.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2049 DMVKIENLTKVYKSRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQ 2127
Cdd:PRK13650 3 NIIEVKNLTFKYKEDQEKYTL--NDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2206
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2207 FIFLDEPTTGMDPKARrflwnliLDLIKTGRS--------VVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFG 2278
Cdd:PRK13650 161 IIILDEATSMLDPEGR-------LELIKTIKGirddyqmtVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
250 260 270
....*....|....*....|....*....|....
gi 45446740 2279 DGYMITVRTKSSQSVKDVVRFFNRNFPEAMLKER 2312
Cdd:PRK13650 233 DLLQLGLDIPFTTSLVQSLRQNGYDLPEGYLTEK 266
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1004-1206 |
6.88e-15 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 78.61 E-value: 6.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1004 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDEIRKNLGMCPQHNVLFDRLTVE 1083
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-THRSIQQRDICMVFQSYALFPHMSLG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 EHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIW 1163
Cdd:PRK11432 97 ENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRRSMR 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 1164 DLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK11432 177 EKIreLQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
993-1200 |
8.76e-15 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 8.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTkVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMD--EIRKnLGMC 1070
Cdd:COG3845 260 VENLS-VRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDI-TGLSprERRR-LGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 -----PQHNVLFDRLTVEEHLWF-------YSRLKSMAQEEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRKLSVAIA 1137
Cdd:COG3845 337 yipedRLGRGLVPDMSVAENLILgryrrppFSRGGFLDRKAIRAFAEELIEEFDVRTPGpDTPARSLSGGNQQKVILARE 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1138 FVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:COG3845 417 LSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILALSDRIAVMYEGRI 480
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1007-1206 |
9.58e-15 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 76.21 E-value: 9.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDE-----IRKNLGMCPQHNVLFDR 1079
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkaireLRRNVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLWFYS-RLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA 1158
Cdd:PRK11124 97 LTVQQNLIEAPcRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1159 RRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIA------IISHGKLKCCGSP 1206
Cdd:PRK11124 177 TAQIVSIIRELaETGITQVIVTHEVEVARKTASRVVymenghIVEQGDASCFTQP 231
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1000-1205 |
1.12e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.87 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE--IRKNLGMCPQHNVLF 1077
Cdd:PRK11160 348 YPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYSEaaLRQAISVVSQRVHLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRlTVEEHLwfysrlkSMAQEEIRREmdKMIEDLE---LSNkrhsLVQT--------------LSGGMKRKLSVAIAFVG 1140
Cdd:PRK11160 427 SA-TLRDNL-------LLAAPNASDE--ALIEVLQqvgLEK----LLEDdkglnawlgeggrqLSGGEQRRLGIARALLH 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTH------HMdeadllgDRIAIISHGKLKCCGS 1205
Cdd:PRK11160 493 DAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHrltgleQF-------DRICVMDNGQIIEQGT 556
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
1010-1206 |
1.14e-14 |
|
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: 78.23 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1010 KLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-----RKNLGMCPQHNVLFDRLTVEE 1084
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLwFYSRLKSMAQEEIRREmDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD--------P 1156
Cdd:TIGR02142 95 NL-RYGMKRARPSERRISF-ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDdprkyeilP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1157 YARRaiwdliLKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:TIGR02142 173 YLER------LHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPI 216
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2070-2283 |
1.22e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 76.81 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYCPQC--DALFDElT 2144
Cdd:PRK13636 21 ALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDpdNQLFSA-S 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2145 AREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2224
Cdd:PRK13636 100 VYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2225 LWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLknrFGDGYMI 2283
Cdd:PRK13636 180 IMKLLVEMQKeLGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEV---FAEKEML 236
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
2074-2245 |
2.33e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2074 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkELLQVQQSLGYCPQCDALFDELTAREHLQLYT 2153
Cdd:PRK13539 21 LSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYLGHRNAMKPALTVAENLEFWA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2154 RLRGiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY-PAFIfLDEPTTGMDPKARRFLWNLILDL 2232
Cdd:PRK13539 99 AFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNrPIWI-LDEPTAALDAAAVALFAELIRAH 173
|
170
....*....|...
gi 45446740 2233 IKTGRSVVLTSHS 2245
Cdd:PRK13539 174 LAQGGIVIAATHI 186
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2063-2263 |
2.43e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 78.33 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2063 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGHSVLKELLQVQQSLGYC--PQCDA 2138
Cdd:TIGR02633 9 KTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvyPHGTWDGEIYWSGSPLKASNIRDTERAGIViiHQELT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2139 LFDELTAREHLQLYTR--LRGISWKDEARVVKWA--LEKLELTKYAD-KPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2213
Cdd:TIGR02633 89 LVPELSVAENIFLGNEitLPGGRMAYNAMYLRAKnlLRELQLDADNVtRPVGDYGGGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 2214 TTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:TIGR02633 169 SSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2050-2264 |
2.56e-14 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 75.61 E-value: 2.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKS----RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---- 2121
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQldrk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2122 ------ELLQV--QQSLG-YCPQCDAlfdELTAREHLQLYTRLrgiswkDEARVVKWALEKLEL----TKYADKPAGTYS 2188
Cdd:TIGR02769 82 qrrafrRDVQLvfQDSPSaVNPRMTV---RQIIGEPLRHLTSL------DESEQKARIAELLDMvglrSEDADKLPRQLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2189 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:TIGR02769 153 GGQLQRINIARALAVKPKLIVLDEAVSNLD----MVLQAVILELLRKlqqafGTAYLFITHDLRLVQSFCQRVAVMDKGQ 228
|
.
gi 45446740 2264 L 2264
Cdd:TIGR02769 229 I 229
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2068-2264 |
3.05e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.03 E-value: 3.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2068 ILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ-----VQQSLGYCPqcda 2138
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfasTTAALAagvaiIYQELHLVP---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2139 lfdELTAREHL---QLYTRLrgiSWKDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2212
Cdd:PRK11288 93 ---EMTVAENLylgQLPHKG---GIVNRRLLNYEAREQLEhlgVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2213 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK11288 167 PTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2069-2264 |
3.95e-14 |
|
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: 72.73 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2069 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDElTAREH 2148
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQRPYLFDT-TLRNN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2149 LQlyTRLrgiswkdearvvkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNL 2228
Cdd:cd03247 95 LG--RRF--------------------------------SGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSL 140
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446740 2229 ILDLIKtGRSVVLTSHSMEECEALcTRLAIMVNGRL 2264
Cdd:cd03247 141 IFEVLK-DKTLIWITHHLTGIEHM-DKILFLENGKI 174
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1007-1199 |
4.13e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE--MDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNgpKSSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLW----FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:PRK10762 99 NIFlgreFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETE 178
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 1161 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:PRK10762 179 SLFRVIRELKSqGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| ABC2_membrane_3 |
pfam12698 |
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ... |
707-913 |
4.54e-14 |
|
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: 76.27 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 707 MMPLCMVISWVYSVAMTIQHIVAEKEHRLKEVMKTMGLNNAVHWVAWFITGFVqLSISVTALTAILKYGQVLMHSHVVII 786
Cdd:pfam12698 163 LVGLILMIIILIGAAIIAVSIVEEKESRIKERLLVSGVSPLQYWLGKILGDFL-VGLLQLLIILLLLFGIGIPFGNLGLL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 787 WLFLAVYAVATIMFCFLVSVLYSKAKLASACGGIIYFLSYVPYMYVAIREEVAHdkitaFEKCIASLMSTTAFGLGSKYF 866
Cdd:pfam12698 242 LLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDPPS-----FLQWIFSIIPFFSPIDGLLRL 316
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 867 ALYEVAgvgiqwhtfsqspvegddFNLLLAVTMLMVDAVVYGILTWY 913
Cdd:pfam12698 317 IYGDSL------------------WEIAPSLIILLLFAVVLLLLALL 345
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2071-2264 |
4.64e-14 |
|
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: 72.25 E-value: 4.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREHL 2149
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLPQDDELFSG-SIAENI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2150 qlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2229
Cdd:cd03246 97 -------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAI 139
|
170 180 190
....*....|....*....|....*....|....*
gi 45446740 2230 LDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRL 2264
Cdd:cd03246 140 AALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2028-2264 |
4.88e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 77.37 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2028 VEDDVDVASERQRVLRGDAdndMVKIENLTkVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST 2107
Cdd:COG3845 238 VGREVLLRVEKAPAEPGEV---VLEVENLS-VRDDRGV---PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2108 TGGEAFVNGHSVL----KELLQvqQSLGYCP---QCDALFDELTAREHLQL-------YTRLRGISWKdeaRVVKWALEK 2173
Cdd:COG3845 311 ASGSIRLDGEDITglspRERRR--LGVAYIPedrLGRGLVPDMSVAENLILgryrrppFSRGGFLDRK---AIRAFAEEL 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2174 LEltKY------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2247
Cdd:COG3845 386 IE--EFdvrtpgPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLD 463
|
250
....*....|....*..
gi 45446740 2248 ECEALCTRLAIMVNGRL 2264
Cdd:COG3845 464 EILALSDRIAVMYEGRI 480
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1001-1181 |
5.22e-14 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 5.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDRL 1080
Cdd:PRK13538 11 RDERIL-FSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTEL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLWFYSRLKSMAQEeirremDKMIEDLE---LSNKRHSLVQTLSGGMKRKlsVAIA--FVGGSRAIILDEP----- 1150
Cdd:PRK13538 90 TALENLRFYQRLHGPGDD------EALWEALAqvgLAGFEDVPVRQLSAGQQRR--VALArlWLTRAPLWILDEPftaid 161
|
170 180 190
....*....|....*....|....*....|.
gi 45446740 1151 TAGVDPYARRaiwdLILKYKPGRTILLSTHH 1181
Cdd:PRK13538 162 KQGVARLEAL----LAQHAEQGGMVILTTHQ 188
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2051-2277 |
6.36e-14 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 76.14 E-value: 6.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---ELLQVQ 2127
Cdd:PRK09452 15 VELRGISKSFDGKEV-----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHvpaENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 ---QSlgYcpqcdALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK09452 90 tvfQS--Y-----ALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNK 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRF 2277
Cdd:PRK09452 163 PKVLLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIyeepKNLF 240
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
984-1200 |
6.77e-14 |
|
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: 73.27 E-value: 6.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 984 PTHLPLVVCVDKLTKVYKD-DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMD 1061
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 EIRKNLGMCPQHNVLFDRlTVEEHLWFysRLKSMAQEEIRREMDK-----MIEDLEL-----SNKRHSLvqtLSGGMKRK 1131
Cdd:cd03248 85 YLHSKVSLVGQEPVLFAR-SLQDNIAY--GLQSCSFECVKEAAQKahahsFISELASgydteVGEKGSQ---LSGGQKQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1132 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:cd03248 159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVE-RADQILVLDGGRI 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
2076-2270 |
8.61e-14 |
|
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: 73.27 E-value: 8.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---ELLQVQQSLgycpqcdALFDELTAREHLQLY 2152
Cdd:TIGR01184 6 LTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNY-------SLLPWLTVRENIALA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TR--LRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2230
Cdd:TIGR01184 79 VDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEELM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45446740 2231 DLIKTGR-SVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:TIGR01184 159 QIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQI 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
993-1201 |
9.16e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 76.64 E-value: 9.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATiyghdirtemdeIRKNL--GMC 1070
Cdd:COG0488 1 LENLSKSF-GGRPL-LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVS------------IPKGLriGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNVLFDRLTVEEHLW--FYSRLKSMAQ-EEIRREMDKMIEDL----ELSNK--------------------------R 1117
Cdd:COG0488 67 PQEPPLDDDLTVLDTVLdgDAELRALEAElEELEAKLAEPDEDLerlaELQEEfealggweaearaeeilsglgfpeedL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1118 HSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRaiW--DLILKYkPGrTILLSTH--H-MDEadlLGDRI 1192
Cdd:COG0488 147 DRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIE--WleEFLKNY-PG-TVLVVSHdrYfLDR---VATRI 219
|
....*....
gi 45446740 1193 AIISHGKLK 1201
Cdd:COG0488 220 LELDRGKLT 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2081-2275 |
9.45e-14 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 73.12 E-value: 9.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2081 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKELLQVQQSLGYCPQCDALFDELTAREHL-QLY 2152
Cdd:PRK11124 28 GETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsktpsDKAIRELRRNVGMVFQQYNLWPHLTVQQNLiEAP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2231
Cdd:PRK11124 108 CRVLGLS-KDQALArAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 2232 LIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:PRK11124 187 LAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQ 230
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1007-1200 |
9.47e-14 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 76.49 E-value: 9.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR--TEMDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK11288 19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfaSTTAALAAGVAIIYQELHLVPEMTVAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLW---FYSRL----KSMAQEEIRREMDKMIEDLELSNKrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpy 1157
Cdd:PRK11288 99 NLYlgqLPHKGgivnRRLLNYEAREQLEHLGVDIDPDTP----LKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS-- 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 1158 AR------RAIWDLilkYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11288 173 AReieqlfRVIREL---RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2050-2263 |
1.00e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKE----- 2122
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEykrak 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 -LLQVQQ--SLGYCPqcdalfdELTAREHLQL-YTR--LRGISW---KDEARVVKWALEKLE--LTKYADKPAGTYSGGN 2191
Cdd:COG1101 81 yIGRVFQdpMMGTAP-------SMTIEENLALaYRRgkRRGLRRgltKKRRELFRELLATLGlgLENRLDTKVGLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRsvvLTS----HSMEECEALCTRLAIMVNGR 2263
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENN---LTTlmvtHNMEQALDYGNRLIMMHEGR 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2051-2244 |
1.14e-13 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 70.17 E-value: 1.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAvdrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafVNGHSVLKellqvqqsL 2130
Cdd:cd03221 1 IELENLSKTYGGKLLLKDIS-----LTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVK--------I 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQcdalfdeltarehlqlytrlrgiswkdearvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:cd03221 66 GYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
|
170 180 190
....*....|....*....|....*....|....
gi 45446740 2211 DEPTTGMDPKARRFLWNLildLIKTGRSVVLTSH 2244
Cdd:cd03221 95 DEPTNHLDLESIEALEEA---LKEYPGTVILVSH 125
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2086-2273 |
1.18e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 73.68 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2086 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQVQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISWKD 2162
Cdd:PRK13652 35 VIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLVFQNpdDQIFSP-TVEQDIAFGPINLGLDEET 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2163 EARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVL 2241
Cdd:PRK13652 114 VAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIF 193
|
170 180 190
....*....|....*....|....*....|..
gi 45446740 2242 TSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:PRK13652 194 STHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2045-2273 |
1.18e-13 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 76.34 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2045 DADNDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELL 2124
Cdd:COG4988 331 AAGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVD-LSDLD 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 --QVQQSLGYCPQCDALFdELTAREHLQLYTRlrGISwkDEArvVKWALEKLELTKYADK-PAG----------TYSGGN 2191
Cdd:COG4988 406 paSWRRQIAWVPQNPYLF-AGTIRENLRLGRP--DAS--DEE--LEAALEAAGLDEFVAAlPDGldtplgeggrGLSGGQ 478
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQ 2271
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLALL-AQADRILVLDDGRIVEQGTHE 556
|
..
gi 45446740 2272 HL 2273
Cdd:COG4988 557 EL 558
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2080-2264 |
1.84e-13 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 72.35 E-value: 1.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2080 PGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKELLQVQQSLGYCPQCDALFDELTAREHL-QL 2151
Cdd:COG4161 27 SGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLRQKVGMVFQQYNLWPHLTVMENLiEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2152 YTRLRGISwKDEARV-VKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLIL 2230
Cdd:COG4161 107 PCKVLGLS-KEQAREkAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIR 185
|
170 180 190
....*....|....*....|....*....|....
gi 45446740 2231 DLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:COG4161 186 ELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1011-1206 |
1.90e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 72.88 E-value: 1.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMCPQHNVLFDRLTVEEHL 1086
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1087 WFYSRLKSMAQEEIRREMDKM-IEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDL 1165
Cdd:PRK11831 106 AYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 1166 I--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK11831 186 IseLNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2076-2264 |
2.05e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 73.24 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNG-----HSVLKELLQVQQSLGYCPQC--DALFDElTAREH 2148
Cdd:PRK13649 28 LTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitsTSKNKDIKQIRKKVGLVFQFpeSQLFEE-TVLKD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2149 LQLYTRLRGISwKDEArvVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2224
Cdd:PRK13649 107 VAFGPQNFGVS-QEEA--EALAREKLALVGISeslfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKE 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 2225 LWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK13649 184 LMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
2060-2272 |
2.20e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.33 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2060 YKSRKIGRI-LAVDRL---------CLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--KELLQVQ 2127
Cdd:PRK11288 248 YRPRPLGEVrLRLDGLkgpglrepiSFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDirSPRDAIR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQcDALFDELTA----REHLQLYTR---LRG---ISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGNKRK-- 2194
Cdd:PRK11288 328 AGIMLCPE-DRKAEGIIPvhsvADNINISARrhhLRAgclINNRWEAENADRFIRSLNIkTPSREQLIMNLSGGNQQKai 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2195 ----LSTAIALIgypafiFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRclGSI 2270
Cdd:PRK11288 407 lgrwLSEDMKVI------LLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA--GEL 478
|
..
gi 45446740 2271 QH 2272
Cdd:PRK11288 479 AR 480
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2045-2265 |
2.24e-13 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2045 DADNDMVKIENLTKVY-KSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGGEAFVNGHSV-LK 2121
Cdd:TIGR02633 252 EIGDVILEARNLTCWDvINPHRKR---VDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAyPGKFEGNVFINGKPVdIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2122 ELLQ-VQQSLGYCPQ---CDALFDELTAREH-----LQLYTRLRGISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGN 2191
Cdd:TIGR02633 329 NPAQaIRAGIAMVPEdrkRHGIVPILGVGKNitlsvLKSFCFKMRIDAAAELQIIGSAIQRLKVkTASPFLPIGRLSGGN 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2050-2271 |
2.46e-13 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 72.50 E-value: 2.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQ 2127
Cdd:PRK13548 2 MLEARNLSV-----RLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-LADWspAELA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDAL-FDeLTARE--HLQLYTrlRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI-- 2202
Cdd:PRK13548 76 RRRAVLPQHSSLsFP-FTVEEvvAMGRAP--HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2203 ----GYPAFIFLDEPTTGMDPK--------ARRFLWnlildliKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAhqhhvlrlARQLAH-------ERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTP 225
|
.
gi 45446740 2271 Q 2271
Cdd:PRK13548 226 A 226
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1019-1180 |
2.69e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.73 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1019 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIrTEMDE-----IR-KNLGMCPQHNVLFDRLTVEEHLWFYSRL 1092
Cdd:PRK10584 37 ETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPL-HQMDEearakLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1093 KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYK 1170
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLfsLNRE 195
|
170
....*....|
gi 45446740 1171 PGRTILLSTH 1180
Cdd:PRK10584 196 HGTTLILVTH 205
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
993-1200 |
2.99e-13 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 72.15 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVY-------KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMD 1061
Cdd:TIGR02769 5 VRDVTHTYrtgglfgAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLyqldRKQRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 EIRKNLGMCPQ--HNVLFDRLTVE----EHLWFYSRLKSMAQEEIRREMDKMIE-DLELSNKrhsLVQTLSGGMKRKLSV 1134
Cdd:TIGR02769 85 AFRRDVQLVFQdsPSAVNPRMTVRqiigEPLRHLTSLDESEQKARIAELLDMVGlRSEDADK---LPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1135 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLrkLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
1000-1193 |
3.28e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 71.99 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTS-----GSATIYGHDI---RTEMDEIRKNLGMC- 1070
Cdd:PRK14258 16 YYDTQKI-LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyerRVNLNRLRRQVSMVh 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQHNvLFDrLTVEEHLWFYSRLKSMAQeeiRREMDKMIE------DL--ELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:PRK14258 95 PKPN-LFP-MSVYDNVAYGVKIVGWRP---KLEIDDIVEsalkdaDLwdEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIA 1193
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIqsLRLRSELTMVIVSHNLHQVSRLSDFTA 222
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
993-1219 |
3.76e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 75.06 E-value: 3.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1071
Cdd:PRK11176 344 FRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNQVALVS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRlTVEEHLwFYSRLKSMAQEEIRREMdKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK11176 424 QNVHLFND-TIANNI-AYARTEQYSREQIEEAA-RMAYAMDFINKMDNGLDTvigengvlLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDEADlLGDRIAIISHGKLKCCGSP---LFLKGTYGDGYRL 1219
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIE-KADEILVVEDGEIVERGTHaelLAQNGVYAQLHKM 578
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1008-1206 |
4.25e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 73.72 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR-TEMDEIRKNLGMCPQHNVL---FD-RLTV 1082
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVPQDTSLsfeFDvRQVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1083 E----EHLwfySRLKSMAQEEiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDpyA 1158
Cdd:PRK09536 99 EmgrtPHR---SRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLD--I 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1159 RRAIWDLILKYK---PGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK09536 173 NHQVRTLELVRRlvdDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPP 223
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
2050-2251 |
4.52e-13 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 70.59 E-value: 4.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDES---TTGGEAFVNGHSVLKelLQV 2126
Cdd:COG4136 1 MLSLENLTITLGGRPL-----LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTA--LPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQ-SLGYCPQCDALFDELTAREHLQLYTRlRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:COG4136 74 EQrRIGILFQDDLLFPHLSVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 2206 AFIFLDEPTTGMDP----KARRFLWNLILDLiktGRSVVLTSHSMEECEA 2251
Cdd:COG4136 153 RALLLDEPFSKLDAalraQFREFVFEQIRQR---GIPALLVTHDEEDAPA 199
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1001-1200 |
5.67e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLalNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQH---NV 1075
Cdd:PRK09700 274 RDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESrrdNG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKS---------MAQEEIRREMDKMIEDLELsnKRHSLVQT---LSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK09700 352 FFPNFSIAQNMAISRSLKDggykgamglFHEVDEQRTAENQRELLAL--KCHSVNQNiteLSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLaDDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2038-2264 |
6.62e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.05 E-value: 6.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2038 RQRVLRGDADNDMVKIENLTkvykSRKIGRilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGH 2117
Cdd:PRK09700 253 MKENVSNLAHETVFEVRNVT----SRDRKK---VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2118 --SVLKELLQVQQSLGYCPQC---DALFDELTAREHLQLYTRLRGISWK---------DEARVVKWALEKLELTKYA-DK 2182
Cdd:PRK09700 326 diSPRSPLDAVKKGMAYITESrrdNGFFPNFSIAQNMAISRSLKDGGYKgamglfhevDEQRTAENQRELLALKCHSvNQ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2183 PAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2262
Cdd:PRK09700 406 NITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEG 485
|
..
gi 45446740 2263 RL 2264
Cdd:PRK09700 486 RL 487
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
996-1199 |
6.80e-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: 6.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY--GHDIRTE--MDEIRKNLGMCP 1071
Cdd:TIGR02633 7 IVKTFGGVK--ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPLKASniRDTERAGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLWFYSRL----KSMAQEEIRREMDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAII 1146
Cdd:TIGR02633 85 QELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALNKQARLLI 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1147 LDEPTAGVDPYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1199
Cdd:TIGR02633 165 LDEPSSSLTEKETEILLDIIrdLKAHGVACVYIS-HKLNEVKAVCDTICVIRDGQ 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
993-1237 |
8.33e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.98 E-value: 8.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKkLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1071
Cdd:PRK10790 343 IDNVSFAYRDDN-LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNV-----LFDRLTV-----EEHLWfySRLKSMAQEEIRREMDKMIEDL--ELSNkrhslvqTLSGGMKRKLSVAIAFV 1139
Cdd:PRK10790 422 QDPVvladtFLANVTLgrdisEEQVW--QALETVQLAELARSLPDGLYTPlgEQGN-------NLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1140 GGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKLKCCGSP---LFLKGTY 1213
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLStivEA----DTILVLHRGQAVEQGTHqqlLAAQGRY 568
|
250 260
....*....|....*....|....
gi 45446740 1214 GDGYRLTLVKRPAEPGGPQEPGLA 1237
Cdd:PRK10790 569 WQMYQLQLAGEELAASVREEESLS 592
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
2074-2247 |
8.93e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.19 E-value: 8.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2074 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQVQQSLGYC---PQCDALFDELTARE 2147
Cdd:PRK13638 20 LNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQIFYTDIDSDI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HLQLytRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2227
Cdd:PRK13638 100 AFSL--RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIA 177
|
170 180
....*....|....*....|
gi 45446740 2228 LILDLIKTGRSVVLTSHSME 2247
Cdd:PRK13638 178 IIRRIVAQGNHVIISSHDID 197
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
996-1209 |
9.51e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 72.37 E-value: 9.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKKLALNK-LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRteMDEI---RKNLGMCP 1071
Cdd:PRK11000 6 LRNVTKAYGDVVISKdINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD--LFIGEKR--MNDVppaERGVGMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:PRK11000 82 QSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1152 AGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1209
Cdd:PRK11000 162 SNLDAALRVQMRIEIsrLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
988-1189 |
1.24e-12 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 69.84 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 988 PLVVCvDKLTKVYKDDKKLA--LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1061
Cdd:PRK11629 4 ILLQC-DNLCKRYQEGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 EIRKN-LGMCPQHNVLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVG 1140
Cdd:PRK11629 83 ELRNQkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLG 1189
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLgeLNRLQGTAFLVVTHDLQLAKRMS 213
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2081-2262 |
1.25e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 70.68 E-value: 1.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2081 GECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELlqvQQSL-GYCPQ---CDALFDELTarEHLQLYTRLR 2156
Cdd:PRK15056 33 GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAYVPQseeVDWSFPVLV--EDVVMMGRYG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 GISW-----KDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2231
Cdd:PRK15056 108 HMGWlrrakKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE 187
|
170 180 190
....*....|....*....|....*....|.
gi 45446740 2232 LIKTGRSVVLTSHSMEECEALCTrLAIMVNG 2262
Cdd:PRK15056 188 LRDEGKTMLVSTHNLGSVTEFCD-YTVMVKG 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2066-2264 |
1.26e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 70.33 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2066 GRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-----DESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDAL 2139
Cdd:PRK14247 14 GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKmDVIELRRRVQMVFQIPNP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2140 FDELTAREHLQLYTRLRGI--SWKDEARVVKWALEKLEL----TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEP 2213
Cdd:PRK14247 94 IPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2214 TTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK14247 174 TANLDPENTAKIESLFLEL-KKDMTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
955-1201 |
1.42e-12 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 955 TPRLSVMEEDQACAMESRRfEETRGMEEEPTHLPLVVC-VDKLTKVYKDDKKLA-LNKLSLNLYENQVVSFLGHNGAGKT 1032
Cdd:TIGR02633 222 TKDMSTMSEDDIITMMVGR-EITSLYPHEPHEIGDVILeARNLTCWDVINPHRKrVDDVSFSLRRGEILGVAGLVGAGRT 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1033 TTMSILTGLFPPT-SGSATIYGH--DIRTEMDEIRKNLGMCPQ--------------HNVlfdRLTVEEHLWFYSRLKSM 1095
Cdd:TIGR02633 301 ELVQALFGAYPGKfEGNVFINGKpvDIRNPAQAIRAGIAMVPEdrkrhgivpilgvgKNI---TLSVLKSFCFKMRIDAA 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1096 AQEEIrreMDKMIEDLELSNKRHSL-VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGR 1173
Cdd:TIGR02633 378 AELQI---IGSAIQRLKVKTASPFLpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLaQEGV 454
|
250 260
....*....|....*....|....*...
gi 45446740 1174 TILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:TIGR02633 455 AIIVVSSELAEVLGLSDRVLVIGEGKLK 482
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2048-2276 |
1.45e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 70.53 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ-V 2126
Cdd:PRK13647 2 DNIIEVEDLHFRYKDGT----KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQC--DALFdELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK13647 78 RSKVGLVFQDpdDQVF-SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHLKNR 2276
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDE 228
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1006-1200 |
1.93e-12 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 69.23 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1006 LALNKLSLnLYENQVVSF------------LGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQH 1073
Cdd:PRK10771 2 LKLTDITW-LYHHLPMRFdltvergervaiLGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NVLFDRLTVEEH--LWFYSRLKSMAQEeiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:PRK10771 80 NNLFSHLTVAQNigLGLNPGLKLNAAQ--REKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1152 AGVDPYARRAIWDLILKYKPGR--TILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRI 208
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
982-1200 |
2.70e-12 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 69.32 E-value: 2.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 982 EEPTHL----PLVVcvDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGsATIYGhdiR 1057
Cdd:PRK11247 2 MNTARLnqgtPLLL--NAVSKRYGE--RTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAG-ELLAG---T 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1058 TEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFysRLKSMAQEEIRREMdkmiEDLELSNKRHSLVQTLSGGMKRKLSVAIA 1137
Cdd:PRK11247 74 APLAEAREDTRLMFQDARLLPWKKVIDNVGL--GLKGQWRDAALQAL----AAVGLADRANEWPAALSGGQKQRVALARA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1138 FVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIesLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
991-1182 |
3.42e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 69.14 E-value: 3.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 991 VCVDKLTKVYKDDKKlALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMdeiRKNL-GM 1069
Cdd:PRK15056 7 IVVNDVTVTWRNGHT-ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1070 CPQ-HNVLFDRLTVEEHLWFYSRLKSM-----AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK15056 83 VPQsEEVDWSFPVLVEDVVMMGRYGHMgwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQ 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHM 1182
Cdd:PRK15056 163 VILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNL 202
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2083-2264 |
3.51e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 69.10 E-value: 3.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2083 CFGLLGVNGAGKTS---TFKMLT--GDESTTGGEAFVNGHSVLKE---LLQVQQSLGYCPQCDALFDELTAREHLQLYTR 2154
Cdd:PRK14267 32 VFALMGPSGCGKSTllrTFNRLLelNEEARVEGEVRLFGRNIYSPdvdPIEVRREVGMVFQYPNPFPHLTIYDNVAIGVK 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2155 LRGI--SWKDEARVVKWALEKLEL-----TKYADKPaGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWN 2227
Cdd:PRK14267 112 LNGLvkSKKELDERVEWALKKAALwdevkDRLNDYP-SNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEE 190
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446740 2228 LILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK14267 191 LLFEL-KKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
2048-2264 |
4.18e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 68.37 E-value: 4.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlKELLQVQ 2127
Cdd:PRK11614 3 KVMLSFDKVSAHY-----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG----KDITDWQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 ------QSLGYCPQCDALFDELTAREHLQLytrlrGISWKDEARV---VKWALEKL-ELTKYADKPAGTYSGGNKRKLST 2197
Cdd:PRK11614 74 takimrEAVAIVPEGRRVFSRMTVEENLAM-----GGFFAERDQFqerIKWVYELFpRLHERRIQRAGTMSGGEQQMLAI 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2198 AIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK11614 149 GRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHV 215
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
2080-2244 |
4.36e-12 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.83 E-value: 4.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2080 PGECFGLLGVNGAGKTSTFKMLTGDESTTG--GEAFVNGHSVLKellQVQQSLGYCPQCDALFDELTAREHLQLYTRLR- 2156
Cdd:PLN03211 93 PGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKRTGFVTQDDILYPHLTVRETLVFCSLLRl 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 --GISWKDEARVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2229
Cdd:PLN03211 170 pkSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTL 249
|
170
....*....|....*
gi 45446740 2230 LDLIKTGRSVVLTSH 2244
Cdd:PLN03211 250 GSLAQKGKTIVTSMH 264
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
993-1200 |
4.64e-12 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 68.62 E-value: 4.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE---------MDEI 1063
Cdd:PRK11264 6 VKNLVKKFHGQT--VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1064 RKNLGMCPQHNVLFDRLTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGS 1142
Cdd:PRK11264 84 RQHVGFVFQNFNLFPHRTVLENIIEGPVIvKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1143 RAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11264 164 EVILFDEPTSALDPELVGEVLNTIRQLaQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
976-1204 |
5.01e-12 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 71.32 E-value: 5.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 976 ETRGMEEEPTHLP-----LVVcvDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT 1050
Cdd:COG4618 313 AAVPAEPERMPLPrpkgrLSV--ENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVR 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1051 IYGHDIRT-EMDEIRKNLGMCPQHNVLFDRlTVEEHLwfySRLKSMAQEEI-----RREMDKMIedLELSNKRHSLV--- 1121
Cdd:COG4618 391 LDGADLSQwDREELGRHIGYLPQDVELFDG-TIAENI---ARFGDADPEKVvaaakLAGVHEMI--LRLPDGYDTRIgeg 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1122 -QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKpGRTILLSTHHMdeaDLLG--DRIAIIS 1196
Cdd:COG4618 465 gARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIraLKAR-GATVVVITHRP---SLLAavDKLLVLR 540
|
....*...
gi 45446740 1197 HGKLKCCG 1204
Cdd:COG4618 541 DGRVQAFG 548
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
1011-1206 |
5.56e-12 |
|
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: 67.78 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGSATIYGHDIrTEMDEIRKNLGMCPQH-----NVLFdrlT 1081
Cdd:TIGR02770 5 LNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPL-LPLSIRGRHIATIMQNprtafNPLF---T 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEEH----LWFYSRLKSMAQEEIRREMDKM-IEDLELSNKRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1156
Cdd:TIGR02770 81 MGNHaietLRSLGKLSKQARALILEALEAVgLPDPEEVLKKYPF--QLSGGMLQRVMIALALLLEPPFLIADEPTTDLDV 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1157 YARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:TIGR02770 159 VNQARVLKLLreLRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTV 210
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2070-2245 |
7.12e-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: 70.47 E-value: 7.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDElTAREH 2148
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSVCAQDAHLFDT-TVREN 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2149 LQLytrLRGISWKDEARvvkWALEKLELTKY-ADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2217
Cdd:TIGR02868 429 LRL---ARPDATDEELW---AALERVGLADWlRALPDGldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTEHL 502
|
170 180
....*....|....*....|....*...
gi 45446740 2218 DPKARRFLWNLILDlIKTGRSVVLTSHS 2245
Cdd:TIGR02868 503 DAETADELLEDLLA-ALSGRTVVLITHH 529
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2071-2264 |
8.04e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 70.42 E-value: 8.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ--VQQSLGYCPQ---CDALFDELTA 2145
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYISEdrkRDGLVLGMSV 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2146 REHLQLyTRLRGISWKdeARVVKWALEKLELTKY----------ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2215
Cdd:PRK10762 348 KENMSL-TALRYFSRA--GGSLKHADEQQAVSDFirlfniktpsMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTR 424
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 2216 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK10762 425 GVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1002-1200 |
8.79e-12 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 8.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1002 DDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRl 1080
Cdd:PRK13657 345 DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLFNR- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLwfysRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQT--------LSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:PRK13657 424 SIEDNI----RVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTvvgergrqLSGGERQRLAIARALLKDPPILILDEAT 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1152 AGVDPYARRAIWDLILKYKPGRTILLSTHHMD---EAdllgDRIAIISHGKL 1200
Cdd:PRK13657 500 SALDVETEAKVKAALDELMKGRTTFIIAHRLStvrNA----DRILVFDNGRV 547
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1011-1200 |
9.01e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 9.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMC------PQHNVLFDR----- 1079
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylpedrQSSGLYLDAplawn 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 ---LTVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK15439 362 vcaLTHNRRGFWIKPARENAVlERYRRALNIKFNHAEQA------ARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1156 PYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK15439 436 VSARNDIYQLIRSIaAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2051-2272 |
1.03e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 68.32 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL-----KELLQ 2125
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQC--DALFDElTAREHLQLYTRLRGISwKDEAR--VVKWaLEKLEL-TKYADKPAGTYSGGNKRKLSTAIA 2200
Cdd:PRK13641 83 LRKKVSLVFQFpeAQLFEN-TVLKDVEFGPKNFGFS-EDEAKekALKW-LKKVGLsEDLISKSPFELSGGQMRRVAIAGV 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLrclgsIQH 2272
Cdd:PRK13641 160 MAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKL-----IKH 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
993-1206 |
1.04e-11 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 67.69 E-value: 1.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDE---------- 1062
Cdd:PRK10619 8 VIDLHKRYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1063 ----IRKNLGMCPQHNVLFDRLTVEEHLW-----FYSRLKSMAQEEIRREMDKMIEDlELSNKRHSLvqTLSGGMKRKLS 1133
Cdd:PRK10619 86 qlrlLRTRLTMVFQHFNLWSHMTVLENVMeapiqVLGLSKQEARERAVKYLAKVGID-ERAQGKYPV--HLSGGQQQRVS 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 1134 VAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK10619 163 IARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLaEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAP 236
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2051-2271 |
1.16e-11 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 68.96 E-value: 1.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2130
Cdd:PRK10851 3 IEIANIKKSF-----GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV-SRLHARDRKV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQ-----LYTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:PRK10851 77 GFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2206 AFIFLDEPTTGMDPKA----RRFLWNLILDLIKTGrsvVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQ 2271
Cdd:PRK10851 156 QILLLDEPFGALDAQVrkelRRWLRQLHEELKFTS---VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPD 222
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1008-1200 |
1.21e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 69.69 E-value: 1.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQHNVLFDRLTVEEH 1085
Cdd:PRK15439 27 LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiyLVPQEPLLFPNLSVKEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1086 LWF--------YSRLKSMAQE-EIRREMDKMIEDLELSNKRhsLVQTLSGGMKRklsvaiafvggSRAIILDEPTAGVDP 1156
Cdd:PRK15439 107 ILFglpkrqasMQKMKQLLAAlGCQLDLDSSAGSLEVADRQ--IVEILRGLMRD-----------SRILILDEPTASLTP 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 1157 YARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK15439 174 AETERLFSRIRELlAQGVGIVFISHKLPEIRQLADRISVMRDGTI 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1000-1198 |
1.49e-11 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 66.28 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEI-RKNLGMCPQHNVLFD 1078
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RlTVEEHLWFYSRLKsmaqeEIRREMDKMIEDL-------ELSNKRhslVQTLSGGMKRKLSVA--IAFVggSRAIILDE 1149
Cdd:PRK10247 95 D-TVYDNLIFPWQIR-----NQQPDPAIFLDDLerfalpdTILTKN---IAELSGGEKQRISLIrnLQFM--PKVLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1150 PTAGVDPYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:PRK10247 164 ITSALDESNKHNVNEIIHRYvrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1002-1198 |
1.52e-11 |
|
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: 66.30 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1002 DDKKL-ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDIRT---------EMDEIRKN-LGMC 1070
Cdd:COG4778 20 GGKRLpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGS-ILVRHDGGWvdlaqasprEILALRRRtIGYV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1071 PQH-NVLfDRLT----VEEHLwfysRLKSMAQEEIRREMDKMIEDLELSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSRA 1144
Cdd:COG4778 99 SQFlRVI-PRVSaldvVAEPL----LERGVDREEARARARELLARLNLPERLWDLPpATFSGGEQQRVNIARGFIADPPL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1145 IILDEPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHG 1198
Cdd:COG4778 174 LLLDEPTASLDAANRAVVVELIEEAKArGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2050-2269 |
1.58e-11 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 67.32 E-value: 1.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKELLQVQ 2127
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPA 2206
Cdd:PRK13644 77 KLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2207 FIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGS 2269
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGE 218
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1000-1181 |
1.94e-11 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.74 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMCPQHNVLFDR 1079
Cdd:PRK13540 11 YHD--QPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLWFYSRLKSMAQeeirrEMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYAR 1159
Cdd:PRK13540 89 LTLRENCLYDIHFSPGAV-----GITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163
|
170 180
....*....|....*....|...
gi 45446740 1160 RAIWDLILKY-KPGRTILLSTHH 1181
Cdd:PRK13540 164 LTIITKIQEHrAKGGAVLLTSHQ 186
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
2084-2283 |
2.40e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 66.61 E-value: 2.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2084 FGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLR 2156
Cdd:PRK14246 39 FGIMGPSGSGKSTLLKVLNrlieiyDSKIKVDGKVLYFGKDIFQiDAIKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSH 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 GISWKDE-ARVVKWALEKLELTKYA----DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2231
Cdd:PRK14246 119 GIKEKREiKKIVEECLRKVGLWKEVydrlNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2232 LiKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYMI 2283
Cdd:PRK14246 199 L-KNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftspKNELTEKYVI 253
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
1019-1181 |
2.42e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.14 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1019 QVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDiRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRL---KSM 1095
Cdd:PLN03211 95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANN-RKPTKQILKRTGFVTQDDILYPHLTVRETLVFCSLLrlpKSL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1096 AQEEIRREMDKMIEDLELSNKRH-----SLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY-ARRAIWDLILKY 1169
Cdd:PLN03211 174 TKQEKILVAESVISELGLTKCENtiignSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATaAYRLVLTLGSLA 253
|
170
....*....|..
gi 45446740 1170 KPGRTILLSTHH 1181
Cdd:PLN03211 254 QKGKTIVTSMHQ 265
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
994-1206 |
2.82e-11 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 66.55 E-value: 2.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 994 DKLTKVYkdDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRKNLGMCPQ 1072
Cdd:PRK10253 11 EQLTLGY--GKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIqHYASKEVARRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEE--------HLWFYSRLKSMAQEEIRREMDKM-IEDLELSNkrhslVQTLSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK10253 89 NATTPGDITVQElvargrypHQPLFTRWRKEDEEAVTKAMQATgITHLADQS-----VDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLseLNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAP 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
988-1199 |
3.00e-11 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 66.10 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 988 PLVVcVDKLTKVYKDDKklALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDE- 1062
Cdd:PRK11701 5 PLLS-VRGLTKLYGPRK--GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLrdlyALSEa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1063 -----IRKNLGMCPQHNVLFDRLTVEEHLWFYSRLksMAQ-----EEIRREMDKMIEDLELSNKR-HSLVQTLSGGMKRK 1131
Cdd:PRK11701 82 errrlLRTEWGFVHQHPRDGLRMQVSAGGNIGERL--MAVgarhyGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1132 LSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLrgLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1000-1188 |
3.61e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 68.98 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLFppTSGSATIYGHDIRTEMDEIrknLGMCPQHN 1074
Cdd:TIGR00956 771 IKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVI--TGGDRLVNGRPLDSSFQRS---IGYVQQQD 845
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VLFDRLTVEEHLWFYSRL---KSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGM----KRKLSVAIAFVGGSRAII- 1146
Cdd:TIGR00956 846 LHLPTSTVRESLRFSAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVVGVPGEGLnveqRKRLTIGVELVAKPKLLLf 925
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1147 LDEPTAGVDPYARRAIWDLILKY-KPGRTILLSTHH-----MDEADLL 1188
Cdd:TIGR00956 926 LDEPTSGLDSQTAWSICKLMRKLaDHGQAILCTIHQpsailFEEFDRL 973
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
1004-1200 |
3.66e-11 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 68.60 E-value: 3.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1004 KKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRtEMDE--IRKNLGMCPQHNVLFDRlT 1081
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-QYDHhyLHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEEHLWFysRLKSMAQEEIRREMDKMIED---LELSNKRHSLV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGV 1154
Cdd:TIGR00958 571 VRENIAY--GLTDTPDEEIMAAAKAANAHdfiMEFPNGYDTEVgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSAL 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1155 DPYARRAIWDliLKYKPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:TIGR00958 649 DAECEQLLQE--SRSRASRTVLLIAHRLSTVE-RADQILVLKKGSV 691
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
2047-2264 |
4.09e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 66.80 E-value: 4.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2047 DNDMVKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFK----MLTGDESTTGGEAFVNGHSVLKE 2122
Cdd:PRK13631 18 DDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIKSKYGTIQVGDIYIGDKKNNH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 llqvQQSLGYCPQCDALFDELTAR-------EHLQLY--TRLRGISW--------KDEAR-VVKWALEKLEL-TKYADKP 2183
Cdd:PRK13631 98 ----ELITNPYSKKIKNFKELRRRvsmvfqfPEYQLFkdTIEKDIMFgpvalgvkKSEAKkLAKFYLNKMGLdDSYLERS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2184 AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK13631 174 PFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253
|
.
gi 45446740 2264 L 2264
Cdd:PRK13631 254 I 254
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2052-2265 |
4.40e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.03 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLT---KVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG---GEAFVNGHSV-LKELL 2124
Cdd:PRK13549 261 EVRNLTawdPVNPHIKR-----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG--AYPGrweGEIFIDGKPVkIRNPQ 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2125 Q-VQQSLGYCPQ---CDALFDELTAREHLQL--YTRLRGISWKDEARVVKWALE---KLEL-TKYADKPAGTYSGGNKRK 2194
Cdd:PRK13549 334 QaIAQGIAMVPEdrkRDGIVPVMGVGKNITLaaLDRFTGGSRIDDAAELKTILEsiqRLKVkTASPELAIARLSGGNQQK 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2195 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLR 2265
Cdd:PRK13549 414 AVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
2048-2270 |
4.66e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 65.61 E-value: 4.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTK---VYKSRKiGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE 2111
Cdd:PRK13546 2 NVSVNIKNVTKeyrIYRTNK-ERMkdalipkhknktfFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2112 AFVNGhsvlkELLQVQQSLGycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN 2191
Cdd:PRK13546 81 VDRNG-----EVSVIAISAG-------LSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGM 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:PRK13546 149 RAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGEL 227
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1007-1199 |
5.58e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 67.45 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI--RTEMDEIRKNLGMCPQHNVLFDRLTVEE 1084
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfKSSKEALENGISMVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWF--YSrLKSM--AQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:PRK10982 93 NMWLgrYP-TKGMfvDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 1161 AIWDLILKYKP-GRTILLSTHHMDEADLLGDRIAIISHGK 1199
Cdd:PRK10982 172 HLFTIIRKLKErGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2069-2261 |
6.28e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 65.54 E-value: 6.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2069 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQ-VQQSLGYCPQC-DALFDELTAR 2146
Cdd:PRK13648 23 FTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEkLRKHIGIVFQNpDNQFVGSIVK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2147 EHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLW 2226
Cdd:PRK13648 103 YDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190
....*....|....*....|....*....|....*
gi 45446740 2227 NLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVN 2261
Cdd:PRK13648 183 DLVRKV-KSEHNITIISITHDLSEAMEADHVIVMN 216
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2048-2264 |
7.13e-11 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 65.42 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVnGHSVLKE--LLQ 2125
Cdd:PRK13635 3 EEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITV-GGMVLSEetVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK13635 79 VRRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2264
Cdd:PRK13635 159 PDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSiTHDLDEA-AQADRVIVMNKGEI 218
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2078-2218 |
7.60e-11 |
|
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: 63.82 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTG---GEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTR 2154
Cdd:cd03233 30 VKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTVRETLDFALR 109
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2155 LRGiswKDEARVVkwalekleltkyadkpagtySGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2218
Cdd:cd03233 110 CKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
993-1206 |
8.42e-11 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 63.97 E-value: 8.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1071
Cdd:cd03369 9 VENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRremdkmiEDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:cd03369 89 QDPTLFSG-TIRSNLDPFDE---YSDEEIY-------GALRVSEGG----LNLSQGQRQLLCLARALLKRPRVLVLDEAT 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 1152 AGVDPYARRAIWDLILKYKPGRTILLSTHHMDE-ADLlgDRIAIISHGKLKCCGSP 1206
Cdd:cd03369 154 ASIDYATDALIQKTIREEFTNSTILTIAHRLRTiIDY--DKILVMDAGEVKEYDHP 207
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
2055-2263 |
8.86e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 8.86e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2055 NLTKvyksrKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG--DESTTGGEAFVNGhsvlkELLQVQ----- 2127
Cdd:PRK13549 10 NITK-----TFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvyPHGTYEGEIIFEG-----EELQASnirdt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 ---------QSLgycpqcdALFDELTAREHLQL---YTRLRGISW-KDEARVVKWaLEKLELTKYADKPAGTYSGGNKRK 2194
Cdd:PRK13549 80 eragiaiihQEL-------ALVKELSVLENIFLgneITPGGIMDYdAMYLRAQKL-LAQLKLDINPATPVGNLGLGQQQL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2195 LSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK13549 152 VEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2051-2316 |
9.34e-11 |
|
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: 67.13 E-value: 9.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE---LLQVQ 2127
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFT-----IEEGEVLGILGRSGAGKSVLMHVLRGMDQYEPTSGRIIYHVALCEkcgYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGY-CPQC---------------DALFDELTAREHLQLYtrlRGISWKDEARVVKWALEKLELTKYADKP-------- 2183
Cdd:TIGR03269 76 SKVGEpCPVCggtlepeevdfwnlsDKLRRRIRKRIAIMLQ---RTFALYGDDTVLDNVLEALEEIGYEGKEavgravdl 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2184 -------------AGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIK-TGRSVVLTSHSMEEC 2249
Cdd:TIGR03269 153 iemvqlshrithiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKaSGISMVLTSHWPEVI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2250 EALCTRLAIMVNGRLRCLGSIQHLKNRFgdgymitvrtksSQSVKDVVRFFNRNFPEAMLKERHHTK 2316
Cdd:TIGR03269 233 EDLSDKAIWLENGEIKEEGTPDEVVAVF------------MEGVSEVEKECEVEVGEPIIKVRNVSK 287
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1007-1199 |
9.83e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 66.88 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIY-------GHDIR-TEmdeiRKNLGMCPQHNVLFD 1078
Cdd:PRK13549 20 ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTYEGEIIfegeelqASNIRdTE----RAGIAIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RLTVEEHLWF---YSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK13549 96 ELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1156 PYARRAIWDLI--LKYKPGRTILLStHHMDEADLLGDRIAIISHGK 1199
Cdd:PRK13549 176 ESETAVLLDIIrdLKAHGIACIYIS-HKLNEVKAISDTICVIRDGR 220
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1008-1200 |
9.90e-11 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 67.06 E-value: 9.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEI----RKNLGMCPQHNVLFDRLTV 1082
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALaqlrREHFGFIFQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1083 EEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1162
Cdd:PRK10535 104 AQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEV 183
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 1163 WDlILKY--KPGRTILLSTHHMDEADlLGDRIAIISHGKL 1200
Cdd:PRK10535 184 MA-ILHQlrDRGHTVIIVTHDPQVAA-QAERVIEIRDGEI 221
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2070-2262 |
1.02e-10 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQS-LGYCPQCDALFDELTARE 2147
Cdd:PRK10762 19 ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtFNGPKSSQEAgIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HLQL----YTRLRGISWK---DEARVVkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2220
Cdd:PRK10762 99 NIFLgrefVNRFGRIDWKkmyAEADKL---LARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDT 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45446740 2221 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNG 2262
Cdd:PRK10762 176 ETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
2018-2268 |
1.45e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 66.80 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2018 PQRMPVSTKPVEDDVDVASERQRVLRGDAdndMVKIENLTKVYKSR-----KIGR-ILAVDRLCLGVRPGECFGLLGVNG 2091
Cdd:PRK10261 284 PRRFPLISLEHPAKQEPPIEQDTVVDGEP---ILQVRNLVTRFPLRsgllnRVTReVHAVEKVSFDLWPGETLSLVGESG 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2092 AGKTSTFKMLTGDESTTGGEAFVNGHSV-------LKEL--------------LQVQQSLGYcpqcdalfdelTAREHLQ 2150
Cdd:PRK10261 361 SGKSTTGRALLRLVESQGGEIIFNGQRIdtlspgkLQALrrdiqfifqdpyasLDPRQTVGD-----------SIMEPLR 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2151 LYTRLRGiswKDEARVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLI 2229
Cdd:PRK10261 430 VHGLLPG---KAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLL 506
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 45446740 2230 LDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLG 2268
Cdd:PRK10261 507 LDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
2086-2244 |
1.54e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2086 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREH--LQLYTRLRGISWKDE 2163
Cdd:PRK13540 32 LKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGINPYLTLRENclYDIHFSPGAVGITEL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2164 ARVVKwalekleLTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTS 2243
Cdd:PRK13540 112 CRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTS 184
|
.
gi 45446740 2244 H 2244
Cdd:PRK13540 185 H 185
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
996-1155 |
1.73e-10 |
|
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: 62.67 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 996 LTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPT---SGSATIYGHDIRTEMDEIRKNLGMCPQ 1072
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 HNVLFDRLTVEEHLWFYSRLKSmaqeeirremdkmiedlelsnkrHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:cd03233 91 EDVHFPTLTVRETLDFALRCKG-----------------------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147
|
...
gi 45446740 1153 GVD 1155
Cdd:cd03233 148 GLD 150
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
2052-2263 |
1.75e-10 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYksrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA-FVNGHSVLKELLQVQQS- 2129
Cdd:PRK11701 8 SVRGLTKLY-----GPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQLRDLYALSEAe 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 --------LGYCPQ--CDALFDELTAREHLQlyTRLRGISWKDEARV----VKWaLEKLEL--TKYADKPAgTYSGGNKR 2193
Cdd:PRK11701 83 rrrllrteWGFVHQhpRDGLRMQVSAGGNIG--ERLMAVGARHYGDIrataGDW-LERVEIdaARIDDLPT-TFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMD--PKARrflwnlILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDvsVQAR------LLDLLRGlvrelGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1008-1209 |
1.81e-10 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 64.04 E-value: 1.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFDRLTVEE-- 1084
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRElv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 ----HLWfYSRLKSMAQEEiRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARR 1160
Cdd:PRK10575 107 aigrYPW-HGALGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1161 AIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSPLFL 1209
Cdd:PRK10575 185 DVLALVhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2053-2269 |
1.87e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 64.26 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2053 IENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV------LKELLQV 2126
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkkIKEVKRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQCD--ALFDELTARE------HLQlytrlrgiswKDEARVVKWALEKLELTK----YADKPAGTYSGGNKRK 2194
Cdd:PRK13645 89 RKEIGLVFQFPeyQLFQETIEKDiafgpvNLG----------ENKQEAYKKVPELLKLVQlpedYVKRSPFELSGGQKRR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2195 LSTA--IALIGYPafIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK13645 159 VALAgiIAMDGNT--LVLDEPTGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
2048-2264 |
2.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 63.96 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLtkVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKE-LLQV 2126
Cdd:PRK13642 2 NKILEVENL--VFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 QQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYP 2205
Cdd:PRK13642 80 RRKIGMVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2206 AFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECeALCTRLAIMVNGRL 2264
Cdd:PRK13642 160 EIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSiTHDLDEA-ASSDRILVMKAGEI 218
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2073-2264 |
2.39e-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: 2.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2073 RLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkellqvqQSLGYCPQCD----ALFDELTAREH 2148
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLING-----------VDVTAAPPADrpvsMLFQENNLFAH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2149 LQLYT-----RLRGISWKDEAR-VVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2222
Cdd:cd03298 85 LTVEQnvglgLSPGLKLTAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 2223 RFLWNLILDLIK-TGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:cd03298 165 AEMLDLVLDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2044-2247 |
2.45e-10 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 65.77 E-value: 2.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2044 GDADNDMVKIENLTKVYKsrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL 2123
Cdd:TIGR02857 315 TAAPASSLEFSGVSVAYP----GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVP-LADA 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQ--VQQSLGYCPQCDALFdELTAREHLQLYTRlrgiSWKDEArvVKWALEKLELTKY-ADKPAGTY----------SGG 2190
Cdd:TIGR02857 390 DAdsWRDQIAWVPQHPFLF-AGTIAENIRLARP----DASDAE--IREALERAGLDEFvAALPQGLDtpigeggaglSGG 462
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2191 NKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHSME 2247
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLA 518
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2050-2264 |
3.15e-10 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 62.85 E-value: 3.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKIgrILAVDrlcLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG-----EAFVNGHSVLKE-- 2122
Cdd:PRK11264 3 AIEVKNLVKKFHGQTV--LHGID---LEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDTARSLSQqk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 --LLQVQQSLGYCPQCDALFDELTAREH-LQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAI 2199
Cdd:PRK11264 78 glIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2200 ALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2078-2264 |
3.80e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.14 E-value: 3.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGG---------------EAFVNGHSVLKEllqVQQSLGYCPQCDALFDE 2142
Cdd:PRK10982 271 LHKGEILGIAGLVGAKRTDIVETLFGIREKSAGtitlhgkkinnhnanEAINHGFALVTE---ERRSTGIYAYLDIGFNS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2143 LTAreHLQLY-TRLRGISWKDEARVVKWALEKLEL-TKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2220
Cdd:PRK10982 348 LIS--NIRNYkNKVGLLDNSRMKSDTQWVIDSMRVkTPGHRTQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVG 425
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 2221 ARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK10982 426 AKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1008-1200 |
5.07e-10 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 62.78 E-value: 5.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDI----RTEMDEIRKNLGMC---------PQHN 1074
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQMVfqdsisavnPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1075 VlfdRLTVEEHLWFYSRLKSMAQEEIRREMDKMIE-DLELSNKRHslvQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:PRK10419 108 V---REIIREPLRHLLSLDKAERLARASEMLRAVDlDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 1154 VDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK10419 182 LDLVLQAGVIRLLkkLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2053-2264 |
5.14e-10 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 62.39 E-value: 5.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2053 IENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEafvnghsvlkeLLQVQQSLGy 2132
Cdd:PRK11247 15 LNAVSKRYGERTV-----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGE-----------LLAGTAPLA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2133 cpqcdalfdelTAREHlqlyTRL-----RGISWKdeaRVV---------KW---ALEKLELTKYADK----PAgTYSGGN 2191
Cdd:PRK11247 78 -----------EARED----TRLmfqdaRLLPWK---KVIdnvglglkgQWrdaALQALAAVGLADRanewPA-ALSGGQ 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2192 KRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK11247 139 KQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1012-1200 |
6.50e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.16 E-value: 6.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1012 SLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH--DIRTEMDEIRKNLGMCPQhnvlfDR--------LT 1081
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKpiDIRSPRDAIRAGIMLCPE-----DRkaegiipvHS 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEE---------HLWFYSRLKSmAQEeiRREMDKMIEDLELSNK-RHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:PRK11288 348 VADninisarrhHLRAGCLINN-RWE--AENADRFIRSLNIKTPsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPT 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1152 AGVDPYARRAIWDLILKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK11288 425 RGIDVGAKHEIYNVIYELaAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1005-1201 |
7.01e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.00 E-value: 7.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1005 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEE 1084
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLWFYSRLKSmaqEEIRREMD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDP 1156
Cdd:PLN03232 698 NILFGSDFES---ERYWRAIDvtALQHDLDLL-PGRDLTEigergvNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1157 YARRAIWDLILKYK-PGRTILLSTHHMDEADLLgDRIAIISHGKLK 1201
Cdd:PLN03232 774 HVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLM-DRIILVSEGMIK 818
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
1008-1206 |
7.98e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.87 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT----EMDEIRKNLgmCPQHNVLFDRltve 1083
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYL--SQQQTPPFAM---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1084 eHLWFY---SRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAI-------ILDEPTAG 1153
Cdd:PRK03695 85 -PVFQYltlHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQVWPDInpagqllLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 1154 VDpYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGSP 1206
Cdd:PRK03695 164 LD-VAQQAALDRLLSElcQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRR 217
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2054-2269 |
1.01e-09 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 61.93 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2054 ENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGY 2132
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVE-----IPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHyASKEVARRIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2133 CPQ-----CDALFDELTAR---EHLQLYTRLRgiswKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK10253 86 LAQnattpGDITVQELVARgryPHQPLFTRWR----KEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2050-2264 |
1.04e-09 |
|
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: 61.30 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV--LKE--LLQ 2125
Cdd:COG4181 8 IIELRGLTKTVGTGA-GELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaLDEdaRAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 V-QQSLGYCPQCDALFDELTAREHLQLYTRLRGISwKDEARVVKWaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:COG4181 87 LrARHVGFVFQSFQLLPTLTALENVMLPLELAGRR-DARARARAL-LERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45446740 2205 PAFIFLDEPTTGMDPKARRflwnLILDLI-----KTGRSVVLTSHSmEECEALCTRLAIMVNGRL 2264
Cdd:COG4181 165 PAILFADEPTGNLDAATGE----QIIDLLfelnrERGTTLVLVTHD-PALAARCDRVLRLRAGRL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2078-2262 |
1.94e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 1.94e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQVQQSLG-Y-CPQCDALFDELTAREHLQLytRL 2155
Cdd:PRK15439 34 LHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGiYlVPQEPLLFPNLSVKENILF--GL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2156 RGiSWKDEARvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2235
Cdd:PRK15439 112 PK-RQASMQK-MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQ 189
|
170 180
....*....|....*....|....*..
gi 45446740 2236 GRSVVLTSHSMEECEALCTRLAIMVNG 2262
Cdd:PRK15439 190 GVGIVFISHKLPEIRQLADRISVMRDG 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2051-2263 |
2.12e-09 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 59.79 E-value: 2.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkellqvqqSL 2130
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDElTAREHLqlytrLRGISWkDEAR---VVK-WALEK-LELTkyadkPAG----------TYSGGNKRKL 2195
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI-----LFGKPF-DEERyekVIKaCALEPdLEIL-----PDGdlteigekgiNLSGGQKQRI 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2196 STAIALIGYPAFIFLDEPTTGMDPKARRFLW-NLILDLIKTGRSVVLTSHSMEECEAlCTRLAIMVNGR 2263
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
2050-2339 |
2.16e-09 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 60.48 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKEllqvQQS 2129
Cdd:PRK11248 1 MLQISHLYADYGGKP-----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP----GAE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIF 2209
Cdd:PRK11248 72 RGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2210 LDEPTTGMDPKARRFLWNLILDLI-KTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLgsiQHLKNRFGDGYmitVRTK 2288
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWqETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRF---VAGE 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2289 SSQSVKDVVRFFNRNfpeamlkerhhtkvqyqlksEHIsLAQVFSKMEQVS 2339
Cdd:PRK11248 226 SSRSIKSDPQFIAMR--------------------EYV-LSRVFEQREAFS 255
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1028-1201 |
2.41e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 62.25 E-value: 2.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1028 GAGKTTTMSILTGLFP-PTSGSATIYGH--DIRTEMDEIRKNLGMCP--------------QHNVLfdrLTVEEHLWFYS 1090
Cdd:PRK13549 298 GAGRTELVQCLFGAYPgRWEGEIFIDGKpvKIRNPQQAIAQGIAMVPedrkrdgivpvmgvGKNIT---LAALDRFTGGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1091 RLKSMAQEE-IRREMDKM---IEDLELSnkrhslVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI 1166
Cdd:PRK13549 375 RIDDAAELKtILESIQRLkvkTASPELA------IARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLI 448
|
170 180 190
....*....|....*....|....*....|....*.
gi 45446740 1167 LKY-KPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:PRK13549 449 NQLvQQGVAIIVISSELPEVLGLSDRVLVMHEGKLK 484
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2070-2273 |
2.43e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 62.53 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKELLQVQ--QSLGYCPQCDALFDElTARE 2147
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADYSEAAlrQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HLQLytrlrGISWKDEARVVKwALEKLELTKYADKPAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2217
Cdd:PRK11160 433 NLLL-----AAPNASDEALIE-VLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2218 DPKARRFLWNLILDLIKtGRSVVLTSH---SMEECEALCtrlaIMVNGRLRCLGSIQHL 2273
Cdd:PRK11160 507 DAETERQILELLAEHAQ-NKTVLMITHrltGLEQFDRIC----VMDNGQIIEQGTHQEL 560
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
2048-2279 |
2.70e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYK--SRKIGRI-------------LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEA 2112
Cdd:PRK13545 2 NYKVKFEHVTKKYKmyNKPFDKLkdlffrskdgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2113 FVNGHSVLkellqVQQSLGycpqcdaLFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNK 2192
Cdd:PRK13545 82 DIKGSAAL-----IAISSG-------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2193 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2272
Cdd:PRK13545 150 SRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKE 229
|
....*..
gi 45446740 2273 LKNRFGD 2279
Cdd:PRK13545 230 VVDHYDE 236
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1008-1180 |
2.86e-09 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 60.13 E-value: 2.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSatiyghdIRTEmDEIRknLGMCPQhNVLFDR---LTVEE 1084
Cdd:PRK09544 20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGV-------IKRN-GKLR--IGYVPQ-KLYLDTtlpLTVNR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1085 HLwfysRLKSMAQEeirremDKMIEDLELSNKRHSL---VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1161
Cdd:PRK09544 89 FL----RLRPGTKK------EDILPALKRVQAGHLIdapMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVA 158
|
170 180
....*....|....*....|.
gi 45446740 1162 IWDLI--LKYKPGRTILLSTH 1180
Cdd:PRK09544 159 LYDLIdqLRRELDCAVLMVSH 179
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2078-2256 |
3.15e-09 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 59.48 E-value: 3.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPqcdALFDELTAREHLQLYTRLR 2156
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRgDRSRFMAYLGHLP---GLKADLSTLENLHFLCGLH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 GISWKdeaRVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTG 2236
Cdd:PRK13543 111 GRRAK---QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGG 187
|
170 180
....*....|....*....|
gi 45446740 2237 RSVVLTSHSMEECEALCTRL 2256
Cdd:PRK13543 188 GAALVTTHGAYAAPPVRTRM 207
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
1025-1179 |
3.21e-09 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 62.14 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1025 GHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLF-DrlTVEEHLWfYSRLKSmAQEEIRR 1102
Cdd:COG5265 391 GPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGIVPQDTVLFnD--TIAYNIA-YGRPDA-SEEEVEA 466
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1103 -----EMDKMIEDLElsNKRHSLVQ----TLSGGMKRKlsVAIAfvggsRAI-------ILDEPTAGVDPYARRAIWDLI 1166
Cdd:COG5265 467 aaraaQIHDFIESLP--DGYDTRVGerglKLSGGEKQR--VAIA-----RTLlknppilIFDEATSALDSRTERAIQAAL 537
|
170
....*....|....*...
gi 45446740 1167 LKYKPGRTIL-----LST 1179
Cdd:COG5265 538 REVARGRTTLviahrLST 555
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2048-2250 |
3.76e-09 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 60.20 E-value: 3.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG---DESTTGGEAFVNGHSVL-KEL 2123
Cdd:PRK13640 3 DNIVEFKHVSFTYPDSKKP---ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGlllPDDNPNSKITVDGITLTaKTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQVQQSLGYCPQC-DALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:PRK13640 80 WDIREKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECE 2250
Cdd:PRK13640 160 VEPKIIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEAN 208
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
1005-1200 |
3.96e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 60.11 E-value: 3.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1005 KLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSG-----SATIYGHDIRTEMD--EIRKNLGMCPQHNVLF 1077
Cdd:PRK14271 34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDvlEFRRRVGMLFQRPNPF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQT----LSGGMKRKLSVAIAFVGGSRAIILDEPTAG 1153
Cdd:PRK14271 114 PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1154 VDPYARRAIWDLILKYKPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK14271 194 LDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1022-1180 |
4.05e-09 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 62.56 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1022 SFLGHNGAGKTTTMSILTGlfPPTSGsaTIYGhDIRT-----EMDEIRKNLGMCPQHNVLFDRLTVEEHLWF--YSRL-K 1093
Cdd:PLN03140 910 ALMGVSGAGKTTLMDVLAG--RKTGG--YIEG-DIRIsgfpkKQETFARISGYCEQNDIHSPQVTVRESLIYsaFLRLpK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1094 SMAQEEIRREMDKMIEDLELSNKRHSLV-----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYA----RRAIWD 1164
Cdd:PLN03140 985 EVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAaaivMRTVRN 1064
|
170
....*....|....*.
gi 45446740 1165 LIlkyKPGRTILLSTH 1180
Cdd:PLN03140 1065 TV---DTGRTVVCTIH 1077
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
969-1200 |
5.61e-09 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 61.40 E-value: 5.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 969 MESRRFEETRGMEEEPTHLPLVVCVDKLTkVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGlFPPTSGS 1048
Cdd:PRK11174 328 LETPLAHPQQGEKELASNDPVTIEAEDLE-ILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLG-FLPYQGS 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1049 ATIYGHDIRT-EMDEIRKNL---GMCPQ--HNVLFDRLTVEEHlwfysrlkSMAQEEIRREMDK-----MIEDLELSnkR 1117
Cdd:PRK11174 406 LKINGIELRElDPESWRKHLswvGQNPQlpHGTLRDNVLLGNP--------DASDEQLQQALENawvseFLPLLPQG--L 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1118 HSLVQ----TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMDeaDLLG-DRI 1192
Cdd:PRK11174 476 DTPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLE--DLAQwDQI 553
|
....*...
gi 45446740 1193 AIISHGKL 1200
Cdd:PRK11174 554 WVMQDGQI 561
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2069-2278 |
5.72e-09 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 59.04 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2069 LAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV-LKELLQVQQSLGYCPQCDALFDElTARE 2147
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQVGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HlqlytrlrgISWKDEA----RVVKWA--------LEKLEL---TKYADKPAGtYSGGNKRKLSTAIALIGYPAFIFLDE 2212
Cdd:cd03252 95 N---------IALADPGmsmeRVIEAAklagahdfISELPEgydTIVGEQGAG-LSGGQRQRIAIARALIHNPRILIFDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2213 PTTGMDPKARRFLWNLILDlIKTGRSVVLTSHSMEECEAlCTRLAIMVNGRLRCLGSIQHLKNRFG 2278
Cdd:cd03252 165 ATSALDYESEHAIMRNMHD-ICAGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENG 228
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
1003-1200 |
6.15e-09 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 61.14 E-value: 6.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTE-MDEIRKNLGMCPQHNVLFDRLT 1081
Cdd:PRK10522 334 DNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAVFTDFHLFDQLL 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEEhlwfySRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRA 1161
Cdd:PRK10522 414 GPE-----GKPANPALVEKWLERLKMAHKLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRRE 487
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 45446740 1162 IWDLILKY--KPGRTILLSTHHmDEADLLGDRIAIISHGKL 1200
Cdd:PRK10522 488 FYQVLLPLlqEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
989-1193 |
7.42e-09 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 61.10 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 989 LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIR-TEMDEIRKNL 1067
Cdd:TIGR03719 321 KVIEAENLTKAFGD--KLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKlAYVDQSRDAL 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1068 GmcPQHNVlfdrltveehlWfysrlksmaqEEIRREMDKM-IEDLELSNK------------RHSLVQTLSGGMKRKLSV 1134
Cdd:TIGR03719 398 D--PNKTV-----------W----------EEISGGLDIIkLGKREIPSRayvgrfnfkgsdQQKKVGQLSGGERNRVHL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1135 AIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYkPGRTILLStHhmDEADLlgDRIA 1193
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF-AGCAVVIS-H--DRWFL--DRIA 507
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
1006-1180 |
9.97e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 57.57 E-value: 9.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1006 LALNKLSLNLYENQV----VSFL--------GHNGAGKTTTMSILTGLFPPTSGSatIYGHDIRTemDEIRKNLGMCPQH 1073
Cdd:PRK13541 2 LSLHQLQFNIEQKNLfdlsITFLpsaityikGANGCGKSSLLRMIAGIMQPSSGN--IYYKNCNI--NNIAKPYCTYIGH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NV-LFDRLTVEEHLWFYSRLKSMAQeeirrEMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTA 1152
Cdd:PRK13541 78 NLgLKLEMTVFENLKFWSEIYNSAE-----TLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
170 180
....*....|....*....|....*....
gi 45446740 1153 GVDPYARRAIWDLI-LKYKPGRTILLSTH 1180
Cdd:PRK13541 153 NLSKENRDLLNNLIvMKANSGGIVLLSSH 181
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
1001-1180 |
1.02e-08 |
|
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: 57.25 E-value: 1.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSIL-----TGLfppTSGSATIYGHDIRtemDEIRKNLGMCPQHNV 1075
Cdd:cd03232 16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGV---ITGEILINGRPLD---KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTVEEHLWFYSRLKSMAQEEirremdkmiedlelsnkrhslvqtlsggmKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:cd03232 90 HSPNLTVREALRFSALLRGLSVEQ-----------------------------RKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180
....*....|....*....|....*.
gi 45446740 1156 PYARRAIWDLILKY-KPGRTILLSTH 1180
Cdd:cd03232 141 SQAAYNIVRFLKKLaDSGQAILCTIH 166
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2052-2269 |
1.16e-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: 57.54 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2052 KIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDEST--TGGEAFVNGHSVLkellqvqqs 2129
Cdd:cd03217 2 EIKDLHVSVGGKEI-----LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYevTEGEILFKGEDIT--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 lgycpqcdalfdeltareHLQLYTRLR---GISWKDEARV--VKWAleklELTKYADKpagTYSGGNKRKLSTAIALIGY 2204
Cdd:cd03217 68 ------------------DLPPEERARlgiFLAFQYPPEIpgVKNA----DFLRYVNE---GFSGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEAL-CTRLAIMVNGRLRCLGS 2269
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
2049-2246 |
1.31e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 58.20 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2049 DMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGeafvnghsVLKEllQVQQ 2128
Cdd:PRK09544 3 SLVSLENVSVSFGQRRV-----LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEG--------VIKR--NGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQcdALFDELTAREHLQLYTRLR-GISWKDearvVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2207
Cdd:PRK09544 68 RIGYVPQ--KLYLDTTLPLTVNRFLRLRpGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSM 2246
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2076-2268 |
1.35e-08 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 60.15 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV---LKELLQvqQSLGYCPQCDALFDElTAREHLqly 2152
Cdd:COG4618 353 FSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLsqwDREELG--RHIGYLPQDVELFDG-TIAENI--- 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TRLRGIswkDEARVVKWAlekleltKYAD-------KPAGtY-----------SGGNKRKLSTAIALIGYPAFIFLDEPT 2214
Cdd:COG4618 427 ARFGDA---DPEKVVAAA-------KLAGvhemilrLPDG-YdtrigeggarlSGGQRQRIGLARALYGDPRLVVLDEPN 495
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2215 TGMDPKARRFLWNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLG 2268
Cdd:COG4618 496 SNLDDEGEAALAAAIRALKARGATVVVITHRP---SLLaaVDKLLVLRDGRVQAFG 548
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2050-2264 |
1.48e-08 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 58.25 E-value: 1.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKigrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT--GD---ESTTGGEAFVNGHSVLK--- 2121
Cdd:PRK14239 5 ILQVSDLSVYYNKKK-----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDlnpEVTITGSIVYNGHNIYSprt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2122 ELLQVQQSLGYCPQCDALFdELTAREHLQLYTRLRGIswKDEArVVKWALEKL--------ELTKYADKPAGTYSGGNKR 2193
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGI--KDKQ-VLDEAVEKSlkgasiwdEVKDRLHDSALGLSGGQQQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDL 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
1011-1208 |
2.14e-08 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 2.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP----TSGS----------ATIYGHDIRTEMDEIRKNLGmcPQHNVl 1076
Cdd:PRK10418 22 VSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRvlldgkpvapCALRGRKIATIMQNPRSAFN--PLHTM- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1077 fdRLTVEEHLWFYSRLKSMAQeeIRREMDKM-IEDLELSNKRHSLvqTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK10418 99 --HTHARETCLALGKPADDAT--LTAALEAVgLENAARVLKLYPF--EMSGGMLQRMMIALALLCEAPFIIADEPTTDLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 1156 PYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLKCCGS--PLF 1208
Cdd:PRK10418 173 VVAQARILDLLesIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDveTLF 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2055-2264 |
2.23e-08 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 57.13 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2055 NLTKVYKSRKIGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-------ELLqvQ 2127
Cdd:PRK11629 10 NLCKRYQEGSVQTDVLHN-VSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlssaakaELR--N 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLGYCPQCDALFDELTAREHLQLYTRLRGiswKDEARVVKWALEKLE---LTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK11629 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGK---KKPAEINSRALEMLAavgLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAiMVNGRL 2264
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2051-2264 |
2.30e-08 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 58.17 E-value: 2.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG------------------DESTTGGEA 2112
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNAlllpdtgtiewifkdeknKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2113 FVNGHSV-------LKELLQVQQSLGYCPQCD--ALFDElTAREHLQLYTRLRGISwKDEARvvKWALEKLELT----KY 2179
Cdd:PRK13651 83 VLEKLVIqktrfkkIKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSMGVS-KEEAK--KRAAKYIELVgldeSY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2180 ADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIM 2259
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
....*
gi 45446740 2260 VNGRL 2264
Cdd:PRK13651 239 KDGKI 243
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2048-2275 |
2.77e-08 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 57.47 E-value: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----EL 2123
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCI-----FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQVQQSLGYCPQCDALFDELTA--------REHLQLYTRLRgiswkdeARVVKWALEKLELTKYADKPAGTYSGGNKRK- 2194
Cdd:PRK11831 80 YTVRKRMSMLFQSGALFTDMNVfdnvayplREHTQLPAPLL-------HSTVMMKLEAVGLRGAAKLMPSELSGGMARRa 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2195 -LSTAIALigYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2272
Cdd:PRK11831 153 aLARAIAL--EPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQA 230
|
...
gi 45446740 2273 LKN 2275
Cdd:PRK11831 231 LQA 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1007-1200 |
3.23e-08 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 57.11 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGH-----DIRTEMDEIRknlgMCPQ--HNVLFDR 1079
Cdd:PRK15112 28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplhfgDYSYRSQRIR----MIFQdpSTSLNPR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1080 LTVEEHLWFYSRLKSMAQEEIRREmdKMIEDLE----LSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK15112 104 QRISQILDFPLRLNTDLEPEQREK--QIIETLRqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 45446740 1156 PYARRAIWDLILKY--KPGRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK15112 182 MSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2078-2244 |
3.33e-08 |
|
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: 56.99 E-value: 3.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGdesttggeafvnghsvlkellQVQQSLG-YC--PQCDALFDELTAREhLQLY-T 2153
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAG---------------------KLKPNLGkFDdpPDWDEILDEFRGSE-LQNYfT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2154 RLRG--------------------------ISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAF 2207
Cdd:cd03236 81 KLLEgdvkvivkpqyvdlipkavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADF 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446740 2208 IFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:cd03236 161 YFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEH 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2048-2244 |
6.26e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 58.02 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkELLQVQ 2127
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGT-IEIGETV--KLAYVD 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2128 QSLgycpqcDALFDELTAREHL---QLYTRLRGISWKDEARVVKWALekleltKYAD--KPAGTYSGGNKRKLSTAIALI 2202
Cdd:TIGR03719 392 QSR------DALDPNKTVWEEIsggLDIIKLGKREIPSRAYVGRFNF------KGSDqqKKVGQLSGGERNRVHLAKTLK 459
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2244
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLNF---AGCAVVISH 498
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
2034-2273 |
9.85e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 55.87 E-value: 9.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2034 VASERQRVLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTG-DESTT 2108
Cdd:PRK14271 1 MACERLGGQSGAADVDAaapaMAAVNLTLGFAGKTV-----LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmNDKVS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2109 G----GEAFVNGHSVL--KELLQVQQSLGYC-----PQCDALFDELTA--REH-LQLYTRLRGISwkdEARVVKWALEKL 2174
Cdd:PRK14271 76 GyrysGDVLLGGRSIFnyRDVLEFRRRVGMLfqrpnPFPMSIMDNVLAgvRAHkLVPRKEFRGVA---QARLTEVGLWDA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2175 ELTKYADKPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTgRSVVLTSHSMEECEALCT 2254
Cdd:PRK14271 153 VKDRLSDSPF-RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISD 230
|
250
....*....|....*....
gi 45446740 2255 RLAIMVNGRLRCLGSIQHL 2273
Cdd:PRK14271 231 RAALFFDGRLVEEGPTEQL 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
2070-2263 |
1.08e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 57.05 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELLQ-----VQQSLGYCPQCDALF 2140
Cdd:PRK10982 13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfksSKEALEngismVHQELNLVLQRSVMD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2141 DELTAR--------EHLQLYTRLRGIswkdearvvkwaLEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDE 2212
Cdd:PRK10982 93 NMWLGRyptkgmfvDQDKMYRDTKAI------------FDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2213 PTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGR 2263
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
2074-2245 |
1.10e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2074 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKellqVQQS-LGYCPQCDALFDELTAREHLQLY 2152
Cdd:PRK13541 19 LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINN----IAKPyCTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2153 TRLRgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2232
Cdd:PRK13541 95 SEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|...
gi 45446740 2233 IKTGRSVVLTSHS 2245
Cdd:PRK13541 170 ANSGGIVLLSSHL 182
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2023-2264 |
1.16e-07 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 57.03 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2023 VSTKPVEDDVDVASERqrvLRGDadndmVKIENLTKVYKSRKIGrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT 2102
Cdd:TIGR02203 311 LDSPPEKDTGTRAIER---ARGD-----VEFRNVTFRYPGRDRP---ALDSISLVIEPGETVALVGRSGSGKSTLVNLIP 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2103 GDESTTGGEAFVNGHSVLKELLQ-VQQSLGYCPQCDALFDELTAREhlQLYTRLRGIswkDEARVVKwALEKLELTKYAD 2181
Cdd:TIGR02203 380 RFYEPDSGQILLDGHDLADYTLAsLRRQVALVSQDVVLFNDTIANN--IAYGRTEQA---DRAEIER-ALAAAYAQDFVD 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2182 K-PAGTY----------SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRfLWNLILDLIKTGRSVVLTSHSMEECE 2250
Cdd:TIGR02203 454 KlPLGLDtpigengvllSGGQRQRLAIARALLKDAPILILDEATSALDNESER-LVQAALERLMQGRTTLVIAHRLSTIE 532
|
250
....*....|....
gi 45446740 2251 AlCTRLAIMVNGRL 2264
Cdd:TIGR02203 533 K-ADRIVVMDDGRI 545
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2188-2264 |
1.34e-07 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 55.56 E-value: 1.34e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2188 SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK13646 147 SGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENKTIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
2051-2261 |
1.72e-07 |
|
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: 54.54 E-value: 1.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2129
Cdd:cd03254 3 IEFENVNFSYDEKKP----VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDElTAREHLqLYTRLRgISWKDEARVVKWA-----LEKLE--LTKYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENI-RLGRPN-ATDEEVIEAAKEAgahdfIMKLPngYDTVLGENGGNLSQGERQLLAIARAML 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2203 GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSHsmeecealctRLAIMVN 2261
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAH----------RLSTIKN 203
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
993-1201 |
2.25e-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: 2.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFpPTSGSATIYGHDIRT-EMDEIRKNLGMCP 1071
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL-STEGEIQIDGVSWNSvTLQTWRKAFGVIP 1298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1072 QHNVLFDRlTVEEHLWFYSRlksMAQEEIRREMDK-----MIE------DLELSNKRHslvqTLSGGMKRKLSVAIAFVG 1140
Cdd:TIGR01271 1299 QKVFIFSG-TFRKNLDPYEQ---WSDEEIWKVAEEvglksVIEqfpdklDFVLVDGGY----VLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLILKYKPGRTILLSTHHMdEADLLGDRIAIISHGKLK 1201
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRV-EALLECQQFLVIEGSSVK 1430
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
1001-1199 |
2.38e-07 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 53.63 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1001 KDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHdirtemdeirknLGMCPQ-------- 1072
Cdd:cd03250 14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------IAYVSQepwiqngt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 --HNVLFDRltVEEHLWFYSRLKSMAQEEirremdkmieDLE-LSNKRHSLVQ----TLSGGMKRKLSVAIAFVGGSRAI 1145
Cdd:cd03250 82 irENILFGK--PFDEERYEKVIKACALEP----------DLEiLPDGDLTEIGekgiNLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 1146 ILDEPTAGVDPYARRAIWD-LILKY-KPGRTILLSTHHMdeaDLLG--DRIAIISHGK 1199
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFEnCILGLlLNNKTRILVTHQL---QLLPhaDQIVVLDNGR 204
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
980-1156 |
2.58e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 980 MEEEPTHLPLVVCVDKLTkvYKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT- 1058
Cdd:PRK13543 1 MIEPLHTAPPLLAAHALA--FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1059 EMDEIRKNLGMCPQhnvLFDRLTVEEHLWFysrLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAF 1138
Cdd:PRK13543 79 DRSRFMAYLGHLPG---LKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLW 152
|
170
....*....|....*...
gi 45446740 1139 VGGSRAIILDEPTAGVDP 1156
Cdd:PRK13543 153 LSPAPLWLLDEPYANLDL 170
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2070-2267 |
3.13e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 55.75 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKtSTFKM-LTGDESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDA-LFDELTARE 2147
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGK-STLAMlLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFhLFDQLLGPE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2148 HLQlytrlrgiswKDEARVVKWaLEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKAR 2222
Cdd:PRK10522 417 GKP----------ANPALVEKW-LERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 2223 RFLWNLILDLIK-TGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCL 2267
Cdd:PRK10522 486 REFYQVLLPLLQeMGKTIFAISHDDHYFI-HADRLLEMRNGQLSEL 530
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2076-2247 |
3.84e-07 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 53.82 E-value: 3.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVL--------------KELLQVQQSLGYCPQCDALFD 2141
Cdd:PRK10619 26 LQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQLRLLRTRLTMVFQHFNLWS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2142 ELTAREH-LQLYTRLRGISwKDEA--RVVKWaLEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGM 2217
Cdd:PRK10619 106 HMTVLENvMEAPIQVLGLS-KQEAreRAVKY-LAKVGIDERAqGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
|
170 180 190
....*....|....*....|....*....|
gi 45446740 2218 DPKARRFLWNLILDLIKTGRSVVLTSHSME 2247
Cdd:PRK10619 184 DPELVGEVLRIMQQLAEEGKTMVVVTHEMG 213
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1007-1180 |
4.41e-07 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 54.35 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPP---TSGSATIYGHDI----RTEMDEIR-KNLGMCPQhnvlfD 1078
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQ-----D 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 RLT-----------VEEHLWFYSRL-KSMAQEEIRREMD--KMIEdlelSNKRHSLV-QTLSGGMKRKLSVAIAFVGGSR 1143
Cdd:PRK09473 106 PMTslnpymrvgeqLMEVLMLHKGMsKAEAFEESVRMLDavKMPE----ARKRMKMYpHEFSGGMRQRVMIAMALLCRPK 181
|
170 180 190
....*....|....*....|....*....|....*....
gi 45446740 1144 AIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTH 1180
Cdd:PRK09473 182 LLIADEPTTALDVTVQAQIMTLLneLKREFNTAIIMITH 220
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2071-2248 |
4.47e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 53.18 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGEcFGLL-GVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK---EllQVQQSLGYCPQCDALFDElTAR 2146
Cdd:PRK10247 23 LNNISFSLRAGE-FKLItGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpE--IYRQQVSYCAQTPTLFGD-TVY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2147 EHLQLYTRLRGISwKDEARVVKwALEKLELTKYA-DKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFL 2225
Cdd:PRK10247 99 DNLIFPWQIRNQQ-PDPAIFLD-DLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176
|
170 180
....*....|....*....|....
gi 45446740 2226 WNLILDLIK-TGRSVVLTSHSMEE 2248
Cdd:PRK10247 177 NEIIHRYVReQNIAVLWVTHDKDE 200
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1000-1155 |
6.93e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 55.13 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1000 YKDDKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT-EMDEIRKNLGMCPQHNVLFD 1078
Cdd:PLN03130 1247 YRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFS 1326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1079 ---RLTVE---EH----LWfYSRLKSMAQEEIRREMDKMieDLELSNKRhslvQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:PLN03130 1327 gtvRFNLDpfnEHndadLW-ESLERAHLKDVIRRNSLGL--DAEVSEAG----ENFSVGQRQLLSLARALLRRSKILVLD 1399
|
....*..
gi 45446740 1149 EPTAGVD 1155
Cdd:PLN03130 1400 EATAAVD 1406
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2157-2273 |
8.54e-07 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 53.10 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 GISWKDEARVVKWALEKLELT-KYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT 2235
Cdd:PRK13634 115 GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKE 194
|
90 100 110
....*....|....*....|....*....|....*....
gi 45446740 2236 -GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:PRK13634 195 kGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2063-2273 |
1.09e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 53.94 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2063 RKIGRILAVDRLCLGVRPGECFGLLGVNGAGKtstfkmltgdeSTTG----------GEAFVNGHSVlkELLQVQQSLGY 2132
Cdd:PRK15134 294 RTVDHNVVVKNISFTLRPGETLGLVGESGSGK-----------STTGlallrlinsqGEIWFDGQPL--HNLNRRQLLPV 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2133 CPQCDALFDE----LTAR--------EHLQLYTRLRGISWKdEARVVKwALEKLEL---TKYadKPAGTYSGGNKRKLST 2197
Cdd:PRK15134 361 RHRIQVVFQDpnssLNPRlnvlqiieEGLRVHQPTLSAAQR-EQQVIA-VMEEVGLdpeTRH--RYPAEFSGGQRQRIAI 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2198 AIALIGYPAFIFLDEPTTGMDpkarRFLWNLILDLIKT-----GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2272
Cdd:PRK15134 437 ARALILKPSLIILDEPTSSLD----KTVQAQILALLKSlqqkhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCER 512
|
.
gi 45446740 2273 L 2273
Cdd:PRK15134 513 V 513
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
2183-2247 |
1.09e-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: 53.16 E-value: 1.09e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45446740 2183 PAGTYSGGNKRKLSTAIALI---GYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSME 2247
Cdd:pfam13304 233 PAFELSDGTKRLLALLAALLsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPL 300
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
1017-1195 |
1.10e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 52.37 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1017 ENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAT------------------IYGHDIRT-EMDEIRKnlgmcPQHnvlF 1077
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildefrgselqNYFTKLLEgDVKVIVK-----PQY---V 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1078 DRL------TVEEHLwfysrlksmAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEPT 1151
Cdd:cd03236 97 DLIpkavkgKVGELL---------KKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 45446740 1152 AGVDPYAR----RAIWDLIlkyKPGRTILLSTHHMDEADLLGDRIAII 1195
Cdd:cd03236 168 SYLDIKQRlnaaRLIRELA---EDDNYVLVVEHDLAVLDYLSDYIHCL 212
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
952-1200 |
1.17e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.58 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 952 WARTPRLSVMEEDQACAMESRRFEETRGMEEEPTHLPLVVCVDKLTKVykddKKLALNKLSLNLYENQVVSFLGHNGAGK 1031
Cdd:PRK10982 212 WIATQPLAGLTMDKIIAMMVGRSLTQRFPDKENKPGEVILEVRNLTSL----RQPSIRDVSFDLHKGEILGIAGLVGAKR 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1032 TTTMSILTGLFPPTSGSATIYGHDI--RTEMDEI----------RKNLGMCPQHNVLFDRL--TVEEHLwfySRLKSMAQ 1097
Cdd:PRK10982 288 TDIVETLFGIREKSAGTITLHGKKInnHNANEAInhgfalvteeRRSTGIYAYLDIGFNSLisNIRNYK---NKVGLLDN 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1098 EEIRREMDKMIEDLELSNKRHS-LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKY-KPGRTI 1175
Cdd:PRK10982 365 SRMKSDTQWVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI 444
|
250 260
....*....|....*....|....*..
gi 45446740 1176 LLSTHHMDEadLLG--DRIAIISHGKL 1200
Cdd:PRK10982 445 IIISSEMPE--LLGitDRILVMSNGLV 469
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2067-2261 |
1.30e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2067 RILAVDRLCLgvRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE---AFVngHSVLKELLQVQQSLGYCPQ---CDALF 2140
Cdd:PRK10938 17 KTLQLPSLTL--NAGDSWAFVGANGSGKSALARALAGELPLLSGErqsQFS--HITRLSFEQLQKLVSDEWQrnnTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2141 -DE----LTAREHLQLYTrlrgiswKDEARVVKWAlEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTT 2215
Cdd:PRK10938 93 pGEddtgRTTAEIIQDEV-------KDPARCEQLA-QQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 2216 GMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVN 2261
Cdd:PRK10938 165 GLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
993-1184 |
1.42e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.74 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 993 VDKLTKVYKDDKK----LALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSAtiyghDIRTEMDEIRKNLG 1068
Cdd:PRK13545 21 FDKLKDLFFRSKDgeyhYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1069 mcpqhnvLFDRLTVEEHLWFYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILD 1148
Cdd:PRK13545 96 -------LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVID 168
|
170 180 190
....*....|....*....|....*....|....*..
gi 45446740 1149 EPTAGVDPYARRAIWDLILKYKP-GRTILLSTHHMDE 1184
Cdd:PRK13545 169 EALSVGDQTFTKKCLDKMNEFKEqGKTIFFISHSLSQ 205
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
2048-2244 |
1.49e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 53.64 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE-AFVNGhsvLKellqv 2126
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRII-----LDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEiGLAKG---IK----- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2127 qqsLGYCPQCDALF---DElTAREHLqlytrlrgiswkdeARVVKWALEKlELTKY-------ADK---PAGTYSGGNKR 2193
Cdd:PRK10636 377 ---LGYFAQHQLEFlraDE-SPLQHL--------------ARLAPQELEQ-KLRDYlggfgfqGDKvteETRRFSGGEKA 437
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2244
Cdd:PRK10636 438 RLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDF---EGALVVVSH 485
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
1008-1199 |
1.65e-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: 51.07 E-value: 1.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLN----LYENQVVSFL-------GHNGAGKTTTMS----ILTGLFPPTSgsatiYGHDIRTEMdeIRKNlgmcpq 1072
Cdd:cd03240 1 IDKLSIRnirsFHERSEIEFFspltlivGQNGAGKTTIIEalkyALTGELPPNS-----KGGAHDPKL--IREG------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1073 hnvlfdRLTVEEHLWFYSRLKsmAQEEIRR--------------EMDKMIEDLelsnkrhslVQTLSGGMKRKLSV---- 1134
Cdd:cd03240 68 ------EVRAQVKLAFENANG--KKYTITRslailenvifchqgESNWPLLDM---------RGRCSGGEKVLASLiirl 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1135 AIAFVGGSRA--IILDEPTAGVDPYARR-AIWDLI--LKYKPGRTILLSTHHMDEADLLGD--RIAIISHGK 1199
Cdd:cd03240 131 ALAETFGSNCgiLALDEPTTNLDEENIEeSLAEIIeeRKSQKNFQLIVITHDEELVDAADHiyRVEKDGRQK 202
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2013-2311 |
2.16e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2013 NFLRRPQRMPVSTKPVEddVDVASERQRVLRGDAD--------NDMVKI-ENLTKVYKSRKIGRILAVDRLCLGV-RPGE 2082
Cdd:TIGR00956 11 NFRKLIDSDPIYYKPYK--LGVAYKNLSAYGVAADsdyqptfpNALLKIlTRGFRKLKKFRDTKTFDILKPMDGLiKPGE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2083 CFGLLGVNGAGKTSTFKMLTGD----ESTTGGEAFVNGHSVLKELLQVQQSLGYCPQCDALFDELTAREHLQLYTRLR-- 2156
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIASNtdgfHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKtp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 -----GISWKDEA-RVVKWALEKLELTKYADKPAGT-----YSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK-ARRF 2224
Cdd:TIGR00956 169 qnrpdGVSREEYAkHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAtALEF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2225 LWNL--ILDLIKTGRSVVLTSHSMEECEaLCTRLAIMVNGRLRCLGSIQHLKNRFGD-GYM-------------ITVRT- 2287
Cdd:TIGR00956 249 IRALktSANILDTTPLVAIYQCSQDAYE-LFDKVIVLYEGYQIYFGPADKAKQYFEKmGFKcpdrqttadfltsLTSPAe 327
|
330 340 350
....*....|....*....|....*....|....*
gi 45446740 2288 ---------KSSQSVKDVVRFFnRNFPE--AMLKE 2311
Cdd:TIGR00956 328 rqikpgyekKVPRTPQEFETYW-RNSPEyaQLMKE 361
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
998-1155 |
2.26e-06 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 52.02 E-value: 2.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 998 KVY---KDDKKL---------ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR----TEMD 1061
Cdd:PRK15079 15 KVHfdiKDGKQWfwqppktlkAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLgmkdDEWR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 EIRKNLGMCPQHNV--LFDRLTV----EEHLWFYSrlKSMAQEEIRREMDKMIEDLEL-SNKRHSLVQTLSGGMKRKLSV 1134
Cdd:PRK15079 95 AVRSDIQMIFQDPLasLNPRMTIgeiiAEPLRTYH--PKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGI 172
|
170 180
....*....|....*....|.
gi 45446740 1135 AIAFVGGSRAIILDEPTAGVD 1155
Cdd:PRK15079 173 ARALILEPKLIICDEPVSALD 193
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2051-2282 |
4.02e-06 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 51.57 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIGRILAVDrlclgVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQVQQSL 2130
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLD-----IHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-NDVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFL 2210
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2211 DEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL----KNRFGDGYM 2282
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELyhypANRFVAGFI 234
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
2076-2244 |
4.53e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGE-------------------------AFVNG-----HSVLKELLQ 2125
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRiiyeqdlivarlqqdpprnvegtvyDFVAEgieeqAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQcDALFDELtAR-----EHLQLytrlrgisWKDEARVvKWALEKLELTkyADKPAGTYSGGNKRKLSTAIA 2200
Cdd:PRK11147 104 ISHLVETDPS-EKNLNEL-AKlqeqlDHHNL--------WQLENRI-NEVLAQLGLD--PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 45446740 2201 LIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2244
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF---QGSIIFISH 211
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2051-2244 |
5.85e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 51.66 E-value: 5.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRkigriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHSVlkellqvqqSL 2130
Cdd:PRK11819 325 IEAENLSKSFGDR-----LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGT-IKIGETV---------KL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 GYCPQC-DALFDELTAREhlqlytrlrgiswkdearVVKWALEKLELTKY---------------AD--KPAGTYSGGNK 2192
Cdd:PRK11819 390 AYVDQSrDALDPNKTVWE------------------EISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGER 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2193 RKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLiktGRSVVLTSH 2244
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEF---PGCAVVISH 500
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2048-2264 |
6.42e-06 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 50.08 E-value: 6.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2048 NDMVKIENLTkVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLTGDESTTGGEAFVNGHSVLKEL 2123
Cdd:PRK10418 2 PQQIELRNIA-LQAAQPL-----VHGVSLTLQRGRVLALVGGSGSGKSLTcaaaLGILPAGVRQTAGRVLLDGKPVAPCA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 LQ------VQQSlgycPQcdALFDEL-TAREHLQLYTRLRGISwKDEARVVKwALEKLELTKyADKPAGTY----SGGNK 2192
Cdd:PRK10418 76 LRgrkiatIMQN----PR--SAFNPLhTMHTHARETCLALGKP-ADDATLTA-ALEAVGLEN-AARVLKLYpfemSGGML 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2193 RKLSTAIALIGYPAFIFLDEPTTGMDPKAR-RFLwNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:PRK10418 147 QRMMIALALLCEAPFIIADEPTTDLDVVAQaRIL-DLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
2078-2222 |
7.82e-06 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 49.71 E-value: 7.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlkellqvqqslGYCPQCDALFDELTAREHLQLYTRLRG 2157
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----------SYKPQYIKADYEGTVRDLLSSITKDFY 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2158 IS--WKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKlsTAIAL-IGYPAFIFL-DEPTTGMDPKAR 2222
Cdd:cd03237 91 THpyFKTE------IAKPLQIEQILDREVPELSGGELQR--VAIAAcLSKDADIYLlDEPSAYLDVEQR 151
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
2071-2264 |
9.33e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 50.94 E-value: 9.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKT----STFKMLTGdeSTTGGEAFVNGHSVlkELLQVQQS----LGYcpqcdALFDe 2142
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTelamSVFGRSYG--RNISGTVFKDGKEV--DVSTVSDAidagLAY-----VTED- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2143 ltaREHLQL-----------YTRLRGIS---WKDEARVVKWALE---KLEL-TKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:NF040905 346 ---RKGYGLnliddikrnitLANLGKVSrrgVIDENEEIKVAEEyrkKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEECEALCTRLAIMVNGRL 2264
Cdd:NF040905 423 PDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
983-1162 |
9.44e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 9.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 983 EPTHLP-LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIyGHDIRtemd 1061
Cdd:PRK10636 304 APESLPnPLLKMEKVSAGYGD--RIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGIK---- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1062 eirknLGMCPQHNVLFDRLTvEEHLWFYSRLKSMAQEEIRREM--------DKMIEDLElsnkrhslvqTLSGGMKRKLS 1133
Cdd:PRK10636 377 -----LGYFAQHQLEFLRAD-ESPLQHLARLAPQELEQKLRDYlggfgfqgDKVTEETR----------RFSGGEKARLV 440
|
170 180
....*....|....*....|....*....
gi 45446740 1134 VAIAFVGGSRAIILDEPTAGVDPYARRAI 1162
Cdd:PRK10636 441 LALIVWQRPNLLLLDEPTNHLDLDMRQAL 469
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2076-2244 |
1.07e-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: 49.15 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2076 LGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVlKELLQ--VQQSLGYCPQCDALFDElTAREHLQlYT 2153
Cdd:cd03253 22 FTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVTLdsLRRAIGVVPQDTVLFND-TIGYNIR-YG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2154 RLrgiSWKDEA--RVVKWALEKLELTKYADKPA------GTY-SGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2224
Cdd:cd03253 99 RP---DATDEEviEAAKAAQIHDKIMRFPDGYDtivgerGLKlSGGEKQRVAIARAILKNPPILLLDEATSALDTHTERE 175
|
170 180
....*....|....*....|
gi 45446740 2225 LWNLILDLIKtGRSVVLTSH 2244
Cdd:cd03253 176 IQAALRDVSK-GRTTIVIAH 194
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
1117-1180 |
1.34e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.74 E-value: 1.34e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1117 RHSLVQTLSGGMKRKLSVAIAFVGGSRA----IILDEPTAGVDPYARRAIWDLILK-YKPGRTILLSTH 1180
Cdd:cd03227 71 LIFTRLQLSGGEKELSALALILALASLKprplYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITH 139
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
990-1205 |
1.67e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 50.24 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 990 VVCVDKLTKVYKDDKKL--ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIR---------- 1057
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRrrsrqviels 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1058 ----TEMDEIR-KNLGMCPQH-----NVLFdrlTVEEHLWFYSRL-KSMAQEEIRREMDKMIEDLELSNKRHSLVQ---T 1123
Cdd:PRK10261 92 eqsaAQMRHVRgADMAMIFQEpmtslNPVF---TVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1124 LSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGKLK 1201
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAV 248
|
....
gi 45446740 1202 CCGS 1205
Cdd:PRK10261 249 ETGS 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1008-1155 |
1.91e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.95 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSaTIYGHDI---RTEMDEIRKNLGmcpqhNVlFDRLT--- 1081
Cdd:PRK11147 19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGR-IIYEQDLivaRLQQDPPRNVEG-----TV-YDFVAegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 --VEEHLWFYSRL-KSMAQEEIRR---EMDKMIEDLELSN-----KR------------HSLVQTLSGGMKRKLSVAIAF 1138
Cdd:PRK11147 92 eeQAEYLKRYHDIsHLVETDPSEKnlnELAKLQEQLDHHNlwqleNRinevlaqlgldpDAALSSLSGGWLRKAALGRAL 171
|
170
....*....|....*..
gi 45446740 1139 VGGSRAIILDEPTAGVD 1155
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLD 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2030-2255 |
2.03e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2030 DDVDvASERQR-VLRGDADNDM----VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD 2104
Cdd:PRK15064 295 EEVK-PSSRQNpFIRFEQDKKLhrnaLEVENLTKGFDNGPL-----FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGE 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2105 ESTTGGEafvnghsvlkellqVQQS----LGYCPQcD--ALFDE-LTAREHLQLYTRLrgiswKDEARVVKWALEKLELT 2177
Cdd:PRK15064 369 LEPDSGT--------------VKWSenanIGYYAQ-DhaYDFENdLTLFDWMSQWRQE-----GDDEQAVRGTLGRLLFS 428
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2178 K-YADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLwNLILDLIKTgrSVVLTSHSMEECEALCTR 2255
Cdd:PRK15064 429 QdDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESL-NMALEKYEG--TLIFVSHDREFVSSLATR 504
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2070-2218 |
2.13e-05 |
|
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: 49.74 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSvLKEL--LQVQQSLGYCPQCDALFDElTARE 2147
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFS-LKDIdrHTLRQFINYLPQEPYIFSG-SILE 566
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 2148 HLQLYTRlRGISWKDEARVVKWA-----LEKLEL---TKYADKpAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD 2218
Cdd:TIGR01193 567 NLLLGAK-ENVSQDEIWAACEIAeikddIENMPLgyqTELSEE-GSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2050-2232 |
2.20e-05 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 48.63 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSR----KIGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHsvlkellq 2125
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 vQQSLG---YCPQC-DALFDE----LTAREH--------LQLYTRLRGISwkDEARVVKWALEKLELTKYADKPAGTYSG 2189
Cdd:PRK15112 76 -PLHFGdysYRSQRiRMIFQDpstsLNPRQRisqildfpLRLNTDLEPEQ--REKQIIETLRQVGLLPDHASYYPHMLAP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 2190 GNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL 2232
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLEL 195
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2051-2219 |
2.31e-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: 47.87 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSrkiGRILAVDRLCLGVRPGECFGLLGVNGAGKTST----FKMLtgdeSTTGGEAFVNGHSVLK-ELLQ 2125
Cdd:cd03244 3 IEFKNVSLRYRP---NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLllalFRLV----ELSSGSILIDGVDISKiGLHD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQQSLGYCPQCDALFDElTAREHLQLYTRlrgisWKDEARvvkW-ALEKLELTKYADKPAGT-----------YSGGNKR 2193
Cdd:cd03244 76 LRSRISIIPQDPVLFSG-TIRSNLDPFGE-----YSDEEL---WqALERVGLKEFVESLPGGldtvveeggenLSVGQRQ 146
|
170 180
....*....|....*....|....*.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDP 2219
Cdd:cd03244 147 LLCLARALLRKSKILVLDEATASVDP 172
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1009-1260 |
2.58e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.32 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1009 NKLSLNLYENQVVSFLGHNGAGKT-TTMSILTGL-FPP---TSGSATIYGHDI----RTEMDEIRKN-LGMCPQH----- 1073
Cdd:PRK15134 26 NDVSLQIEAGETLALVGESGSGKSvTALSILRLLpSPPvvyPSGDIRFHGESLlhasEQTLRGVRGNkIAMIFQEpmvsl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1074 NVLFdrlTVEEHLW-FYSRLKSMAQEEIRREMDKMIEDLELSNKRHSLV---QTLSGGMKRKLSVAIAFVGGSRAIILDE 1149
Cdd:PRK15134 106 NPLH---TLEKQLYeVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1150 PTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHMDEADLLGDRIAIISHGklKCC----GSPLFLKGTYGDGYRLTlvk 1223
Cdd:PRK15134 183 PTTALDVSVQAQILQLLreLQQELNMGLLFITHNLSIVRKLADRVAVMQNG--RCVeqnrAATLFSAPTHPYTQKLL--- 257
|
250 260 270
....*....|....*....|....*....|....*..
gi 45446740 1224 rPAEPGGPQEPglasSPPGRAPLSSCSELQVSQFIRK 1260
Cdd:PRK15134 258 -NSEPSGDPVP----LPEPASPLLDVEQLQVAFPIRK 289
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1982-2275 |
2.96e-05 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 49.91 E-value: 2.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1982 SPFEWDIVTrglvAMAVEGVvgfLLTIMCQYNFLRRPQRMPV---STKPVEDDVDVASERQRVLRGDADNDMVKIENLTK 2058
Cdd:TIGR01271 1153 STLQWAVNS----SIDVDGL---MRSVSRVFKFIDLPQEEPRpsgGGGKYQLSTVLVIENPHAQKCWPSGGQMDVQGLTA 1225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2059 VYKSRkiGRILAVDrLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTgGEAFVNGHSVLKELLQV-QQSLGYCPQCD 2137
Cdd:TIGR01271 1226 KYTEA--GRAVLQD-LSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTwRKAFGVIPQKV 1301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2138 ALFDElTAREHLQLYTRlrgisWKDEA--RVVKWALEKLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFI 2208
Cdd:TIGR01271 1302 FIFSG-TFRKNLDPYEQ-----WSDEEiwKVAEEVGLKSVIEQFPDKldfvlVDGGYvlSNGHKQLMCLARSILSKAKIL 1375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45446740 2209 FLDEPTTGMDPkarrFLWNLILDLIKTGRS---VVLTSHSME---ECEALctrlaIMVNG-RLRCLGSIQHLKN 2275
Cdd:TIGR01271 1376 LLDEPSAHLDP----VTLQIIRKTLKQSFSnctVILSEHRVEallECQQF-----LVIEGsSVKQYDSIQKLLN 1440
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
2062-2269 |
3.23e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 48.28 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2062 SRKIGRILavDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTG--------GEAFVNGHSVLK-ELLQVQQSLGY 2132
Cdd:PRK13547 10 ARRHRAIL--RDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLAAiDAPRLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2133 CPQCDALFDELTAREHLQL----YTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIAL------- 2201
Cdd:PRK13547 88 LPQAAQPAFAFSAREIVLLgrypHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2202 --IGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLT-SHSMEECEALCTRLAIMVNGRLRCLGS 2269
Cdd:PRK13547 168 daAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAiVHDPNLAARHADRIAMLADGAIVAHGA 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2070-2244 |
3.30e-05 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 49.01 E-value: 3.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2070 AVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSV----LKELlqvQQSLGYCPQcDA-LFDElT 2144
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIrdltLESL---RRQIGVVPQ-DTfLFSG-T 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2145 AREHLqLYTRLrGISwkDEArvVKWALEKLELTKYADK-PAG----------TYSGGNKRKLSTAIALIGYPAFIFLDEP 2213
Cdd:COG1132 430 IRENI-RYGRP-DAT--DEE--VEEAAKAAQAHEFIEAlPDGydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 45446740 2214 TTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2244
Cdd:COG1132 504 TSALDTETEALIQEALERLMK-GRTTIVIAH 533
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1008-1205 |
3.67e-05 |
|
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: 49.56 E-value: 3.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRTEMDEIRKNLGMcpQHNVLFDRLTVEEHlw 1087
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSL--RENILFGKALNEKY-- 729
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1088 FYSRLKSMAqeeirremdkMIEDLEL--SNKRHSLVQ---TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAI 1162
Cdd:TIGR00957 730 YQQVLEACA----------LLPDLEIlpSGDRTEIGEkgvNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 1163 WDLILKYK---PGRTILLSTHHMDEADLLgDRIAIISHGKLKCCGS 1205
Cdd:TIGR00957 800 FEHVIGPEgvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGS 844
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1007-1200 |
3.74e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 49.08 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1007 ALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATIYGHDIRT----EMDEIRKNLGMCPQ--HNVLFDRL 1080
Cdd:PRK10261 339 AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQdpYASLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1081 TVEEHLWFYSRLKSMAQ-EEIRREMDKMIEDLELSnKRHSL--VQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPY 1157
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLL-PEHAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 45446740 1158 ARRAIWDLILKYKP--GRTILLSTHHMDEADLLGDRIAIISHGKL 1200
Cdd:PRK10261 498 IRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMYLGQI 542
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2078-2218 |
4.76e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsVLKELlqvqqSLGYCPQcdalfdELTAREHLQLYTRLR 2156
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKT-TFaKLLAGVLKPDEGE-------VDPEL-----KISYKPQ------YIKPDYDGTVEDLLR 422
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2157 GIS-------WKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPAFIF-LDEPTTGMD 2218
Cdd:PRK13409 423 SITddlgssyYKSE------IIKPLQLERLLDKNVKDLSGGELQRVAIAACL-SRDADLYlLDEPSAHLD 485
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2051-2218 |
4.89e-05 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 48.63 E-value: 4.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKigriLAVDRlclG-VRPGECFGLLGVNGAGKTsTF-KMLTGDESTTGGEafvnghsvlkelLQVQQ 2128
Cdd:COG1245 342 VEYPDLTKSYGGFS----LEVEG---GeIREGEVLGIVGPNGIGKT-TFaKILAGVLKPDEGE------------VDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2129 SLGYCPQCDALFDELTAREHL--QLYTRLRGISWKDEarvvkwALEKLELTKYADKPAGTYSGGNKRKLSTAIALiGYPA 2206
Cdd:COG1245 402 KISYKPQYISPDYDGTVEEFLrsANTDDFGSSYYKTE------IIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDA 474
|
170
....*....|...
gi 45446740 2207 FIF-LDEPTTGMD 2218
Cdd:COG1245 475 DLYlLDEPSAHLD 487
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2051-2248 |
7.20e-05 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 46.95 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLT------GDESTTGGEAFVNGHSVLKEL- 2123
Cdd:PRK14258 8 IKVNNLSFYYDTQKI-----LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNrmneleSEVRVEGRVEFFNQNIYERRVn 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2124 ---LQVQQSLGYcPQCDaLFdELTAREHLQLYTRLrgISWKDEAR---VVKWALEKLEL----TKYADKPAGTYSGGNKR 2193
Cdd:PRK14258 83 lnrLRRQVSMVH-PKPN-LF-PMSVYDNVAYGVKI--VGWRPKLEiddIVESALKDADLwdeiKHKIHKSALDLSGGQQQ 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDL-IKTGRSVVLTSHSMEE 2248
Cdd:PRK14258 158 RLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLrLRSELTMVIVSHNLHQ 213
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2060-2248 |
8.37e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 8.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2060 YKSRKIgrilaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESttggEAFVNgHSVL--------KELLQVQQSLG 2131
Cdd:PRK10938 270 YNDRPI-----LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHP----QGYSN-DLTLfgrrrgsgETIWDIKKHIG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2132 YcpqcdalfdeLTAREHL--QLYTRLR-----------GI----SWKDEARVVKWaLEKLELTKY-ADKPAGTYSGGNKR 2193
Cdd:PRK10938 340 Y----------VSSSLHLdyRVSTSVRnvilsgffdsiGIyqavSDRQQKLAQQW-LDILGIDKRtADAPFHSLSWGQQR 408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVL-TSHSMEE 2248
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLfVSHHAED 464
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1008-1200 |
8.62e-05 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 46.56 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1008 LNKLSLNLYENQVVSFLGHNGAGKTTTMSILTG--LFPPTSGSATIYGHDIRTEMDEIRKNLG--MCPQH--------NV 1075
Cdd:CHL00131 23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGifLAFQYpieipgvsNA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1076 LFDRLTveehlwFYSRLKSMAQEEIrremdKMIEDLELSNKRHSLV------------QTLSGGMKRK---LSVAIAfvg 1140
Cdd:CHL00131 103 DFLRLA------YNSKRKFQGLPEL-----DPLEFLEIINEKLKLVgmdpsflsrnvnEGFSGGEKKRneiLQMALL--- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 1141 GSRAIILDEPTAGVDPYARRAIWDLILKYK-PGRTILLSTHHMDEAD-LLGDRIAIISHGKL 1200
Cdd:CHL00131 169 DSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHYQRLLDyIKPDYVHVMQNGKI 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1003-1155 |
9.37e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.78 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1003 DKKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPpTSGSATIYGHDI----RTEMDEIRKNLGMCPQ--HNVL 1076
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLhnlnRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1077 FDRLTV----EEHLWFYSRLKSMAQEEIR--REMDKMIEDLELsnkRHSLVQTLSGGMKRKLSVAIAFVGGSRAIILDEP 1150
Cdd:PRK15134 376 NPRLNVlqiiEEGLRVHQPTLSAAQREQQviAVMEEVGLDPET---RHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
....*
gi 45446740 1151 TAGVD 1155
Cdd:PRK15134 453 TSSLD 457
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
2079-2244 |
9.50e-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: 9.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2079 RPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEaFVNGHS---VLK-----ELLQVQQSL-------GYCPQ-CDALFDE 2142
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGD-YDEEPSwdeVLKrfrgtELQDYFKKLangeikvAHKPQyVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2143 L--TAREHLQLYtrlrgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2220
Cdd:COG1245 176 FkgTVRELLEKV---------DERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
170 180
....*....|....*....|....
gi 45446740 2221 ARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:COG1245 247 QRLNVARLIRELAEEGKYVLVVEH 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2081-2356 |
1.02e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2081 GECFGLLGVNGAGKTSTFKMLT---------------------GDeSTTGGEAFVNGHSVLKELLQVQQSL--------- 2130
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAmhaidgipkncqilhveqevvGD-DTTALQCVLNTDIERTQLLEEEAQLvaqqrelef 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2131 ------GYCPQCDALFDELTAREHLQLYTRLRGI-SWKDEARVVKwALEKLELT-KYADKPAGTYSGGNKRKLSTAIALI 2202
Cdd:PLN03073 282 etetgkGKGANKDGVDKDAVSQRLEEIYKRLELIdAYTAEARAAS-ILAGLSFTpEMQVKATKTFSGGWRMRIALARALF 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2203 GYPAFIFLDEPTTGMDPKArrFLWnLILDLIKTGRSVVLTSHSMEECEALCTrlaimvngrlrclgSIQHLKNR----FG 2278
Cdd:PLN03073 361 IEPDLLLLDEPTNHLDLHA--VLW-LETYLLKWPKTFIVVSHAREFLNTVVT--------------DILHLHGQklvtYK 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2279 DGYMITVRTKSSQsVKDVVRFFnrnfpEAMLKERHHTKV---QYQLKSEHISLAQ----VFSKMEQVSGVLGIEDYSVSQ 2351
Cdd:PLN03073 424 GDYDTFERTREEQ-LKNQQKAF-----ESNERSRSHMQAfidKFRYNAKRASLVQsrikALDRLGHVDAVVNDPDYKFEF 497
|
....*
gi 45446740 2352 TTLDN 2356
Cdd:PLN03073 498 PTPDD 502
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
989-1051 |
1.29e-04 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 47.04 E-value: 1.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 989 LVVCVDKLTKVYKDdkKLALNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGSATI 1051
Cdd:PRK11819 323 KVIEAENLSKSFGD--RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2051-2244 |
1.66e-04 |
|
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: 45.68 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTKVYKSRKIgriLAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQS 2129
Cdd:cd03251 1 VEFKNVTFRYPGDGP---PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFDElTAREHLqLYTRLRGiswkDEARVVKwALEKLELTKYADK-PAG----------TYSGGNKRKLSTA 2198
Cdd:cd03251 78 IGLVSQDVFLFND-TVAENI-AYGRPGA----TREEVEE-AARAANAHEFIMElPEGydtvigergvKLSGGQRQRIAIA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 2199 IALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKtGRSVVLTSH 2244
Cdd:cd03251 151 RALLKDPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAH 195
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
2205-2309 |
1.69e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.53 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHSMEecealctrLAIMVNgrlrcLGSIQHLKNRFGDGYMIT 2284
Cdd:COG3593 188 NPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPH--------LLSEVP-----LENIRRLRRDSGGTTSTK 254
|
90 100
....*....|....*....|....*
gi 45446740 2285 VRTKSSQSVKDVVRFFNRNFPEAML 2309
Cdd:COG3593 255 LIDLDDEDLRKLLRYLGVTRSELLF 279
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2051-2247 |
1.87e-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: 44.45 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2051 VKIENLTkvYKSRKiGRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGD-ESTTGgeafvnghsvlkellqvqqS 2129
Cdd:cd03223 1 IELENLS--LATPD-GRVL-LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLwPWGSG-------------------R 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2130 LGYCPQCDALFdeLTAREHLQLYTrLRGIS---WKDEarvvkwalekleltkyadkpagtYSGGNKRKLSTAIALIGYPA 2206
Cdd:cd03223 58 IGMPEGEDLLF--LPQRPYLPLGT-LREQLiypWDDV-----------------------LSGGEQQRLAFARLLLHKPK 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 45446740 2207 FIFLDEPTTGMDPKARRFLWNLILD----LIKTGRSVVLTS-HSME 2247
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKElgitVISVGHRPSLWKfHDRV 157
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2066-2273 |
2.28e-04 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 45.55 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2066 GRILaVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGhsvlkELLQVQQS------LGYCPQCDAL 2139
Cdd:PRK10575 23 GRTL-LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDA-----QPLESWSSkafarkVAYLPQQLPA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2140 FDELTAREHLQL-----YTRLRGISWKDEARVVKwALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPT 2214
Cdd:PRK10575 97 AEGMTVRELVAIgrypwHGALGRFGAADREKVEE-AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPT 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2215 TGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQHL 2273
Cdd:PRK10575 176 SALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1011-1180 |
2.81e-04 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 45.94 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1011 LSLNLYENQVVsFL-GHNGAGKTTTMSILTGLFPPTSGSATIYGHDI-RTEMDEIRknlgmcpQH-------NVLFDRLT 1081
Cdd:COG4615 351 IDLTIRRGELV-FIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYR-------QLfsavfsdFHLFDRLL 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1082 VEEhlwfysrlksmaQEEIRREMDKMIEDLELSNK------RHSLVQtLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:COG4615 423 GLD------------GEADPARARELLERLELDHKvsvedgRFSTTD-LSQGQRKRLALLVALLEDRPILVFDEWAADQD 489
|
170 180 190
....*....|....*....|....*....|
gi 45446740 1156 PYARRAIWDLILkykP-----GRTILLSTH 1180
Cdd:COG4615 490 PEFRRVFYTELL---PelkarGKTVIAISH 516
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
2181-2245 |
3.54e-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: 43.85 E-value: 3.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45446740 2181 DKPAGTYSGGNKR--KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSHS 2245
Cdd:cd03238 82 GQKLSTLSGGELQrvKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
1021-1210 |
4.90e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1021 VSFLGHNGAGKTTTMSILTGLFPPTSGSATIyghdirtemdeIRKNLGMCPQHNVLFDRlTVEEHLWFYSRLKSmaqEEI 1100
Cdd:PLN03130 646 VAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TVRDNILFGSPFDP---ERY 710
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1101 RREMD--KMIEDLELSnKRHSLVQ------TLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLILKYK-P 1171
Cdd:PLN03130 711 ERAIDvtALQHDLDLL-PGGDLTEigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDElR 789
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 45446740 1172 GRTILLST---HHMDEAdllgDRIAIISHGKLK--------CCGSPLFLK 1210
Cdd:PLN03130 790 GKTRVLVTnqlHFLSQV----DRIILVHEGMIKeegtyeelSNNGPLFQK 835
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2071-2275 |
5.02e-04 |
|
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: 44.46 E-value: 5.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2071 VDRLCLGVRPGECFGLLGVNGAGKTSTF----KMLtgdesTTGGEAFVNGHSVLKELLQV-QQSLGYCPQCDALFDElTA 2145
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLsaflRLL-----NTEGDIQIDGVSWNSVPLQKwRKAFGVIPQKVFIFSG-TF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2146 REHLQLYTRlrgisWKDEA--RVVKWALEKLELTKYADK-----PAGTY--SGGNKRKLSTAIALIGYPAFIFLDEPTTG 2216
Cdd:cd03289 94 RKNLDPYGK-----WSDEEiwKVAEEVGLKSVIEQFPGQldfvlVDGGCvlSHGHKQLMCLARSVLSKAKILLLDEPSAH 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45446740 2217 MDPKARRFLwNLILDLIKTGRSVVLTSHSMeecEAL--CTRLAIMVNGRLRCLGSIQHLKN 2275
Cdd:cd03289 169 LDPITYQVI-RKTLKQAFADCTVILSEHRI---EAMleCQRFLVIEENKVRQYDSIQKLLN 225
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
1024-1155 |
5.15e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 45.48 E-value: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1024 LGHNGAGKTTTMSILTGL---FPPTSGSATIY-GHDIRTEMDEIRKNLGMCPQHNVLFDRLTVEEHLWFYSRLKSMA--- 1096
Cdd:TIGR00956 93 LGRPGSGCSTLLKTIASNtdgFHIGVEGVITYdGITPEEIKKHYRGDVVYNAETDVHFPHLTVGETLDFAARCKTPQnrp 172
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1097 -----QEEIRREMDKMIEDLELSNKRHS-----LVQTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVD 1155
Cdd:TIGR00956 173 dgvsrEEYAKHIADVYMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2074-2287 |
5.71e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.35 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2074 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK-ELLQVQQSLGYCPQCDALF--------DELT 2144
Cdd:PLN03232 1255 LSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFsgtvrfniDPFS 1334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2145 AREHLQLYTRLRGISWKDEARVVKWALEKlELTKYADkpagTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRF 2224
Cdd:PLN03232 1335 EHNDADLWEALERAHIKDVIDRNPFGLDA-EVSEGGE----NFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45446740 2225 LWNLILDLIKTGrSVVLTSHSMEECeALCTRLAIMVNGRLRCLGSIQHLKNRFGDGYMITVRT 2287
Cdd:PLN03232 1410 IQRTIREEFKSC-TMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHS 1470
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
2188-2244 |
6.47e-04 |
|
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: 42.73 E-value: 6.47e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45446740 2188 SGGNKRKLSTAIAL-----IGYPaFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:cd03227 79 SGGEKELSALALILalaslKPRP-LYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITH 139
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2050-2244 |
6.60e-04 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 45.10 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2050 MVKIENLTKVYKSRKiGRILAVDRLCLGVRPGECFGLLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLK----ELLQ 2125
Cdd:PRK10535 4 LLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2126 VQ-QSLGYCPQCDALFDELTAREHLQLYTRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGY 2204
Cdd:PRK10535 83 LRrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 45446740 2205 PAFIFLDEPTTGMDPKARRFLWNLILDLIKTGRSVVLTSH 2244
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTH 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2046-2231 |
6.86e-04 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 44.80 E-value: 6.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2046 ADNDMVKIENLTkVYKSRkiGRILaVDRLCLGVRPGEcfGLL--GVNGAGKTSTFKMLTG-DESTTGgeafvnghsvlke 2122
Cdd:COG4178 358 SEDGALALEDLT-LRTPD--GRPL-LEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGlWPYGSG------------- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2123 llqvqqSLGYCPQCDALFdeLTAREHLQLYTrLRGI--------SWKDEArvVKWALEKLELTKYADKP------AGTYS 2188
Cdd:COG4178 419 ------RIARPAGARVLF--LPQRPYLPLGT-LREAllypataeAFSDAE--LREALEAVGLGHLAERLdeeadwDQVLS 487
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 45446740 2189 GGNKRKLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILD 2231
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE 530
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
2086-2270 |
8.14e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 44.09 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2086 LLGVNGAGKTSTFKMLTGDESTTGGEAFVNGHSVLKELLQV-----QQSLGYCPQcDA-LFDELTAREHLQlYtrlrGIS 2159
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppeKRRIGYVFQ-DArLFPHYKVRGNLR-Y----GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2160 WKDEA---RVVKW-ALEKLeLTKYadkPAgTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMD-PKARR---FLWNLILD 2231
Cdd:PRK11144 103 KSMVAqfdKIVALlGIEPL-LDRY---PG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKREllpYLERLARE 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 45446740 2232 lIKTgrSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSI 2270
Cdd:PRK11144 178 -INI--PILYVSHSLDEILRLADRVVVLEQGKVKAFGPL 213
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
2078-2244 |
1.70e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2078 VRPGECFGLLGVNGAGKTSTFKMLTG--------DESTTGGEAFVN---G---HSVLKELLQVQQSLGYCPQ-CDALFDE 2142
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGelipnlgdYEEEPSWDEVLKrfrGtelQNYFKKLYNGEIKVVHKPQyVDLIPKV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2143 L--TAREHLQLYtrlrgiswkDEARVVKWALEKLELTKYADKPAGTYSGGNKRKLSTAIALIGYPAFIFLDEPTTGMDPK 2220
Cdd:PRK13409 176 FkgKVRELLKKV---------DERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
170 180
....*....|....*....|....
gi 45446740 2221 ARRFLWNLILDLIKtGRSVVLTSH 2244
Cdd:PRK13409 247 QRLNVARLIRELAE-GKYVLVVEH 269
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
2084-2259 |
2.61e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.49 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2084 FGLLGVNGAGKTSTFKMLT----GDesTTGGEAFVNGHSVLKellqvqqslgycPQCDALFDELTAREHLQLY--TRLRG 2157
Cdd:cd03279 31 FLICGPTGAGKSTILDAITyalyGK--TPRYGRQENLRSVFA------------PGEDTAEVSFTFQLGGKKYrvERSRG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2158 ISWKDEARVVkwALEKLELTKYADKPAGTYSGGNKRKLSTAIAL---------IGYP-AFIFLDEPTTGMDPKARRFLWN 2227
Cdd:cd03279 97 LDYDQFTRIV--LLPQGEFDRFLARPVSTLSGGETFLASLSLALalsevlqnrGGARlEALFIDEGFGTLDPEALEAVAT 174
|
170 180 190
....*....|....*....|....*....|...
gi 45446740 2228 lILDLIKT-GRSVVLTSHSMEECEALCTRLAIM 2259
Cdd:cd03279 175 -ALELIRTeNRMVGVISHVEELKERIPQRLEVI 206
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
2074-2244 |
2.62e-03 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 41.84 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2074 LCLGVRPGECFGLLGVNGAGKTSTFKMLTGdeSTTG-GEAFVNGHSvLKELLQVQQSL--GY-CPQCDALFdELTAREHL 2149
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG--LLPGsGSIQFAGQP-LEAWSAAELARhrAYlSQQQTPPF-AMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2150 QLYtRLRGISWKDEARVVKWALEKLELTKYADKPAGTYSGGN-KRKLSTAIALIGYPA------FIFLDEPTTGMDPKAR 2222
Cdd:PRK03695 91 TLH-QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwQRVRLAAVVLQVWPDinpagqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|..
gi 45446740 2223 RFLWNLILDLIKTGRSVVLTSH 2244
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSH 191
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
1046-1182 |
2.65e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 43.48 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 1046 SGSATIYGHDI-RTEMDEIRKNLGMCPQHNVLFDrLTVEEHLWFYSrlKSMAQEEIRR-----EMDKMIEdlELSNKRHS 1119
Cdd:PTZ00265 1276 SGKILLDGVDIcDYNLKDLRNLFSIVSQEPMLFN-MSIYENIKFGK--EDATREDVKRackfaAIDEFIE--SLPNKYDT 1350
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45446740 1120 LV----QTLSGGMKRKLSVAIAFVGGSRAIILDEPTAGVDPYARRAIWDLI--LKYKPGRTILLSTHHM 1182
Cdd:PTZ00265 1351 NVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdIKDKADKTIITIAHRI 1419
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
2194-2276 |
7.22e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 41.04 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 2194 KLSTAIALIGYPAFIFLDEPTTGMDPKARRFLWNLILDLIKT-GRSVVLTSHSMEECEALCTRLAIMVNGRLRCLGSIQH 2272
Cdd:COG4170 166 KVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLqGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQ 245
|
....
gi 45446740 2273 LKNR 2276
Cdd:COG4170 246 ILKS 249
|
|
| MelB |
COG2211 |
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism]; |
707-832 |
7.58e-03 |
|
Na+/melibiose symporter or related transporter [Carbohydrate transport and metabolism];
Pssm-ID: 441813 [Multi-domain] Cd Length: 447 Bit Score: 41.43 E-value: 7.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45446740 707 MMPLCMVISWVYSVAMTIQHIVAEKEH-RLKEVMKTMgLNNAVHWVAWFITGFVQLSISVTAlTAILKYGQVLMHSHVVI 785
Cdd:COG2211 188 IFAVLGLLAFLLTFFGTKERPVPEEEKvSLKESLKAL-LKNRPFLLLLLAYLLFFLALALVA-ALLLYYFKYVLGLSAAL 265
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 45446740 786 IWLFLAVYAVATIMFCFLVSVL---YSKAKLASAcGGIIYFLSYVPYMYV 832
Cdd:COG2211 266 VGLLLALYFLAALLGAPLWPRLakrFGKKKAFII-GLLLAALGLLLLFFL 314
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
973-1048 |
8.01e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.42 E-value: 8.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45446740 973 RFEETRGMEEepthlpLVVCVDKLTKVYkDDKKLaLNKLSLNLYENQVVSFLGHNGAGKTTTMSILTGLFPPTSGS 1048
Cdd:PRK15064 308 RFEQDKKLHR------NALEVENLTKGF-DNGPL-FKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT 375
|
|
| |
